HAUS1_HUMAN
ID HAUS1_HUMAN Reviewed; 278 AA.
AC Q96CS2; B2RDM7; Q8N837;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=HAUS augmin-like complex subunit 1;
DE AltName: Full=Coiled-coil domain-containing protein 5;
DE AltName: Full=Enhancer of invasion-cluster;
DE Short=HEI-C;
GN Name=HAUS1; Synonyms=CCDC5, HEIC;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH MICROTUBULES.
RC TISSUE=Cervix carcinoma;
RX PubMed=15082789; DOI=10.1128/mcb.24.9.3957-3971.2004;
RA Einarson M.B., Cukierman E., Compton D.A., Golemis E.A.;
RT "Human enhancer of invasion-cluster, a coiled-coil protein required for
RT passage through mitosis.";
RL Mol. Cell. Biol. 24:3957-3971(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Choriocarcinoma, and Chronic myeloid leukemia cell;
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 [4]
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 [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
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. {ECO:0000269|PubMed:15082789,
CC ECO:0000269|PubMed:19369198, 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. Associates with microtubules. The
CC interaction with microtubules is strong during mitosis, while it is
CC weak or absent during interphase. It is unclear whether this
CC interaction is direct or indirect. Interacts with EML3 (phosphorylated
CC at 'Thr-881') (PubMed:30723163). {ECO:0000269|PubMed:15082789,
CC ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217,
CC ECO:0000269|PubMed:30723163}.
CC -!- INTERACTION:
CC Q96CS2; Q96MA6: AK8; NbExp=3; IntAct=EBI-2514791, EBI-8466265;
CC Q96CS2; P53365: ARFIP2; NbExp=3; IntAct=EBI-2514791, EBI-638194;
CC Q96CS2; Q9Y5K8: ATP6V1D; NbExp=3; IntAct=EBI-2514791, EBI-2684998;
CC Q96CS2; P46379-2: BAG6; NbExp=3; IntAct=EBI-2514791, EBI-10988864;
CC Q96CS2; Q13515: BFSP2; NbExp=5; IntAct=EBI-2514791, EBI-10229433;
CC Q96CS2; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-2514791, EBI-465781;
CC Q96CS2; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-2514791, EBI-10193358;
CC Q96CS2; Q6ZUJ4: C3orf62; NbExp=4; IntAct=EBI-2514791, EBI-2837036;
CC Q96CS2; Q8TC20: CAGE1; NbExp=3; IntAct=EBI-2514791, EBI-10196469;
CC Q96CS2; Q8NA61: CBY2; NbExp=3; IntAct=EBI-2514791, EBI-741724;
CC Q96CS2; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-2514791, EBI-10171416;
CC Q96CS2; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-2514791, EBI-2808286;
CC Q96CS2; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-2514791, EBI-10175300;
CC Q96CS2; Q01850: CDR2; NbExp=3; IntAct=EBI-2514791, EBI-1181367;
CC Q96CS2; Q6IPU0: CENPP; NbExp=5; IntAct=EBI-2514791, EBI-10250303;
CC Q96CS2; Q96L14: CEP170P1; NbExp=3; IntAct=EBI-2514791, EBI-743488;
CC Q96CS2; Q9C0F1: CEP44; NbExp=4; IntAct=EBI-2514791, EBI-744115;
CC Q96CS2; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-2514791, EBI-747776;
CC Q96CS2; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-2514791, EBI-10181988;
CC Q96CS2; Q96MT8: CEP63; NbExp=4; IntAct=EBI-2514791, EBI-741977;
CC Q96CS2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2514791, EBI-739624;
CC Q96CS2; Q6IAZ5: CRSP9; NbExp=3; IntAct=EBI-2514791, EBI-10283772;
CC Q96CS2; Q13561: DCTN2; NbExp=3; IntAct=EBI-2514791, EBI-715074;
CC Q96CS2; P11532: DMD; NbExp=4; IntAct=EBI-2514791, EBI-295827;
CC Q96CS2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-2514791, EBI-12593112;
