ADIP_HUMAN
ID ADIP_HUMAN Reviewed; 614 AA.
AC Q9Y2D8; A8K8W0; B4DFE3; D3DT13; J3KR02; Q6P2P8; Q6ULS1; Q7L168; Q9UIX0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Afadin- and alpha-actinin-binding protein;
DE Short=ADIP;
DE AltName: Full=Afadin DIL domain-interacting protein;
DE AltName: Full=SSX2-interacting protein;
GN Name=SSX2IP; Synonyms=KIAA0923;
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], INTERACTION WITH SSX2 AND SSX3, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Testis;
RX PubMed=12007189; DOI=10.1002/gcc.10073;
RA de Bruijn D.R.H., dos Santos N.R., Kater-Baats E., Thijssen J.,
RA van den Berk L., Stap J., Balemans M., Schepens M., Merkx G.,
RA van Kessel A.G.;
RT "The cancer-related protein SSX2 interacts with the human homologue of a
RT Ras-like GTPase interactor, RAB3IP, and a novel nuclear protein, SSX2IP.";
RL Genes Chromosomes Cancer 34:285-298(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning a new transcript of X breakpoint 2 interacting protein (SSX2IP) in
RT testis.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ARG-578.
RC TISSUE=Cerebellum, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-578.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 [9]
RP MYELOID LEUKEMIA-ASSOCIATED ANTIGEN.
RX PubMed=17686061; DOI=10.1111/j.1365-2141.2007.06706.x;
RA Denniss F.A., Breslin A., Ingram W., Hardwick N.R., Mufti G.J., Guinn B.A.;
RT "The leukaemia-associated antigen, SSX2IP, is expressed during mitosis on
RT the surface of myeloid leukaemia cells.";
RL Br. J. Haematol. 138:668-669(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-536, AND
RP 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 [11]
RP MYELOID LEUKEMIA-ASSOCIATED ANTIGEN.
RX PubMed=19179477; DOI=10.1182/blood-2008-09-178848;
RA Guinn B., Greiner J., Schmitt M., Mills K.I.;
RT "Elevated expression of the leukemia-associated antigen SSX2IP predicts
RT survival in acute myeloid leukemia patients who lack detectable cytogenetic
RT rearrangements.";
RL Blood 113:1203-1204(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-293 AND SER-312, 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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=23816619; DOI=10.1083/jcb.201302122;
RA Barenz F., Inoue D., Yokoyama H., Tegha-Dunghu J., Freiss S., Draeger S.,
RA Mayilo D., Cado I., Merker S., Klinger M., Hoeckendorf B., Pilz S.,
RA Hupfeld K., Steinbeisser H., Lorenz H., Ruppert T., Wittbrodt J.,
RA Gruss O.J.;
RT "The centriolar satellite protein SSX2IP promotes centrosome maturation.";
RL J. Cell Biol. 202:81-95(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-312; SER-536;
RP SER-540 AND SER-542, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP DEVELOPMENTAL STAGE.
RX PubMed=23826132; DOI=10.1371/journal.pone.0066782;
RA Li P., Chen X., Su L., Li C., Zhi Q., Yu B., Sheng H., Wang J., Feng R.,
RA Cai Q., Li J., Yu Y., Yan M., Liu B., Zhu Z.;
RT "Epigenetic silencing of miR-338-3p contributes to tumorigenicity in
RT gastric cancer by targeting SSX2IP.";
RL PLoS ONE 8:E66782-E66782(2013).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24356449; DOI=10.1091/mbc.e13-09-0526;
RA Klinger M., Wang W., Kuhns S., Baerenz F., Draeger-Meurer S., Pereira G.,
RA Gruss O.J.;
RT "The novel centriolar satellite protein SSX2IP targets Cep290 to the
RT ciliary transition zone.";
RL Mol. Biol. Cell 25:495-507(2014).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WRAP73.
RX PubMed=26545777; DOI=10.1016/j.bbrc.2015.10.169;
RA Hori A., Morand A., Ikebe C., Frith D., Snijders A.P., Toda T.;
RT "The conserved Wdr8-hMsd1/SSX2IP complex localises to the centrosome and
RT ensures proper spindle length and orientation.";
RL Biochem. Biophys. Res. Commun. 468:39-45(2015).
