SSX3_HUMAN
ID SSX3_HUMAN Reviewed; 188 AA.
AC Q99909; O60223; Q5JQZ3; Q9BRW7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein SSX3;
DE AltName: Full=Cancer/testis antigen 5.3;
DE Short=CT5.3;
GN Name=SSX3;
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=Fibrosarcoma, and Testis;
RX PubMed=8697803; DOI=10.1159/000134334;
RA de Leeuw B., Balemans M., Geurts van Kessel A.;
RT "A novel Kruppel-associated box containing the SSX gene (SSX3) on the human
RT X chromosome is not implicated in t(X;18)-positive synovial sarcomas.";
RL Cytogenet. Cell Genet. 73:179-183(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9378559;
RX DOI=10.1002/(sici)1097-0215(19970917)72:6<965::aid-ijc8>3.0.co;2-n;
RA Gure A.O., Tuereci O., Sahin U., Tsang S., Scanlan M.J., Jager E.,
RA Knuth A., Pfreundschuh M., Old L.J., Chen Y.-T.;
RT "SSX: a multigene family with several members transcribed in normal testis
RT and human cancer.";
RL Int. J. Cancer 72:965-971(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow;
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 INTERACTION WITH SSX2IP.
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).
CC -!- FUNCTION: Could act as a modulator of transcription.
CC -!- SUBUNIT: Interacts with SSX2IP. {ECO:0000269|PubMed:12007189}.
CC -!- INTERACTION:
CC Q99909; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-10295431, EBI-741181;
CC Q99909; Q6PJH3: AKAP9; NbExp=5; IntAct=EBI-10295431, EBI-11745576;
CC Q99909; Q9BRT8: CBWD1; NbExp=3; IntAct=EBI-10295431, EBI-1054417;
CC Q99909; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-10295431, EBI-11524851;
CC Q99909; Q96MT8: CEP63; NbExp=4; IntAct=EBI-10295431, EBI-741977;
CC Q99909; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10295431, EBI-739624;
CC Q99909; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-10295431, EBI-17278014;
CC Q99909; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-10295431, EBI-2548702;
CC Q99909; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-10295431, EBI-11522780;
CC Q99909; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-10295431, EBI-3044087;
CC Q99909; Q9NPJ6: MED4; NbExp=6; IntAct=EBI-10295431, EBI-394607;
CC Q99909; P50222: MEOX2; NbExp=3; IntAct=EBI-10295431, EBI-748397;
CC Q99909; Q8TD10: MIPOL1; NbExp=7; IntAct=EBI-10295431, EBI-2548751;
CC Q99909; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-10295431, EBI-10232538;
CC Q99909; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-10295431, EBI-14093916;
CC Q99909; Q9H4E5: RHOJ; NbExp=4; IntAct=EBI-10295431, EBI-6285694;
CC Q99909; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-10295431, EBI-2212028;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99909-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99909-2; Sequence=VSP_042777;
CC -!- SIMILARITY: Belongs to the SSX family. {ECO:0000305}.
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DR EMBL; S82471; AAB37436.2; -; mRNA.
DR EMBL; U90840; AAC05819.1; -; mRNA.
DR EMBL; AL606490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471164; EAW59347.1; -; Genomic_DNA.
DR EMBL; BC005904; AAH05904.1; -; mRNA.
DR EMBL; BC103862; AAI03863.1; -; mRNA.
DR CCDS; CCDS14291.1; -. [Q99909-1]
DR RefSeq; NP_066294.1; NM_021014.3. [Q99909-1]
DR RefSeq; XP_011542187.1; XM_011543885.2. [Q99909-2]
DR AlphaFoldDB; Q99909; -.
DR BioGRID; 115509; 39.
DR IntAct; Q99909; 27.
DR STRING; 9606.ENSP00000298396; -.
DR iPTMnet; Q99909; -.
DR PhosphoSitePlus; Q99909; -.
DR BioMuta; SSX3; -.
DR DMDM; 84028266; -.
DR MassIVE; Q99909; -.
DR PaxDb; Q99909; -.
DR PeptideAtlas; Q99909; -.
DR PRIDE; Q99909; -.
DR ProteomicsDB; 78520; -. [Q99909-1]
DR ProteomicsDB; 78521; -. [Q99909-2]
DR Antibodypedia; 25608; 93 antibodies from 18 providers.
DR DNASU; 10214; -.
DR Ensembl; ENST00000298396.7; ENSP00000298396.2; ENSG00000165584.16. [Q99909-1]
DR Ensembl; ENST00000376893.7; ENSP00000366090.3; ENSG00000165584.16. [Q99909-2]
DR GeneID; 10214; -.
DR KEGG; hsa:10214; -.
DR MANE-Select; ENST00000298396.7; ENSP00000298396.2; NM_021014.4; NP_066294.1.
DR UCSC; uc004djd.3; human. [Q99909-1]
DR CTD; 10214; -.
DR DisGeNET; 10214; -.
DR GeneCards; SSX3; -.
DR HGNC; HGNC:11337; SSX3.
DR HPA; ENSG00000165584; Tissue enriched (testis).
DR MIM; 300325; gene.
DR neXtProt; NX_Q99909; -.
DR OpenTargets; ENSG00000165584; -.
DR PharmGKB; PA36161; -.
DR VEuPathDB; HostDB:ENSG00000165584; -.
DR eggNOG; ENOG502RU1A; Eukaryota.
DR GeneTree; ENSGT00390000012484; -.
DR HOGENOM; CLU_097196_1_0_1; -.
DR InParanoid; Q99909; -.
DR OMA; CGNEVER; -.
DR OrthoDB; 1270676at2759; -.
DR PhylomeDB; Q99909; -.
DR TreeFam; TF338517; -.
DR PathwayCommons; Q99909; -.
DR SignaLink; Q99909; -.
DR BioGRID-ORCS; 10214; 51 hits in 612 CRISPR screens.
DR ChiTaRS; SSX3; human.
DR GenomeRNAi; 10214; -.
DR Pharos; Q99909; Tdark.
DR PRO; PR:Q99909; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q99909; protein.
DR Bgee; ENSG00000165584; Expressed in buccal mucosa cell and 34 other tissues.
DR ExpressionAtlas; Q99909; baseline and differential.
DR Genevisible; Q99909; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR003655; aKRAB.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR028804; SSX.
DR InterPro; IPR019041; SSXRD_motif.
DR PANTHER; PTHR14112; PTHR14112; 1.
DR Pfam; PF09514; SSXRD; 1.
DR SMART; SM00349; KRAB; 1.
DR SUPFAM; SSF109640; SSF109640; 1.
DR PROSITE; PS50806; KRAB_RELATED; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..188
FT /note="Protein SSX3"
FT /id="PRO_0000181830"
FT DOMAIN 20..83
FT /note="KRAB-related"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00120"
FT REGION 113..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16385"
FT VAR_SEQ 157..188
FT /note="PKRGEHAWTHRLRERKQLVIYEEISDPEEDDE -> VLQRYCRFGSRPLQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042777"
FT CONFLICT 95
FT /note="Q -> L (in Ref. 1; AAB37436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21697 MW; 988294793159C36E CRC64;
MNGDDTFARR PTVGAQIPEK IQKAFDDIAK YFSKEEWEKM KVSEKIVYVY MKRKYEAMTK
LGFKAILPSF MRNKRVTDFQ GNDFDNDPNR GNQVQRPQMT FGRLQGIFPK IMPKKPAEEG
NVSKEVPEAS GPQNDGKQLC PPGKPTTSEK INMISGPKRG EHAWTHRLRE RKQLVIYEEI
SDPEEDDE