CC Q96CS2; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-2514791, EBI-465804;
CC Q96CS2; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-2514791, EBI-7225287;
CC Q96CS2; Q9NVK5: FGFR1OP2; NbExp=3; IntAct=EBI-2514791, EBI-1104764;
CC Q96CS2; P22607: FGFR3; NbExp=3; IntAct=EBI-2514791, EBI-348399;
CC Q96CS2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2514791, EBI-618309;
CC Q96CS2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-2514791, EBI-8285963;
CC Q96CS2; P06396: GSN; NbExp=3; IntAct=EBI-2514791, EBI-351506;
CC Q96CS2; Q9H6D7: HAUS4; NbExp=11; IntAct=EBI-2514791, EBI-2558168;
CC Q96CS2; Q7Z4H7: HAUS6; NbExp=11; IntAct=EBI-2514791, EBI-2558196;
CC Q96CS2; O14964: HGS; NbExp=3; IntAct=EBI-2514791, EBI-740220;
CC Q96CS2; P01112: HRAS; NbExp=3; IntAct=EBI-2514791, EBI-350145;
CC Q96CS2; O14879: IFIT3; NbExp=3; IntAct=EBI-2514791, EBI-745127;
CC Q96CS2; Q8IY31: IFT20; NbExp=5; IntAct=EBI-2514791, EBI-744203;
CC Q96CS2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2514791, EBI-6509505;
CC Q96CS2; O60341: KDM1A; NbExp=2; IntAct=EBI-2514791, EBI-710124;
CC Q96CS2; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-2514791, EBI-2125614;
CC Q96CS2; O14901: KLF11; NbExp=3; IntAct=EBI-2514791, EBI-948266;
CC Q96CS2; P04264: KRT1; NbExp=3; IntAct=EBI-2514791, EBI-298429;
CC Q96CS2; P19012: KRT15; NbExp=3; IntAct=EBI-2514791, EBI-739566;
CC Q96CS2; P05783: KRT18; NbExp=3; IntAct=EBI-2514791, EBI-297888;
CC Q96CS2; P08727: KRT19; NbExp=3; IntAct=EBI-2514791, EBI-742756;
CC Q96CS2; P12035: KRT3; NbExp=3; IntAct=EBI-2514791, EBI-2430095;
CC Q96CS2; Q15323: KRT31; NbExp=3; IntAct=EBI-2514791, EBI-948001;
CC Q96CS2; O76015: KRT38; NbExp=5; IntAct=EBI-2514791, EBI-1047263;
CC Q96CS2; Q6A162: KRT40; NbExp=3; IntAct=EBI-2514791, EBI-10171697;
CC Q96CS2; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-2514791, EBI-739657;
CC Q96CS2; O95751: LDOC1; NbExp=3; IntAct=EBI-2514791, EBI-740738;
CC Q96CS2; Q96LR2: LURAP1; NbExp=4; IntAct=EBI-2514791, EBI-741355;
CC Q96CS2; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-2514791, EBI-742610;
CC Q96CS2; P43360: MAGEA6; NbExp=3; IntAct=EBI-2514791, EBI-1045155;
CC Q96CS2; Q9NPJ6: MED4; NbExp=4; IntAct=EBI-2514791, EBI-394607;
CC Q96CS2; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-2514791, EBI-2548751;
CC Q96CS2; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-2514791, EBI-742948;
CC Q96CS2; O14777: NDC80; NbExp=3; IntAct=EBI-2514791, EBI-715849;
CC Q96CS2; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-2514791, EBI-10172876;
CC Q96CS2; Q9Y2I6: NINL; NbExp=3; IntAct=EBI-2514791, EBI-719716;
CC Q96CS2; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-2514791, EBI-741048;
CC Q96CS2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2514791, EBI-2811583;
CC Q96CS2; P37198: NUP62; NbExp=3; IntAct=EBI-2514791, EBI-347978;
CC Q96CS2; Q96M63: ODAD1; NbExp=3; IntAct=EBI-2514791, EBI-10173858;
CC Q96CS2; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-2514791, EBI-1105124;
CC Q96CS2; Q16512: PKN1; NbExp=3; IntAct=EBI-2514791, EBI-602382;
CC Q96CS2; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-2514791, EBI-5452779;
CC Q96CS2; Q96R06: SPAG5; NbExp=3; IntAct=EBI-2514791, EBI-413317;
CC Q96CS2; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-2514791, EBI-10172867;