CC -!- FUNCTION: Belongs to an adhesion system, which plays a role in the
CC organization of homotypic, interneuronal and heterotypic cell-cell
CC adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-
CC catenin system through alpha-actinin and may be involved in
CC organization of the actin cytoskeleton at AJs through afadin and alpha-
CC actinin (By similarity). Involved in cell movement: localizes at the
CC leading edge of moving cells in response to PDGF and is required for
CC the formation of the leading edge and the promotion of cell movement,
CC possibly via activation of Rac signaling (By similarity). Acts as a
CC centrosome maturation factor, probably by maintaining the integrity of
CC the pericentriolar material and proper microtubule nucleation at
CC mitotic spindle poles. The function seems to implicate at least in part
CC WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of
CC spindle anchoring at the mitotic centrosome (PubMed:23816619,
CC PubMed:26545777). Involved in ciliogenesis (PubMed:24356449). It is
CC required for targeted recruitment of the BBSome, CEP290, RAB8, and
CC SSTR3 to the cilia (PubMed:24356449). {ECO:0000250|UniProtKB:Q8VC66,
CC ECO:0000269|PubMed:23816619, ECO:0000269|PubMed:24356449,
CC ECO:0000305|PubMed:26545777}.
CC -!- SUBUNIT: Interacts with afadin and alpha-actinin (By similarity).
CC Interacts with VAV2 (By similarity). Interacts with SSX2 and SSX3. Does
CC not interact with SSX1 and SSX4 (PubMed:12007189). Interacts with PCM1
CC (By similarity). Interacts with WRAP73 (PubMed:26545777).
CC {ECO:0000250|UniProtKB:Q8VC66, ECO:0000269|PubMed:12007189,
CC ECO:0000269|PubMed:26545777}.
CC -!- INTERACTION:
CC Q9Y2D8; O94929: ABLIM3; NbExp=3; IntAct=EBI-2212028, EBI-351267;
CC Q9Y2D8; Q8WTP8: AEN; NbExp=3; IntAct=EBI-2212028, EBI-8637627;
CC Q9Y2D8; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-2212028, EBI-541426;
CC Q9Y2D8; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-2212028, EBI-745073;
CC Q9Y2D8; Q13895: BYSL; NbExp=5; IntAct=EBI-2212028, EBI-358049;
CC Q9Y2D8; Q9H0W9: C11orf54; NbExp=3; IntAct=EBI-2212028, EBI-740204;
CC Q9Y2D8; Q9H257: CARD9; NbExp=3; IntAct=EBI-2212028, EBI-751319;
CC Q9Y2D8; Q9NVL8: CCDC198; NbExp=3; IntAct=EBI-2212028, EBI-10238351;
CC Q9Y2D8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-2212028, EBI-10175300;
CC Q9Y2D8; P51946: CCNH; NbExp=4; IntAct=EBI-2212028, EBI-741406;
CC Q9Y2D8; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-2212028, EBI-396137;
CC Q9Y2D8; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-2212028, EBI-5278764;
CC Q9Y2D8; Q53EZ4: CEP55; NbExp=5; IntAct=EBI-2212028, EBI-747776;
CC Q9Y2D8; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-2212028, EBI-743375;
CC Q9Y2D8; Q9UER7: DAXX; NbExp=3; IntAct=EBI-2212028, EBI-77321;
CC Q9Y2D8; Q9Y295: DRG1; NbExp=3; IntAct=EBI-2212028, EBI-719554;
CC Q9Y2D8; Q08426: EHHADH; NbExp=3; IntAct=EBI-2212028, EBI-2339219;
CC Q9Y2D8; Q14240: EIF4A2; NbExp=3; IntAct=EBI-2212028, EBI-73473;
CC Q9Y2D8; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-2212028, EBI-10232522;
CC Q9Y2D8; O75616: ERAL1; NbExp=3; IntAct=EBI-2212028, EBI-6393536;
CC Q9Y2D8; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-2212028, EBI-741626;
CC Q9Y2D8; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2212028, EBI-719941;
