HAUS6_HUMAN
ID HAUS6_HUMAN Reviewed; 955 AA.
AC Q7Z4H7; B3KPK4; B4DX82; Q05CG1; Q14CB6; Q14CD9; Q2TA91; Q6IQ10; Q6NZX5;
AC Q8IZQ4; Q96FN0; Q9H950; Q9H998; Q9HCJ8; Q9NXT8;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=HAUS augmin-like complex subunit 6;
GN Name=HAUS6; Synonyms=DGT6, FAM29A, KIAA1574;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Ding P., Han W., Wang L., Wang Y., Qiu X., Xu M., Ma D.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Guo J.H., Chen L., Yu L.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 288-955 (ISOFORM 3), AND VARIANT GLN-674.
RC TISSUE=Colon, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 251-955 (ISOFORM 2), AND VARIANT ILE-761.
RC TISSUE=Duodenum, Eye, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-955 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [7]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=18443220; DOI=10.1083/jcb.200711053;
RA Goshima G., Mayer M., Zhang N., Stuurman N., Vale R.D.;
RT "Augmin: a protein complex required for centrosome-independent microtubule
RT generation within the spindle.";
RL J. Cell Biol. 181:421-429(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP FUNCTION, INTERACTION WITH PLK1; GAMMA-TUBULIN AND NEDD1, PHOSPHORYLATION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=19029337; DOI=10.1083/jcb.200807046;
RA Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G.;
RT "FAM29A promotes microtubule amplification via recruitment of the NEDD1-
RT gamma-tubulin complex to the mitotic spindle.";
RL J. Cell Biol. 183:835-848(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-584 AND SER-805, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-552; THR-584 AND
RP SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19427217; DOI=10.1016/j.cub.2009.04.033;
RA Lawo S., Bashkurov M., Mullin M., Ferreria M.G., Kittler R., Habermann B.,
RA Tagliaferro A., Poser I., Hutchins J.R.A., Hegemann B., Pinchev D.,
RA Buchholz F., Peters J.-M., Hyman A.A., Gingras A.-C., Pelletier L.;
RT "HAUS, the 8-subunit human augmin complex, regulates centrosome and spindle
RT integrity.";
RL Curr. Biol. 19:816-826(2009).
RN [15]
RP IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19369198; DOI=10.1073/pnas.0901587106;
RA Uehara R., Nozawa R.-S., Tomioka A., Petry S., Vale R.D., Obuse C.,
RA Goshima G.;
RT "The augmin complex plays a critical role in spindle microtubule generation
RT for mitotic progression and cytokinesis in human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6998-7003(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-552, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-552 AND THR-584, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-524; SER-530;
RP SER-550; SER-552; THR-584; SER-715; SER-728; SER-742; SER-805; THR-823;
RP SER-908; SER-914 AND SER-943, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP INTERACTION WITH EML3, AND SUBCELLULAR LOCATION.
RX PubMed=30723163; DOI=10.1074/jbc.ra118.007164;
RA Luo J., Yang B., Xin G., Sun M., Zhang B., Guo X., Jiang Q., Zhang C.;
RT "The microtubule-associated protein EML3 regulates mitotic spindle assembly
RT by recruiting the Augmin complex to spindle microtubules.";
RL J. Biol. Chem. 294:5643-5656(2019).
CC -!- FUNCTION: Contributes to mitotic spindle assembly, maintenance of
CC centrosome integrity and completion of cytokinesis as part of the HAUS
CC augmin-like complex. Promotes the nucleation of microtubules from the
CC spindle through recruitment of NEDD1 and gamma-tubulin.
CC {ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217}.
CC -!- SUBUNIT: Component of the HAUS augmin-like complex. The complex
CC interacts with the gamma-tubulin ring complex and this interaction is
CC required for spindle assembly (PubMed:19369198, PubMed:19427217).
CC Interacts with PLK1, NEDD1 and gamma-tubulin (PubMed:19029337).
CC Interacts with EML3 (phosphorylated at 'Thr-881') (PubMed:30723163).
CC {ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
CC -!- INTERACTION:
CC Q7Z4H7; Q96CS2: HAUS1; NbExp=11; IntAct=EBI-2558196, EBI-2514791;
CC Q7Z4H7; Q9NVX0: HAUS2; NbExp=10; IntAct=EBI-2558196, EBI-720080;
CC Q7Z4H7; Q68CZ6: HAUS3; NbExp=4; IntAct=EBI-2558196, EBI-2558217;
CC Q7Z4H7; Q9H6D7: HAUS4; NbExp=3; IntAct=EBI-2558196, EBI-2558168;
CC Q7Z4H7; O94927: HAUS5; NbExp=3; IntAct=EBI-2558196, EBI-2558224;
CC Q7Z4H7; Q99871: HAUS7; NbExp=3; IntAct=EBI-2558196, EBI-395719;
CC Q7Z4H7; Q9BT25: HAUS8; NbExp=9; IntAct=EBI-2558196, EBI-2558143;
CC Q7Z4H7; Q8NHV4: NEDD1; NbExp=2; IntAct=EBI-2558196, EBI-2555055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18443220, ECO:0000269|PubMed:19029337}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:19029337,
CC ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217,
CC ECO:0000269|PubMed:30723163}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217}. Note=Localizes to interphase centrosomes
CC and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z4H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4H7-2; Sequence=VSP_017017, VSP_017018;
CC Name=3;
CC IsoId=Q7Z4H7-3; Sequence=VSP_040919;
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:19029337}.
