ANKS3_HUMAN
ID ANKS3_HUMAN Reviewed; 656 AA.
AC Q6ZW76; B4DWU4; D3DUE2; Q8TF25;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 3;
GN Name=ANKS3; Synonyms=KIAA1977;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-404.
RC TISSUE=Esophagus, and Thalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-656.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [4]
RP INTERACTION WITH NEK7.
RX PubMed=26188091; DOI=10.1016/j.bbrc.2015.07.063;
RA Ramachandran H., Engel C., Mueller B., Dengjel J., Walz G., Yakulov T.A.;
RT "Anks3 alters the sub-cellular localization of the Nek7 kinase.";
RL Biochem. Biophys. Res. Commun. 464:901-907(2015).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 421-490 OF MUTANT ALA-471
RP HOMODIMER, X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 421-490 OF MUTANT
RP GLU-455 IN COMPLEX WITH ANKS6, DOMAIN, SUBUNIT, INTERACTION WITH ANKS6, AND
RP MUTAGENESIS OF ASP-450; ILE-455; GLU-466; LEU-471; PHE-472 AND LYS-477.
RX PubMed=24998259; DOI=10.1186/1472-6807-14-17;
RA Leettola C.N., Knight M.J., Cascio D., Hoffman S., Bowie J.U.;
RT "Characterization of the SAM domain of the PKD-related protein ANKS6 and
RT its interaction with ANKS3.";
RL BMC Struct. Biol. 14:17-17(2014).
CC -!- FUNCTION: May be involved in vasopressin signaling in the kidney.
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- SUBUNIT: Homooligomer (PubMed:24998259). Interacts (via SAM domain)
CC with ANKS6 (via SAM domain) (PubMed:24998259). Interacts with BICC1 (By
CC similarity). Interacts with NPHP1 (By similarity). Interacts with NEK8
CC (By similarity). Interacts with HIF1AN (By similarity). Interacts with
CC NEK7; this interaction alters the subcellular distribution of NEK7 by
CC preventing its nuclear translocation (PubMed:26188091).
CC {ECO:0000250|UniProtKB:Q9CZK6, ECO:0000269|PubMed:24998259,
CC ECO:0000269|PubMed:26188091}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9CZK6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZW76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZW76-2; Sequence=VSP_038183;
CC -!- DOMAIN: The SAM domain mediates homooligomerization.
CC {ECO:0000269|PubMed:24998259}.
CC -!- PTM: Hydroxylated at Asn-96, most probably by HIF1AN.
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- PTM: Phosphorylations at Ser-5, Ser-225, Thr-319, Ser-320, Ser-368 and
CC Ser-371 occur in a NEK7-dependent manner.
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q9CZK6}.
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DR EMBL; AK123496; BAC85629.1; -; mRNA.
DR EMBL; AK301683; BAG63156.1; -; mRNA.
DR EMBL; CH471112; EAW85271.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85272.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85273.1; -; Genomic_DNA.
DR EMBL; AB075857; BAB85563.1; -; mRNA.
DR CCDS; CCDS10520.1; -. [Q6ZW76-1]
DR RefSeq; NP_001229858.1; NM_001242929.1.
DR RefSeq; NP_001295018.1; NM_001308089.1.
DR RefSeq; NP_597707.1; NM_133450.3. [Q6ZW76-1]
DR RefSeq; XP_005255176.1; XM_005255119.3.
DR RefSeq; XP_011520675.1; XM_011522373.1. [Q6ZW76-1]
DR PDB; 4NJ8; X-ray; 1.60 A; A/B=421-490.
DR PDB; 4NL9; X-ray; 1.50 A; A/B=421-490.
DR PDBsum; 4NJ8; -.
DR PDBsum; 4NL9; -.
DR AlphaFoldDB; Q6ZW76; -.
DR SMR; Q6ZW76; -.
DR BioGRID; 125861; 40.
DR IntAct; Q6ZW76; 13.
DR MINT; Q6ZW76; -.
DR STRING; 9606.ENSP00000304586; -.
DR iPTMnet; Q6ZW76; -.
DR PhosphoSitePlus; Q6ZW76; -.
DR BioMuta; ANKS3; -.
DR DMDM; 74749704; -.
DR EPD; Q6ZW76; -.
DR jPOST; Q6ZW76; -.
DR MassIVE; Q6ZW76; -.
DR MaxQB; Q6ZW76; -.
DR PaxDb; Q6ZW76; -.
DR PeptideAtlas; Q6ZW76; -.
DR PRIDE; Q6ZW76; -.
DR ProteomicsDB; 68467; -. [Q6ZW76-1]
DR ProteomicsDB; 68468; -. [Q6ZW76-2]
DR Antibodypedia; 24396; 93 antibodies from 21 providers.
DR DNASU; 124401; -.
DR Ensembl; ENST00000304283.9; ENSP00000304586.4; ENSG00000168096.15. [Q6ZW76-1]
DR Ensembl; ENST00000585773.5; ENSP00000465294.1; ENSG00000168096.15. [Q6ZW76-2]
DR Ensembl; ENST00000614075.4; ENSP00000480350.1; ENSG00000168096.15. [Q6ZW76-1]
DR GeneID; 124401; -.
DR KEGG; hsa:124401; -.
DR MANE-Select; ENST00000304283.9; ENSP00000304586.4; NM_133450.4; NP_597707.1.
DR UCSC; uc002cxj.3; human. [Q6ZW76-1]
DR CTD; 124401; -.
DR DisGeNET; 124401; -.
DR GeneCards; ANKS3; -.