CC Q96CS2; O75558: STX11; NbExp=3; IntAct=EBI-2514791, EBI-714135;
CC Q96CS2; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-2514791, EBI-6872807;
CC Q96CS2; A1L190: SYCE3; NbExp=4; IntAct=EBI-2514791, EBI-10283466;
CC Q96CS2; Q15561: TEAD4; NbExp=3; IntAct=EBI-2514791, EBI-747736;
CC Q96CS2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2514791, EBI-1105213;
CC Q96CS2; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-2514791, EBI-10178002;
CC Q96CS2; Q13077: TRAF1; NbExp=3; IntAct=EBI-2514791, EBI-359224;
CC Q96CS2; P36406: TRIM23; NbExp=3; IntAct=EBI-2514791, EBI-740098;
CC Q96CS2; P14373: TRIM27; NbExp=3; IntAct=EBI-2514791, EBI-719493;
CC Q96CS2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2514791, EBI-2130429;
CC Q96CS2; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-2514791, EBI-749955;
CC Q96CS2; Q86WT6-2: TRIM69; NbExp=4; IntAct=EBI-2514791, EBI-11525489;
CC Q96CS2; Q99816: TSG101; NbExp=6; IntAct=EBI-2514791, EBI-346882;
CC Q96CS2; Q99757: TXN2; NbExp=3; IntAct=EBI-2514791, EBI-2932492;
CC Q96CS2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2514791, EBI-739895;
CC Q96CS2; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-2514791, EBI-2559305;
CC Q96CS2; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-2514791, EBI-2799833;
CC Q96CS2; Q9Y3C0: WASHC3; NbExp=10; IntAct=EBI-2514791, EBI-712969;
CC Q96CS2-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-11742270, EBI-739624;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15082789, ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000305|PubMed:19369198}.
CC Note=Localizes with the spindle poles in mitotic cells. In metaphase,
CC localizes to the mitotic asters and is highly punctate on the
CC microtubule array. During later stages of mitosis, remains on the
CC spindle but is not present at the interzone, and is finally observed at
CC the microtubule bundles proximal to the midbody, clearly excluded from
CC the midbody. In contrast, does not colocalize with the tubulin
CC cytoskeleton in interphase cells. In interphase, localized at the
CC centrosome and diffusely in the cytoplasm. Localizes to mitotic spindle
CC microtubules. {ECO:0000269|PubMed:15082789,
CC ECO:0000269|PubMed:30723163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96CS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CS2-2; Sequence=VSP_010781;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas, kidney,
CC skeletal muscle, liver and heart. Weakly expressed in lung, brain and
CC placenta. {ECO:0000269|PubMed:15082789}.
CC -!- MISCELLANEOUS: HAUS1-depleted cells retain functional cell cycle
CC checkpoints, but the depletion decreases the G2/M cell cycle
CC compartment and induces apoptosis. The protein level remains constant
CC through the cell cycle.
CC -!- SIMILARITY: Belongs to the HAUS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05036.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY360137; AAQ63649.1; -; mRNA.
DR EMBL; AK097403; BAC05036.1; ALT_FRAME; mRNA.
DR EMBL; AK315605; BAG37974.1; -; mRNA.
DR EMBL; BC005958; AAH05958.1; -; mRNA.
DR EMBL; BC014003; AAH14003.1; -; mRNA.
DR CCDS; CCDS11928.1; -. [Q96CS2-1]
DR RefSeq; NP_612452.1; NM_138443.3. [Q96CS2-1]
DR AlphaFoldDB; Q96CS2; -.
DR SMR; Q96CS2; -.
DR BioGRID; 125412; 185.
DR ComplexPortal; CPX-1847; HAUS complex.
DR CORUM; Q96CS2; -.
DR DIP; DIP-48835N; -.
DR IntAct; Q96CS2; 137.