CC -!- SIMILARITY: Belongs to the HAUS6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26178.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI11042.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90922.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14334.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14388.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG63294.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF533709; AAQ09022.1; -; mRNA.
DR EMBL; AF537091; AAN05700.1; -; mRNA.
DR EMBL; AK000067; BAA90922.1; ALT_INIT; mRNA.
DR EMBL; AK022964; BAB14334.1; ALT_INIT; mRNA.
DR EMBL; AK023068; BAB14388.1; ALT_INIT; mRNA.
DR EMBL; AK301852; BAG63294.1; ALT_INIT; mRNA.
DR EMBL; AK056458; BAG51716.1; -; mRNA.
DR EMBL; AL356000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010632; AAH10632.1; -; mRNA.
DR EMBL; BC026178; AAH26178.1; ALT_SEQ; mRNA.
DR EMBL; BC065935; AAH65935.1; -; mRNA.
DR EMBL; BC071625; AAH71625.1; -; mRNA.
DR EMBL; BC111041; AAI11042.1; ALT_INIT; mRNA.
DR EMBL; BC113981; AAI13982.1; -; mRNA.
DR EMBL; BC114492; AAI14493.1; -; mRNA.
DR EMBL; AB046794; BAB13400.1; -; mRNA.
DR CCDS; CCDS6489.1; -. [Q7Z4H7-1]
DR RefSeq; NP_001257819.1; NM_001270890.1. [Q7Z4H7-3]
DR RefSeq; NP_060115.3; NM_017645.4. [Q7Z4H7-1]
DR AlphaFoldDB; Q7Z4H7; -.
DR SMR; Q7Z4H7; -.
DR BioGRID; 120160; 173.
DR ComplexPortal; CPX-1847; HAUS complex.
DR CORUM; Q7Z4H7; -.
DR DIP; DIP-48830N; -.
DR IntAct; Q7Z4H7; 83.
DR MINT; Q7Z4H7; -.
DR STRING; 9606.ENSP00000369871; -.
DR GlyGen; Q7Z4H7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z4H7; -.
DR MetOSite; Q7Z4H7; -.
DR PhosphoSitePlus; Q7Z4H7; -.
DR SwissPalm; Q7Z4H7; -.
DR BioMuta; HAUS6; -.
DR DMDM; 85700957; -.
DR EPD; Q7Z4H7; -.
DR jPOST; Q7Z4H7; -.
DR MassIVE; Q7Z4H7; -.
DR MaxQB; Q7Z4H7; -.
DR PaxDb; Q7Z4H7; -.
DR PeptideAtlas; Q7Z4H7; -.
DR PRIDE; Q7Z4H7; -.
DR ProteomicsDB; 69184; -. [Q7Z4H7-1]
DR ProteomicsDB; 69185; -. [Q7Z4H7-2]
DR ProteomicsDB; 69186; -. [Q7Z4H7-3]
DR Antibodypedia; 10241; 117 antibodies from 24 providers.
DR DNASU; 54801; -.
DR Ensembl; ENST00000380502.8; ENSP00000369871.3; ENSG00000147874.11. [Q7Z4H7-1]
DR GeneID; 54801; -.
DR KEGG; hsa:54801; -.
DR MANE-Select; ENST00000380502.8; ENSP00000369871.3; NM_017645.5; NP_060115.3.
DR UCSC; uc003znk.5; human. [Q7Z4H7-1]
DR CTD; 54801; -.
DR DisGeNET; 54801; -.
DR GeneCards; HAUS6; -.
DR HGNC; HGNC:25948; HAUS6.
DR HPA; ENSG00000147874; Low tissue specificity.
DR MIM; 613433; gene.
DR neXtProt; NX_Q7Z4H7; -.
DR OpenTargets; ENSG00000147874; -.
DR PharmGKB; PA165585815; -.
DR VEuPathDB; HostDB:ENSG00000147874; -.
DR eggNOG; ENOG502QV4W; Eukaryota.
DR GeneTree; ENSGT00390000008250; -.
DR HOGENOM; CLU_311438_0_0_1; -.
DR InParanoid; Q7Z4H7; -.
DR OMA; MDFGILH; -.
