Q76I76 · SSH2_HUMAN
- ProteinProtein phosphatase Slingshot homolog 2
- GeneSSH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1423 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for spermatogenesis (By similarity).
Involved in acrosome biogenesis, probably by regulating cofilin-mediated actin cytoskeleton remodeling during proacrosomal vesicle fusion and/or Golgi to perinuclear vesicle trafficking (By similarity).
Miscellaneous
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 392 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | acrosomal vesicle | |
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | extracellular space | |
Cellular Component | focal adhesion | |
Molecular Function | actin binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | actin cytoskeleton organization | |
Biological Process | cell differentiation | |
Biological Process | negative regulation of actin filament polymerization | |
Biological Process | protein dephosphorylation | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein phosphatase Slingshot homolog 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ76I76
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 392 | Abrogates phosphatase activity. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_051758 | 743 | in dbSNP:rs2289629 | |||
Sequence: S → L | ||||||
Natural variant | VAR_051759 | 763 | in dbSNP:rs6505140 | |||
Sequence: V → A | ||||||
Natural variant | VAR_051760 | 1300 | in dbSNP:rs8080046 | |||
Sequence: H → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,510 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000094843 | 1-1423 | UniProt | Protein phosphatase Slingshot homolog 2 | |||
Sequence: MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRISHRRNKHAGDLQQHLQAMFILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSSTCTMGLVLPLWSDTLIHLDGDGGFSVSTDNRVHIFKPVSVQAMWSALQSLHKACEVARAHNYYPGSLFLTWVSYYESHINSDQSSVNEWNAMQDVQSHRPDSPALFTDIPTERERTERLIKTKLREIMMQKDLENITSKEIRTELEMQMVCNLREFKEFIDNEMIVILGQMDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGILLASKQRHNKLWRSHSDSDLSDHHEPICKPGLELNKKDITTSADQIAEVKTMESHPPIPPVFVEHMVPQDANQKGLCTKERMICLEFTSREFHAGQIEDELNLNDINGCSSGCCLNESKFPLDNCHASKALIQPGHVPEMANKFPDLTVEDLETDALKADMNVHLLPMEELTSPLKDPPMSPDPESPSPQPSCQTEISDFSTDRIDFFSALEKFVELSQETRSRSFSHSRMEELGGGRNESCRLSVVEVAPSKVTADDQRSSSLSNTPHASEESSMDEEQSKAISELVSPDIFMQSHSENAISVKEIVTEIESISQGVGQIQLKGDILPNPCHTPKKNSIHELLLERAQTPENKPGHMEQDEDSCTAQPELAKDSGMCNPEGCLTTHSSIADLEEGEPAEGEQELQGSGMHPGAKWYPGSVRRATLEFEERLRQEQEHHGAAPTCTSLSTRKNSKNDSSVADLAPKGKSDEAPPEHSFVLKEPEMSKGKGKYSGSEAGSLSHSEQNATVPAPRVLEFDHLPDPQEGPGSDTGTQQEGVLKDLRTVIPYQESETQAVPLPLPKRVEIIEYTHIVTSPNHTGPGSEIATSEKSGEQGLRKVNMEKSVTVLCTLDENLNRTLDPNQVSLHPQVLPLPHSSSPEHNRPTDHPTSILSSPEDRGSSLSTALETAAPFVSHTTHLLSASLDYLHPQTMVHLEGFTEQSSTTDEPSAEQVSWEESQESPLSSGSEVPYKDSQLSSADLSLISKLGDNTGELQEKMDPLPVACRLPHSSSSENIKSLSHSPGVVKERAKEIESRVVFQAGLTKPSQMRRSASLAKLGYLDLCKDCLPEREPASCESPHLKLLQPFLRTDSGMHAMEDQESLENPGAPHNPEPTKSFVEQLTTTECIVQSKPVERPLVQYAKEFGSSQQYLLPRAGLELTSSEGGLPVLQTQGLQCACPAPGLAVAPRQQHGRTHPLRRLKKANDKKRTTNPFYNTM | |||||||
Modified residue | 17 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 25 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 36 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 40 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 461 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 461 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 463 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 466 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 486 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 487 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 487 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 534 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 618 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 631 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 633 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 690 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 779 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 795 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 870 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1187 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1215 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1217 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1217 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1218 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1422 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1422 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q76I76 | HECTD1 Q9ULT8 | 2 | EBI-10977847, EBI-310559 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MALVTVQRSPTPSTTSSPCASE | ||||||
