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Protein

Protein SSX1

Gene

SSX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Could act as a modulator of transcription.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei62 – 632Breakpoint for translocation to form the SSXT-SSX1 fusion protein (rare)
Sitei110 – 1112Breakpoint for translocation to form the SSXT-SSX1 fusion protein

GO - Molecular functioni

  • nucleic acid binding Source: InterPro
  • transcription corepressor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SSX1
Alternative name(s):
Cancer/testis antigen 5.1
Short name:
CT5.1
Synovial sarcoma, X breakpoint 1
Gene namesi
Name:SSX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11335. SSX1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving SSX1 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).

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MIMi312820. gene+phenotype.
Orphaneti3273. Synovial sarcoma.
PharmGKBiPA36159.

Polymorphism and mutation databases

BioMutaiSSX1.
DMDMi3915027.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Protein SSX1PRO_0000181828Add
BLAST

Proteomic databases

PaxDbiQ16384.
PRIDEiQ16384.

PTM databases

PhosphoSiteiQ16384.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ16384.
CleanExiHS_SSX1.
GenevisibleiQ16384. HS.

Organism-specific databases

HPAiHPA045683.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEC2Q9UBF13EBI-10237585,EBI-5651487

Protein-protein interaction databases

BioGridi112634. 3 interactions.
IntActiQ16384. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ16384.
SMRiQ16384. Positions 19-70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 8364KRAB-relatedPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the SSX family.Curated
Contains 1 KRAB-related domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG147011.
GeneTreeiENSGT00390000012484.
HOGENOMiHOG000231461.
HOVERGENiHBG002056.
InParanoidiQ16384.
KOiK15624.
OMAiSDNDRNH.
OrthoDBiEOG7DNNX1.
PhylomeDBiQ16384.
TreeFamiTF338517.

Family and domain databases

InterProiIPR001909. Krueppel-associated_box.
IPR003655. Krueppel-associated_box-rel.
IPR028804. SSX.
IPR019041. SSXRD_motif.
[Graphical view]
PANTHERiPTHR14112. PTHR14112. 1 hit.
PfamiPF09514. SSXRD. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50806. KRAB_RELATED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGDDTFAKR PRDDAKASEK RSKAFDDIAT YFSKKEWKKM KYSEKISYVY
60 70 80 90 100
MKRNYKAMTK LGFKVTLPPF MCNKQATDFQ GNDFDNDHNR RIQVEHPQMT
110 120 130 140 150
FGRLHRIIPK IMPKKPAEDE NDSKGVSEAS GPQNDGKQLH PPGKANISEK
160 170 180
INKRSGPKRG KHAWTHRLRE RKQLVIYEEI SDPEEDDE
Length:188
Mass (Da):21,931
Last modified:December 15, 1998 - v2
Checksum:iE440D1B2AE3AE9F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86174 mRNA. Translation: CAA60110.1.
AL683817 Genomic DNA. Translation: CAI41141.1.
BC001003 mRNA. Translation: AAH01003.1.
BC125151 mRNA. Translation: AAI25152.1.
BC128611 mRNA. Translation: AAI28612.1.
BC133693 mRNA. Translation: AAI33694.1.
BC150487 mRNA. Translation: AAI50488.1.
S79325 mRNA. Translation: AAB35378.1.
CCDSiCCDS14290.1.
PIRiS55057.
RefSeqiNP_001265620.1. NM_001278691.1.
NP_005626.1. NM_005635.3.
UniGeneiHs.434142.

Genome annotation databases

EnsembliENST00000376919; ENSP00000366118; ENSG00000126752.
GeneIDi6756.
KEGGihsa:6756.
UCSCiuc004djb.1. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86174 mRNA. Translation: CAA60110.1.
AL683817 Genomic DNA. Translation: CAI41141.1.
BC001003 mRNA. Translation: AAH01003.1.
BC125151 mRNA. Translation: AAI25152.1.
BC128611 mRNA. Translation: AAI28612.1.
BC133693 mRNA. Translation: AAI33694.1.
BC150487 mRNA. Translation: AAI50488.1.
S79325 mRNA. Translation: AAB35378.1.
CCDSiCCDS14290.1.
PIRiS55057.
RefSeqiNP_001265620.1. NM_001278691.1.
NP_005626.1. NM_005635.3.
UniGeneiHs.434142.

3D structure databases

ProteinModelPortaliQ16384.
SMRiQ16384. Positions 19-70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112634. 3 interactions.
IntActiQ16384. 1 interaction.

PTM databases

PhosphoSiteiQ16384.

Polymorphism and mutation databases

BioMutaiSSX1.
DMDMi3915027.

Proteomic databases

PaxDbiQ16384.
PRIDEiQ16384.

Protocols and materials databases

DNASUi6756.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376919; ENSP00000366118; ENSG00000126752.
GeneIDi6756.
KEGGihsa:6756.
UCSCiuc004djb.1. human.

Organism-specific databases

CTDi6756.
GeneCardsiGC0XP048114.
HGNCiHGNC:11335. SSX1.
HPAiHPA045683.
MIMi312820. gene+phenotype.
neXtProtiNX_Q16384.
Orphaneti3273. Synovial sarcoma.
PharmGKBiPA36159.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG147011.
GeneTreeiENSGT00390000012484.
HOGENOMiHOG000231461.
HOVERGENiHBG002056.
InParanoidiQ16384.
KOiK15624.
OMAiSDNDRNH.
OrthoDBiEOG7DNNX1.
PhylomeDBiQ16384.
TreeFamiTF338517.

Miscellaneous databases

ChiTaRSiSSX1. human.
GeneWikiiSSX1.
GenomeRNAii6756.
NextBioi26356.
PROiQ16384.
SOURCEiSearch...

Gene expression databases

BgeeiQ16384.
CleanExiHS_SSX1.
GenevisibleiQ16384. HS.

Family and domain databases

InterProiIPR001909. Krueppel-associated_box.
IPR003655. Krueppel-associated_box-rel.
IPR028804. SSX.
IPR019041. SSXRD_motif.
[Graphical view]
PANTHERiPTHR14112. PTHR14112. 1 hit.
PfamiPF09514. SSXRD. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50806. KRAB_RELATED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibrosarcoma.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-188.
    Tissue: Synovial sarcoma.

Entry informationi

Entry nameiSSX1_HUMAN
AccessioniPrimary (citable) accession number: Q16384
Secondary accession number(s): A3KN76, Q08AJ2, Q5JQ64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: July 22, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.