DR MINT; Q96CS2; -.
DR STRING; 9606.ENSP00000282058; -.
DR iPTMnet; Q96CS2; -.
DR PhosphoSitePlus; Q96CS2; -.
DR BioMuta; HAUS1; -.
DR DMDM; 50400607; -.
DR EPD; Q96CS2; -.
DR jPOST; Q96CS2; -.
DR MassIVE; Q96CS2; -.
DR MaxQB; Q96CS2; -.
DR PaxDb; Q96CS2; -.
DR PeptideAtlas; Q96CS2; -.
DR PRIDE; Q96CS2; -.
DR ProteomicsDB; 76212; -. [Q96CS2-1]
DR ProteomicsDB; 76213; -. [Q96CS2-2]
DR Antibodypedia; 22454; 103 antibodies from 18 providers.
DR DNASU; 115106; -.
DR Ensembl; ENST00000282058.11; ENSP00000282058.5; ENSG00000152240.13. [Q96CS2-1]
DR GeneID; 115106; -.
DR KEGG; hsa:115106; -.
DR MANE-Select; ENST00000282058.11; ENSP00000282058.5; NM_138443.4; NP_612452.1.
DR UCSC; uc002lbu.3; human. [Q96CS2-1]
DR CTD; 115106; -.
DR DisGeNET; 115106; -.
DR GeneCards; HAUS1; -.
DR HGNC; HGNC:25174; HAUS1.
DR HPA; ENSG00000152240; Low tissue specificity.
DR MIM; 608775; gene.
DR neXtProt; NX_Q96CS2; -.
DR OpenTargets; ENSG00000152240; -.
DR PharmGKB; PA165429013; -.
DR VEuPathDB; HostDB:ENSG00000152240; -.
DR eggNOG; ENOG502QSQA; Eukaryota.
DR GeneTree; ENSGT00390000006029; -.
DR HOGENOM; CLU_063322_0_0_1; -.
DR InParanoid; Q96CS2; -.
DR OMA; YQAEGAH; -.
DR OrthoDB; 1350537at2759; -.
DR PhylomeDB; Q96CS2; -.
DR TreeFam; TF331717; -.
DR PathwayCommons; Q96CS2; -.
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; Q96CS2; -.
DR SIGNOR; Q96CS2; -.
DR BioGRID-ORCS; 115106; 759 hits in 1085 CRISPR screens.
DR ChiTaRS; HAUS1; human.
DR GeneWiki; CCDC5; -.
DR GenomeRNAi; 115106; -.
DR Pharos; Q96CS2; Tbio.
DR PRO; PR:Q96CS2; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96CS2; protein.
DR Bgee; ENSG00000152240; Expressed in ganglionic eminence and 175 other tissues.
DR ExpressionAtlas; Q96CS2; baseline and differential.
DR Genevisible; Q96CS2; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070652; C:HAUS complex; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR InterPro; IPR026243; HAUS1.
DR PANTHER; PTHR31570; PTHR31570; 1.
DR PRINTS; PR02087; HAUSAUGMINL1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..278
FT /note="HAUS augmin-like complex subunit 1"
FT /id="PRO_0000089395"
FT COILED 49..79
FT /evidence="ECO:0000255"
FT COILED 124..177
FT /evidence="ECO:0000255"
FT COILED 249..277
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010781"
SQ SEQUENCE 278 AA; 31863 MW; 06F6A1B9FCF0698A CRC64;
MEPQEERETQ VAAWLKKIFG DHPIPQYEVN PRTTEILHHL SERNRVRDRD VYLVIEDLKQ
KASEYESEAK YLQDLLMESV NFSPANLSST GSRYLNALVD SAVALETKDT SLASFIPAVN
DLTSDLFRTK SKSEEIKIEL EKLEKNLTAT LVLEKCLQED VKKAELHLST ERAKVDNRRQ
NMDFLKAKSE EFRFGIKAAE EQLSARGMDA SLSHQSLVAL SEKLARLKQQ TIPLKKKLES
YLDLMPNPSL AQVKIEEAKR ELDSIEAELT RRVDMMEL