CC Q9Y2D8; Q32MH5: FAM214A; NbExp=3; IntAct=EBI-2212028, EBI-2866142;
CC Q9Y2D8; Q9NW38: FANCL; NbExp=3; IntAct=EBI-2212028, EBI-2339898;
CC Q9Y2D8; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-2212028, EBI-10244131;
CC Q9Y2D8; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-2212028, EBI-744935;
CC Q9Y2D8; Q96NE9: FRMD6; NbExp=3; IntAct=EBI-2212028, EBI-741729;
CC Q9Y2D8; P55040: GEM; NbExp=3; IntAct=EBI-2212028, EBI-744104;
CC Q9Y2D8; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-2212028, EBI-10181260;
CC Q9Y2D8; P56524-2: HDAC4; NbExp=3; IntAct=EBI-2212028, EBI-11953488;
CC Q9Y2D8; Q9C086: INO80B; NbExp=3; IntAct=EBI-2212028, EBI-715611;
CC Q9Y2D8; Q92993: KAT5; NbExp=3; IntAct=EBI-2212028, EBI-399080;
CC Q9Y2D8; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2212028, EBI-14069005;
CC Q9Y2D8; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-2212028, EBI-739890;
CC Q9Y2D8; P19012: KRT15; NbExp=3; IntAct=EBI-2212028, EBI-739566;
CC Q9Y2D8; Q15323: KRT31; NbExp=3; IntAct=EBI-2212028, EBI-948001;
CC Q9Y2D8; Q6A162: KRT40; NbExp=3; IntAct=EBI-2212028, EBI-10171697;
CC Q9Y2D8; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-2212028, EBI-10172290;
CC Q9Y2D8; Q6PJG3: LATS1; NbExp=3; IntAct=EBI-2212028, EBI-10253976;
CC Q9Y2D8; P25791: LMO2; NbExp=3; IntAct=EBI-2212028, EBI-739696;
CC Q9Y2D8; P55081: MFAP1; NbExp=3; IntAct=EBI-2212028, EBI-1048159;
CC Q9Y2D8; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-2212028, EBI-14086479;
CC Q9Y2D8; Q8NDC4: MORN4; NbExp=6; IntAct=EBI-2212028, EBI-10269566;
CC Q9Y2D8; P00540: MOS; NbExp=3; IntAct=EBI-2212028, EBI-1757866;
CC Q9Y2D8; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-2212028, EBI-2513715;
CC Q9Y2D8; P41227: NAA10; NbExp=3; IntAct=EBI-2212028, EBI-747693;
CC Q9Y2D8; Q9UGY1: NOL12; NbExp=3; IntAct=EBI-2212028, EBI-716098;
CC Q9Y2D8; Q15154: PCM1; NbExp=10; IntAct=EBI-2212028, EBI-741421;
CC Q9Y2D8; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-2212028, EBI-713786;
CC Q9Y2D8; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-2212028, EBI-2568609;
CC Q9Y2D8; Q16512: PKN1; NbExp=3; IntAct=EBI-2212028, EBI-602382;
CC Q9Y2D8; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-2212028, EBI-10320765;
CC Q9Y2D8; Q13131: PRKAA1; NbExp=3; IntAct=EBI-2212028, EBI-1181405;
CC Q9Y2D8; O43395: PRPF3; NbExp=3; IntAct=EBI-2212028, EBI-744322;
CC Q9Y2D8; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-2212028, EBI-1567797;
CC Q9Y2D8; P25786: PSMA1; NbExp=3; IntAct=EBI-2212028, EBI-359352;
CC Q9Y2D8; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2212028, EBI-748391;
CC Q9Y2D8; Q9NUL5: SHFL; NbExp=3; IntAct=EBI-2212028, EBI-10313866;
CC Q9Y2D8; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-2212028, EBI-11955083;
CC Q9Y2D8; Q16385: SSX2B; NbExp=8; IntAct=EBI-2212028, EBI-2210673;
CC Q9Y2D8; Q99909: SSX3; NbExp=3; IntAct=EBI-2212028, EBI-10295431;
CC Q9Y2D8; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-2212028, EBI-745392;
CC Q9Y2D8; Q32MN6: TBP; NbExp=3; IntAct=EBI-2212028, EBI-10239991;
CC Q9Y2D8; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-2212028, EBI-10176734;
CC Q9Y2D8; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-2212028, EBI-1105213;
CC Q9Y2D8; O95985: TOP3B; NbExp=4; IntAct=EBI-2212028, EBI-373403;
CC Q9Y2D8; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-2212028, EBI-10175039;
