Q16385 (SSX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein SSX2

Alternative name(s):
Cancer/testis antigen 5.2
Short name=CT5.2
Synovial sarcoma, X breakpoint 2
Tumor antigen HOM-MEL-40

Gene names

Name:	SSX2
Synonyms:	SSX2A
AND
Name:	SSX2B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could act as a modulator of transcription.
Subunit structure	Interacts via its N-terminal region with RAB3IP and SSX2IP. Ref.7
Subcellular location	Nucleus.
Tissue specificity	Expressed at high level in the testis. Expressed at low level in thyroid. Not detected in tonsil, colon, lung, spleen, prostate, kidney, striated and smooth muscles. Detected in rhabdomyosarcoma and fibrosarcoma cell lines. Not detected in mesenchymal and epithelial cell lines.
Involvement in disease	Note=A chromosomal aberration involving SSX2 may be a cause of synovial sarcoma. Translocation t(X;18)(p11.2;q11.2). The translocation is specifically found in more than 80% of synovial sarcoma. The fusion products SSXT-SSX1 or SSXT-SSX2 are probably responsible for transforming activity. Heterogeneity in the position of the breakpoint can occur (low frequency).
Sequence similarities	Belongs to the SSX family. Contains 1 KRAB-related domain.
Sequence caution	The sequence AAB35674.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Non-traceable author statement Ref.1. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: LIFEdb
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAB3IP	Q96QF0-2	4	EBI-2210673,EBI-747865
SSX2IP	Q9Y2D8	5	EBI-2210673,EBI-2212028

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16385-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q16385-2)

The sequence of this isoform differs from the canonical sequence as follows:
     157-188: PKRGEHAWTHRLRERKQLVIYEEISDPEEDDE → NREAQEKEER...PTDCVRENSW