DR HGNC; HGNC:29422; ANKS3.
DR HPA; ENSG00000168096; Low tissue specificity.
DR MalaCards; ANKS3; -.
DR neXtProt; NX_Q6ZW76; -.
DR OpenTargets; ENSG00000168096; -.
DR Orphanet; 101063; Situs inversus totalis.
DR PharmGKB; PA143485303; -.
DR VEuPathDB; HostDB:ENSG00000168096; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000156610; -.
DR HOGENOM; CLU_014543_0_0_1; -.
DR InParanoid; Q6ZW76; -.
DR OMA; NKGHHSK; -.
DR OrthoDB; 58543at2759; -.
DR PhylomeDB; Q6ZW76; -.
DR TreeFam; TF331487; -.
DR PathwayCommons; Q6ZW76; -.
DR SignaLink; Q6ZW76; -.
DR BioGRID-ORCS; 124401; 12 hits in 1079 CRISPR screens.
DR GenomeRNAi; 124401; -.
DR Pharos; Q6ZW76; Tbio.
DR PRO; PR:Q6ZW76; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6ZW76; protein.
DR Bgee; ENSG00000168096; Expressed in cerebellar hemisphere and 130 other tissues.
DR ExpressionAtlas; Q6ZW76; baseline and differential.
DR Genevisible; Q6ZW76; HS.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cell projection;
KW Coiled coil; Cytoplasm; Hydroxylation; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..656
FT /note="Ankyrin repeat and SAM domain-containing protein 3"
FT /id="PRO_0000230777"
FT REPEAT 34..64
FT /note="ANK 1"
FT REPEAT 68..97
FT /note="ANK 2"
FT REPEAT 101..130
FT /note="ANK 3"
FT REPEAT 134..163
FT /note="ANK 4"
FT REPEAT 168..197
FT /note="ANK 5"
FT REPEAT 201..220
FT /note="ANK 6"
FT DOMAIN 425..488
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..422
FT /note="Interaction with NEK7"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT REGION 235..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 501..526
FT /evidence="ECO:0000255"
FT COMPBIAS 346..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M9H0"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M9H0"
FT MOD_RES 96
FT /note="3-hydroxyasparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038183"
FT VARIANT 404
FT /note="A -> T (in dbSNP:rs863980)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048283"
FT VARIANT 593
FT /note="A -> T (in dbSNP:rs9936675)"
FT /id="VAR_048284"
FT MUTAGEN 450
FT /note="D->K: Decreased homooligomerization. No effect on
FT interaction with ANKS6."
FT /evidence="ECO:0000269|PubMed:24998259"
FT MUTAGEN 455
FT /note="I->E: Decreased homooligomerization. No effect on
FT interaction with ANKS6."
FT /evidence="ECO:0000269|PubMed:24998259"
FT MUTAGEN 466
FT /note="E->K: Decreased homooligomerization. No effect on
FT interaction with ANKS6."
FT /evidence="ECO:0000269|PubMed:24998259"
FT MUTAGEN 471
FT /note="L->E: Decreased homooligomerization. Decreased
FT interaction with ANKS6."
FT /evidence="ECO:0000269|PubMed:24998259"
FT MUTAGEN 472
FT /note="F->E: Decreased homooligomerization. Decreased
FT interaction with ANKS6."
FT /evidence="ECO:0000269|PubMed:24998259"
FT MUTAGEN 477
FT /note="K->E: Decreased homooligomerization. Decreased
FT interaction with ANKS6."
FT /evidence="ECO:0000269|PubMed:24998259"
FT CONFLICT 51..56
FT /note="VKECVQ -> HILRLF (in Ref. 3; BAB85563)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="F -> S (in Ref. 1; BAG63156)"
FT /evidence="ECO:0000305"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 461..467
FT /evidence="ECO:0007829|PDB:4NL9"
FT HELIX 472..484
FT /evidence="ECO:0007829|PDB:4NL9"
SQ SEQUENCE 656 AA; 72038 MW; 67BD772ED762A5BA CRC64;
MSELSDEASE PELLNRSLSM WHGLGTQVSG EELDVPLDLH TAASIGQYEV VKECVQRREL
DLNKKNGGGW TPLMYASYIG HDTIVHLLLE AGVSVNVPTP EGQTPLMLAS SCGNESIAYF
LLQQGAELEM KDIQGWTALF HCTSAGHQHM VRFLLDSGAN ANVREPICGF TPLMEAAAAG
HEIIVQYFLN HGVKVDARDH SGATARMLAK QYGHMKIVAL MDTYSPSLPK SLYRSPEKYE
DLSSSDESCP APQRQRPCRK KGVSIHEGPR ALARITGIGL GGRAPRPRYE QAPPRGYVTF
NSSGENPLEE EGLCCRDVTS PINERDVESS SSSSSREEHA FCANLGPVQS SSSSEGLARA
QGLSSEASVE SNEDSDHACK SSARKQAKSY MKTKNPDSQW PPRAATDREG FLAESSPQTQ
RAPYSGPQDL AALLEQIGCL KYLQVFEEQD VDLRIFLTLT ESDLKEIGIT LFGPKRKMTS
AIARWHSSAR PPGDALELAY ADRLEAEMQE LAIQLHKRCE EVEATRGQVC QEQELRAVVE
SCLLEQDRAR EDLQARLRET WALARDAALV LDQLRACQAE LSSRVRQDQP PGAATLGLAV
PPADSKGWQA SLQAMSLPEL SGALEDRVRE MGQALCLVTQ SLEKLQVLNG KKWRET