CC Q9Y2D8; O94972: TRIM37; NbExp=4; IntAct=EBI-2212028, EBI-741602;
CC Q9Y2D8; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-2212028, EBI-5235829;
CC Q9Y2D8; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2212028, EBI-2130429;
CC Q9Y2D8; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2212028, EBI-10241197;
CC Q9Y2D8; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-2212028, EBI-8994397;
CC Q9Y2D8; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-2212028, EBI-6447954;
CC Q9Y2D8; P61964: WDR5; NbExp=3; IntAct=EBI-2212028, EBI-540834;
CC Q9Y2D8; Q9P2S5: WRAP73; NbExp=9; IntAct=EBI-2212028, EBI-1054904;
CC Q9Y2D8; P98170: XIAP; NbExp=4; IntAct=EBI-2212028, EBI-517127;
CC Q9Y2D8; O43167: ZBTB24; NbExp=3; IntAct=EBI-2212028, EBI-744471;
CC Q9Y2D8; Q8N5A5: ZGPAT; NbExp=4; IntAct=EBI-2212028, EBI-3439227;
CC Q9Y2D8; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-2212028, EBI-10183064;
CC Q9Y2D8; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-2212028, EBI-2682299;
CC Q9Y2D8; Q15973: ZNF124; NbExp=3; IntAct=EBI-2212028, EBI-2555767;
CC Q9Y2D8; O95125: ZNF202; NbExp=3; IntAct=EBI-2212028, EBI-751960;
CC Q9Y2D8; P15622-3: ZNF250; NbExp=6; IntAct=EBI-2212028, EBI-10177272;
CC Q9Y2D8; P17036: ZNF3; NbExp=3; IntAct=EBI-2212028, EBI-1640965;
CC Q9Y2D8; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-2212028, EBI-347633;
CC Q9Y2D8; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2212028, EBI-740727;
CC Q9Y2D8; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-2212028, EBI-11962468;
CC Q9Y2D8; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-2212028, EBI-6427977;
CC Q9Y2D8; Q5T619: ZNF648; NbExp=3; IntAct=EBI-2212028, EBI-11985915;
CC Q9Y2D8; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-2212028, EBI-16429014;
CC Q9Y2D8; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-2212028, EBI-10240849;
CC Q9Y2D8; Q15696: ZRSR2; NbExp=3; IntAct=EBI-2212028, EBI-6657923;
CC Q9Y2D8; O43309: ZSCAN12; NbExp=3; IntAct=EBI-2212028, EBI-1210440;
CC Q9Y2D8; A8K932; NbExp=3; IntAct=EBI-2212028, EBI-10174671;
CC Q9Y2D8; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-2212028, EBI-25492395;
CC Q9Y2D8; P03410: tax; Xeno; NbExp=3; IntAct=EBI-2212028, EBI-9676218;
CC Q9Y2D8; Q9JM98: Wrap73; Xeno; NbExp=3; IntAct=EBI-2212028, EBI-11694665;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome, centriolar satellite {ECO:0000269|PubMed:23816619,
CC ECO:0000269|PubMed:24356449}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:24356449}. Note=Not found at cell-matrix AJs.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2D8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2D8-2; Sequence=VSP_011724, VSP_011725;
CC Name=3;
CC IsoId=Q9Y2D8-3; Sequence=VSP_046368;
CC -!- TISSUE SPECIFICITY: Widely expressed, with the highest expression in
CC brain, intermediate expression in kidney, testis, spinal cord, liver,
CC heart, lung, skeletal muscle, ovary, fetal liver and fetal brain, and
CC little to no expression in pancreas and spleen. All specific brain
CC regions showed intermediate to high expression, with highest expression
CC in amygdala. Also expressed in fetal tissues, mainly in liver and
CC brain.
CC -!- DEVELOPMENTAL STAGE: Expressed in interphase and M phase cells. Down-
CC regulated by the miRNA miR338-3p. {ECO:0000269|PubMed:23816619,
CC ECO:0000269|PubMed:23826132}.