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 188	188	Protein SSX2		PRO_0000181829
Regions
	Domain	20 – 83	64	KRAB-related
	Region	1 – 80	80	Interaction with SSX2IP
	Region	25 – 80	56	Interaction with RAB3IP
Sites
	Site	68 – 69	2	Breakpoint for translocation to form the SSXT-SSX2 fusion protein (rare)
	Site	110 – 111	2	Breakpoint for translocation to form the SSXT-SSX2 fusion protein
Natural variations
	Alternative sequence	157 – 188	32	PKRGE…EEDDE → NREAQEKEERRGTAHRWSSQ NTHNIGRFSLSTSMGAVHGT PKTITHNRDPKGGNMPGPTD CVRENSW in isoform 2.		VSP_017595
Experimental info
	Sequence conflict	169	1	R → P in AAH07343. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: BF5D18AA5F45B1B1	FASTA	188	21,620
	10 20 30 40 50 60 MNGDDAFARR PTVGAQIPEK IQKAFDDIAK YFSKEEWEKM KASEKIFYVY MKRKYEAMTK 70 80 90 100 110 120 LGFKATLPPF MCNKRAEDFQ GNDLDNDPNR GNQVERPQMT FGRLQGISPK IMPKKPAEEG 130 140 150 160 170 180 NDSEEVPEAS GPQNDGKELC PPGKPTTSEK IHERSGPKRG EHAWTHRLRE RKQLVIYEEI SDPEEDDE
	Isoform 2 [UniParc]. Checksum: 2BF8E1FFA4D58094	FASTA	223	25,173
	10 20 30 40 50 60 MNGDDAFARR PTVGAQIPEK IQKAFDDIAK YFSKEEWEKM KASEKIFYVY MKRKYEAMTK 70 80 90 100 110 120 LGFKATLPPF MCNKRAEDFQ GNDLDNDPNR GNQVERPQMT FGRLQGISPK IMPKKPAEEG 130 140 150 160 170 180 NDSEEVPEAS GPQNDGKELC PPGKPTTSEK IHERSGNREA QEKEERRGTA HRWSSQNTHN 190 200 210 220 IGRFSLSTSM GAVHGTPKTI THNRDPKGGN MPGPTDCVRE NSW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fusion of SYT to two genes, SSX1 and SSX2, encoding proteins with homology to the Kruppel-associated box in human synovial sarcoma." Crew A.J., Clark J., Fisher C., Gill S., Grimer R., Chand A., Shipley J., Gusterson B.A., Cooper C.S. EMBO J. 14:2333-2340(1995) [PubMed: 7539744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Placenta and Skin.
[4]	"Identification of two alternative fusion genes, SYT-SSX1 and SYT-SSX2, in t(X;18)(p11.2;q11.2)-positive synovial sarcomas." de Leeuw B., Balemans M., Olde Weghuis D., Geurts van Kessel A. Hum. Mol. Genet. 4:1097-1099(1995) [PubMed: 7655467] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-188 (ISOFORM 1). Tissue: Synovial sarcoma.
[5]	"Identification of novel genes, SYT and SSX, involved in the t(X;18)(p11.2;q11.2) translocation found in human synovial sarcoma." Clark J., Rocques P.J., Crew A.J., Gill S., Shipley J., Chan A.M.-L., Gusterson B.A., Cooper C.S. Nat. Genet. 7:502-508(1994) [PubMed: 7951320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-188 (SSXT-SSX2 FUSION PROTEIN). Tissue: Synovial sarcoma.
[6]	"Molecular diagnosis of synovial sarcoma and characterization of a variant SYT-SSX2 fusion transcript." Fligman I., Lonardo F., Jhanwar S.C., Gerald W.L., Woodruff J., Ladanyi M. Am. J. Pathol. 147:1592-1599(1995) [PubMed: 7495284] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-116 (SSXT-SSX2 FUSION PROTEIN).
[7]	"The cancer-related protein SSX2 interacts with the human homologue of a Ras-like GTPase interactor, RAB3IP, and a novel nuclear protein, SSX2IP." de Bruijn D.R.H., dos Santos N.R., Kater-Baats E., Thijssen J., van den Berk L., Stap J., Balemans M., Schepens M., Merkx G., van Kessel A.G. Genes Chromosomes Cancer 34:285-298(2002) [PubMed: 12007189] [Abstract] Cited for: INTERACTION WITH RAB3IP AND SSX2IP.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X86175 mRNA. Translation: CAA60111.1. AL450023 Genomic DNA. Translation: CAI41151.1. AL450023 Genomic DNA. Translation: CAI41152.1. AL445236, AL450023 Genomic DNA. Translation: CAI41623.1. AL445236, AL450023 Genomic DNA. Translation: CAI41624.1. AL450023, AL445236 Genomic DNA. Translation: CAI41157.1. AL450023, AL445236 Genomic DNA. Translation: CAI41158.1. BC002818 mRNA. Translation: AAH02818.1. BC007343 mRNA. Translation: AAH07343.1. BC016957 mRNA. Translation: AAH16957.1. BC069313 mRNA. Translation: AAH69313.1. BC071827 mRNA. Translation: AAH71827.1. BC103863 mRNA. Translation: AAI03864.1. S79332 mRNA. Translation: AAB35379.1. X79200 mRNA. No translation available. S79894 mRNA. Translation: AAB35674.1. Different initiation.
IPI	IPI00001520. IPI00305877.
PIR	S55058.
RefSeq	NP_001157889.1. NM_001164417.1. NP_003138.3. NM_003147.4. NP_783629.1. NM_175698.1.
UniGene	Hs.289105. Hs.661107.
3D structure databases
ProteinModelPortal	Q16385.
SMR	Q16385. Positions 20-70.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16385. 3 interactions.
STRING	Q16385.
Proteomic databases
PRIDE	Q16385.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000337502; ENSP00000338561; ENSG00000241476. ENST00000375515; ENSP00000364665; ENSG00000157950. ENST00000412682; ENSP00000406899; ENSG00000157950. ENST00000447152; ENSP00000397051; ENSG00000157950.
GeneID	6757. 727837.
KEGG	hsa:6757. hsa:727837.
UCSC	uc004dqz.1. human.
Organism-specific databases
CTD	6757. 727837.
GeneCards	GC0XM052725. GC0XP052797.
HGNC	HGNC:11336. SSX2. HGNC:22263. SSX2B.
MIM	300192. gene.
neXtProt	NX_Q16385.
Orphanet	3273. Synovialosarcoma.
PharmGKB	PA162404839.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000012484.
HOVERGEN	HBG002056.
OMA	NTHNIGR.
OrthoDB	EOG4G4GRJ.
Gene expression databases
ArrayExpress	Q16385.
Bgee	Q16385.
CleanEx	HS_SSX2.
Genevestigator	Q16385.
GermOnline	ENSG00000187754. Homo sapiens.
Family and domain databases
InterPro	IPR001909. Krueppel-associated_box. IPR003655. Krueppel-associated_box-rel. IPR019041. SSXRD_motif. [Graphical view]
KO	K15625.
Pfam	PF01352. KRAB. 1 hit. PF09514. SSXRD. 1 hit. [Graphical view]
SMART	SM00349. KRAB. 1 hit. [Graphical view]
SUPFAM	SSF109640. Krueppel-associated_box. 1 hit.
PROSITE	PS50806. KRAB_RELATED. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	26362.
SOURCE	Search...

Entry information

Entry name

SSX2_HUMAN

Accession

Primary (citable) accession number: Q16385
Secondary accession number(s): Q16404 , Q5JS26, Q96IP7, Q9BU88

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	January 25, 2012
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.