DR OrthoDB; 297770at2759; -.
DR PhylomeDB; Q7Z4H7; -.
DR TreeFam; TF325931; -.
DR PathwayCommons; Q7Z4H7; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q7Z4H7; -.
DR SIGNOR; Q7Z4H7; -.
DR BioGRID-ORCS; 54801; 671 hits in 1052 CRISPR screens.
DR ChiTaRS; HAUS6; human.
DR GeneWiki; FAM29A; -.
DR GenomeRNAi; 54801; -.
DR Pharos; Q7Z4H7; Tbio.
DR PRO; PR:Q7Z4H7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q7Z4H7; protein.
DR Bgee; ENSG00000147874; Expressed in ganglionic eminence and 172 other tissues.
DR ExpressionAtlas; Q7Z4H7; baseline and differential.
DR Genevisible; Q7Z4H7; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070652; C:HAUS complex; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR InterPro; IPR026797; HAUS_6.
DR InterPro; IPR028163; HAUS_6_N.
DR PANTHER; PTHR16151; PTHR16151; 1.
DR Pfam; PF14661; HAUS6_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..955
FT /note="HAUS augmin-like complex subunit 6"
FT /id="PRO_0000076217"
FT REGION 474..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 188..219
FT /evidence="ECO:0000255"
FT COMPBIAS 477..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 584
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 823
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 355..389
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040919"
FT VAR_SEQ 589..606
FT /note="ITEIRSSWRKAIEMEENR -> SKLIMLSVTFFFHRHNHC (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017017"
FT VAR_SEQ 607..955
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017018"
FT VARIANT 552
FT /note="S -> T (in dbSNP:rs41269003)"
FT /id="VAR_062243"
FT VARIANT 674
FT /note="H -> Q (in dbSNP:rs10511670)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_024926"
FT VARIANT 761
FT /note="S -> I (in dbSNP:rs4977493)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024927"
FT CONFLICT 82
FT /note="D -> E (in Ref. 1; AAQ09022)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="Missing (in Ref. 4; AAI11042)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Y -> H (in Ref. 3; BAG63294)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="R -> G (in Ref. 3; BAB14334)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="S -> L (in Ref. 3; BAB14388)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="A -> V (in Ref. 5; AAH10632/AAI14493)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="L -> M (in Ref. 3; BAB14388)"
FT /evidence="ECO:0000305"
FT CONFLICT 936..938
FT /note="EED -> GKV (in Ref. 3; BAB14334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 955 AA; 108621 MW; 8EA52C24BA818C00 CRC64;
MSSASVTAFE KEHLWMYLQA LGFEPGPATI ACGKIVSHTH LGVNMFDKLN RDAFHIISYF
LFQVLDQSLT KEVFKFCWPP FDQKSDTEFR KHCCEWIKRI SGECGSSFPQ VVGSLFLSPG
GPKFIHLMYH FARFVAMKYI KSNSKNSSHH FVETFNIKPQ DLHKCIARCH FARSRFLQIL
QRQDCVTQKY QENAQLSVKQ VRNLRSECIG LENQIKKMEP YDDHSNMEEK IQKVRSLWAS
VNETLMFLEK EREVVSSVLS LVNQYALDGT NVAINIPRLL LDKIEKQMFQ LHIGNVYEAG
KLNLLTVIQL LNEVLKVMKY ERCQADQARL TVDLHYLEKE TKFQKERLSD LKHMRYRIKD
DLTTIRHSVV EKQGEWHKKW KEFLGLSPFS LIKGWTPSVD LLPPMSPLSF DPASEEVYAK
SILCQYPASL PDAHKQHNQE NGCRGDSDTL GALHDLANSP ASFLSQSVSS SDRNSVTVLE
KDTKMGTPKE KNEAISKKIP EFEVENSPLS DVAKNTESSA FGGSLPAKKS DPFQKEQDHL
VEEVARAVLS DSPQLSEGKE IKLEELIDSL GSNPFLTRNQ IPRTPENLIT EIRSSWRKAI
EMEENRTKEP IQMDAEHREV LPESLPVLHN QREFSMADFL LETTVSDFGQ SHLTEEKVIS
DCECVPQKHV LTSHIDEPPT QNQSDLLNKK VICKQDLECL AFTKLSETSR METFSPAVGN
RIDVMGGSEE EFMKILDHLE VSCNKPSTNK TMLWNSFQIS SGISSKSFKD NDFGILHETL
PEEVGHLSFN SSSSSEANFK LEPNSPMHGG TLLEDVVGGR QTTPESDFNL QALRSRYEAL
KKSLSKKREE SYLSNSQTPE RHKPELSPTP QNVQTDDTLN FLDTCDLHTE HIKPSLRTSI
GERKRSLSPL IKFSPVEQRL RTTIACSLGE LPNLKEEDIL NKSLDAKEPP SDLTR