CC -!- DOMAIN: Both the N-terminal (up to position 79) and the C-terminal
CC (from position 304) sequences are required for interaction with SSX2.
CC -!- MISCELLANEOUS: Acts as an acute myeloid leukemia-associated antigen and
CC may be used as a potential immunotherapy target for leukemia
CC (PubMed:17686061, PubMed:19179477). {ECO:0000305|PubMed:17686061,
CC ECO:0000305|PubMed:19179477}.
CC -!- SIMILARITY: Belongs to the ADIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76767.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SSX2IPID42407ch1p22.html";
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DR EMBL; AY367055; AAQ72373.1; -; mRNA.
DR EMBL; AB023140; BAA76767.2; ALT_INIT; mRNA.
DR EMBL; AK292475; BAF85164.1; -; mRNA.
DR EMBL; AK294057; BAG57404.1; -; mRNA.
DR EMBL; AL133046; CAB61373.1; -; mRNA.
DR EMBL; AC114482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73224.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73226.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73227.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73228.1; -; Genomic_DNA.
DR EMBL; BC033637; AAH33637.1; -; mRNA.
DR EMBL; BC064389; AAH64389.1; -; mRNA.
DR CCDS; CCDS53337.1; -. [Q9Y2D8-3]
DR CCDS; CCDS699.1; -. [Q9Y2D8-1]
DR PIR; T42649; T42649.
DR RefSeq; NP_001159765.1; NM_001166293.1. [Q9Y2D8-1]
DR RefSeq; NP_001159766.1; NM_001166294.1. [Q9Y2D8-3]
DR RefSeq; NP_001159767.1; NM_001166295.1. [Q9Y2D8-3]
DR RefSeq; NP_001159889.1; NM_001166417.1. [Q9Y2D8-1]
DR RefSeq; NP_054740.3; NM_014021.3. [Q9Y2D8-1]
DR RefSeq; XP_005270484.1; XM_005270427.1. [Q9Y2D8-1]
DR RefSeq; XP_005270485.1; XM_005270428.1. [Q9Y2D8-1]
DR RefSeq; XP_006710394.1; XM_006710331.1. [Q9Y2D8-3]
DR RefSeq; XP_011538912.1; XM_011540610.1.
DR RefSeq; XP_016855723.1; XM_017000234.1. [Q9Y2D8-1]
DR AlphaFoldDB; Q9Y2D8; -.
DR SMR; Q9Y2D8; -.
DR BioGRID; 125567; 306.
DR IntAct; Q9Y2D8; 327.
DR MINT; Q9Y2D8; -.
DR STRING; 9606.ENSP00000340279; -.
DR MoonDB; Q9Y2D8; Predicted.
DR iPTMnet; Q9Y2D8; -.
DR PhosphoSitePlus; Q9Y2D8; -.
DR BioMuta; SSX2IP; -.
DR DMDM; 54035738; -.
DR EPD; Q9Y2D8; -.
DR jPOST; Q9Y2D8; -.
DR MassIVE; Q9Y2D8; -.
DR MaxQB; Q9Y2D8; -.
DR PaxDb; Q9Y2D8; -.
DR PeptideAtlas; Q9Y2D8; -.
DR PRIDE; Q9Y2D8; -.
DR ProteomicsDB; 85743; -. [Q9Y2D8-1]
DR ProteomicsDB; 85744; -. [Q9Y2D8-2]
DR Antibodypedia; 19778; 235 antibodies from 30 providers.
DR DNASU; 117178; -.
DR Ensembl; ENST00000342203.8; ENSP00000340279.3; ENSG00000117155.17. [Q9Y2D8-1]
DR Ensembl; ENST00000437941.6; ENSP00000412781.2; ENSG00000117155.17. [Q9Y2D8-3]
DR Ensembl; ENST00000481102.5; ENSP00000432261.1; ENSG00000117155.17. [Q9Y2D8-2]
DR Ensembl; ENST00000605755.5; ENSP00000474480.1; ENSG00000117155.17. [Q9Y2D8-3]
DR GeneID; 117178; -.
DR KEGG; hsa:117178; -.
DR MANE-Select; ENST00000342203.8; ENSP00000340279.3; NM_001166293.2; NP_001159765.1.
DR UCSC; uc001dkj.4; human. [Q9Y2D8-1]
DR CTD; 117178; -.
DR DisGeNET; 117178; -.
DR GeneCards; SSX2IP; -.
DR HGNC; HGNC:16509; SSX2IP.
DR HPA; ENSG00000117155; Tissue enhanced (retina, testis).
DR MIM; 608690; gene.
DR neXtProt; NX_Q9Y2D8; -.
DR OpenTargets; ENSG00000117155; -.
DR PharmGKB; PA38155; -.
DR VEuPathDB; HostDB:ENSG00000117155; -.
DR eggNOG; ENOG502QQJF; Eukaryota.
DR GeneTree; ENSGT00390000007688; -.
DR HOGENOM; CLU_031049_0_0_1; -.
DR InParanoid; Q9Y2D8; -.
DR OMA; QHCKEMI; -.
DR OrthoDB; 753479at2759; -.
DR PhylomeDB; Q9Y2D8; -.
DR TreeFam; TF332889; -.
DR PathwayCommons; Q9Y2D8; -.
DR SignaLink; Q9Y2D8; -.
DR BioGRID-ORCS; 117178; 5 hits in 1080 CRISPR screens.
DR ChiTaRS; SSX2IP; human.
DR GeneWiki; SSX2IP; -.
DR GenomeRNAi; 117178; -.
DR Pharos; Q9Y2D8; Tbio.
DR PRO; PR:Q9Y2D8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y2D8; protein.
DR Bgee; ENSG00000117155; Expressed in left testis and 182 other tissues.
DR ExpressionAtlas; Q9Y2D8; baseline and differential.
DR Genevisible; Q9Y2D8; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; IEA:Ensembl.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IEA:Ensembl.
DR InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR Pfam; PF11559; ADIP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..614
FT /note="Afadin- and alpha-actinin-binding protein"
FT /id="PRO_0000064455"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..227
FT /evidence="ECO:0000255"
FT COILED 266..293
FT /evidence="ECO:0000255"
FT COILED 374..460
FT /evidence="ECO:0000255"
FT COMPBIAS 292..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046368"
FT VAR_SEQ 557..560
FT /note="SSIN -> RAKN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011724"
FT VAR_SEQ 561..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011725"
FT VARIANT 578
FT /note="C -> R (in dbSNP:rs1057746)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_056726"
FT CONFLICT 232
FT /note="V -> A (in Ref. 2; AAQ72373)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="Missing (in Ref. 8; AAH64389)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="G -> V (in Ref. 2; AAQ72373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 71236 MW; 427903EF86A6FE31 CRC64;
MGDWMTVTDP GLSSESKTIS QYTSETKMSP SSLYSQQVLC SSIPLSKNVH SFFSAFCTED
NIEQSISYLD QELTTFGFPS LYEESKGKET KRELNIVAVL NCMNELLVLQ RKNLLAQENV
ETQNLKLGSD MDHLQSCYSK LKEQLETSRR EMIGLQERDR QLQCKNRNLH QLLKNEKDEV
QKLQNIIASR ATQYNHDMKR KEREYNKLKE RLHQLVMNKK DKKIAMDILN YVGRADGKRG
SWRTGKTEAR NEDEMYKILL NDYEYRQKQI LMENAELKKV LQQMKKEMIS LLSPQKKKPR
ERVDDSTGTV ISDVEEDAGE LSRESMWDLS CETVREQLTN SIRKQWRILK SHVEKLDNQV
SKVHLEGFND EDVISRQDHE QETEKLELEI QQCKEMIKTQ QQLLQQQLAT AYDDDTTSLL
RDCYLLEEKE RLKEEWSLFK EQKKNFERER RSFTEAAIRL GLERKAFEEE RASWLKQQFL
NMTTFDHQNS ENVKLFSAFS GSSDWDNLIV HSRQPQKKPH SVSNGSPVCM SKLTKSLPAS
PSTSDFCQTR SCISEHSSIN VLNITAEEIK PNQVGGECTN QKWSVASRPG SQEGCYSGCS
LSYTNSHVEK DDLP