Region | 1-37 | Disordered | ||||
Sequence: MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRSI | ||||||
Domain | 248-303 | DEK-C | ||||
Sequence: ERTERLIKTKLREIMMQKDLENITSKEIRTELEMQMVCNLREFKEFIDNEMIVILG | ||||||
Domain | 307-448 | Tyrosine-protein phosphatase | ||||
Sequence: SPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGILLA | ||||||
Region | 617-641 | Disordered | ||||
Sequence: TSPLKDPPMSPDPESPSPQPSCQTE | ||||||
Compositional bias | 664-682 | Basic and acidic residues | ||||
Sequence: QETRSRSFSHSRMEELGGG | ||||||
Region | 664-684 | Disordered | ||||
Sequence: QETRSRSFSHSRMEELGGGRN | ||||||
Region | 696-728 | Disordered | ||||
Sequence: PSKVTADDQRSSSLSNTPHASEESSMDEEQSKA | ||||||
Compositional bias | 700-716 | Polar residues | ||||
Sequence: TADDQRSSSLSNTPHAS | ||||||
Compositional bias | 797-813 | Basic and acidic residues | ||||
Sequence: ENKPGHMEQDEDSCTAQ | ||||||
Region | 797-825 | Disordered | ||||
Sequence: ENKPGHMEQDEDSCTAQPELAKDSGMCNP | ||||||
Region | 840-862 | Disordered | ||||
Sequence: EGEPAEGEQELQGSGMHPGAKWY | ||||||
Region | 877-954 | Disordered | ||||
Sequence: LRQEQEHHGAAPTCTSLSTRKNSKNDSSVADLAPKGKSDEAPPEHSFVLKEPEMSKGKGKYSGSEAGSLSHSEQNATV | ||||||
Compositional bias | 885-905 | Polar residues | ||||
Sequence: GAAPTCTSLSTRKNSKNDSSV | ||||||
Compositional bias | 913-934 | Basic and acidic residues | ||||
Sequence: KSDEAPPEHSFVLKEPEMSKGK | ||||||
Region | 962-981 | Disordered | ||||
Sequence: FDHLPDPQEGPGSDTGTQQE | ||||||
Compositional bias | 1019-1039 | Polar residues | ||||
Sequence: TSPNHTGPGSEIATSEKSGEQ | ||||||
Region | 1019-1041 | Disordered | ||||
Sequence: TSPNHTGPGSEIATSEKSGEQGL | ||||||
Region | 1070-1108 | Disordered | ||||
Sequence: SLHPQVLPLPHSSSPEHNRPTDHPTSILSSPEDRGSSLS | ||||||
Region | 1144-1179 | Disordered | ||||
Sequence: TEQSSTTDEPSAEQVSWEESQESPLSSGSEVPYKDS |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q76I76-1
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.
- Name1
- SynonymsL
- Length1,423
- Mass (Da)158,216
- Last updated2004-07-05 v1
- Checksum23D0B59C97D6BE38
Q76I76-2
- Name2
Q76I76-3
- Name3
- SynonymsA
Q76I76-4
- Name4
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KSP5 | J3KSP5_HUMAN | SSH2 | 48 | ||
J3KSQ9 | J3KSQ9_HUMAN | SSH2 | 112 | ||
A0A3B3IS79 | A0A3B3IS79_HUMAN | SSH2 | 1429 | ||
A0A3B3ITS1 | A0A3B3ITS1_HUMAN | SSH2 | 202 | ||
K7EKN7 | K7EKN7_HUMAN | SSH2 | 116 | ||
K7EP00 | K7EP00_HUMAN | SSH2 | 120 | ||
K7EQZ0 | K7EQZ0_HUMAN | SSH2 | 42 | ||
F5H527 | F5H527_HUMAN | SSH2 | 1450 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MALVTVQRSPTPSTTSSPCASE | ||||||
Alternative sequence | VSP_016321 | 1-36 | in isoform 2 | |||
Sequence: MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRS → MTLSTLARKRKAPLACTCSLGGPDMIPYFSANAVISQNAINQL | ||||||
Alternative sequence | VSP_016322 | 179-195 | in isoform 2 and isoform 3 | |||
Sequence: SALQSLHKACEVARAHN → VDRDSRNKHCYVLLVEE | ||||||
Alternative sequence | VSP_016323 | 196-1423 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_016324 | 449 | in isoform 4 | |||
Sequence: S → R | ||||||
Alternative sequence | VSP_016325 | 450-1423 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 664-682 | Basic and acidic residues | ||||
Sequence: QETRSRSFSHSRMEELGGG | ||||||
Compositional bias | 700-716 | Polar residues | ||||
Sequence: TADDQRSSSLSNTPHAS | ||||||
Compositional bias | 797-813 | Basic and acidic residues | ||||
Sequence: ENKPGHMEQDEDSCTAQ | ||||||
Compositional bias | 885-905 | Polar residues | ||||
Sequence: GAAPTCTSLSTRKNSKNDSSV | ||||||
Compositional bias | 913-934 | Basic and acidic residues | ||||
Sequence: KSDEAPPEHSFVLKEPEMSKGK | ||||||
Compositional bias | 1019-1039 | Polar residues | ||||
Sequence: TSPNHTGPGSEIATSEKSGEQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB072358 EMBL· GenBank· DDBJ | BAB84117.1 EMBL· GenBank· DDBJ | mRNA | ||
AB072359 EMBL· GenBank· DDBJ | BAB84118.1 EMBL· GenBank· DDBJ | mRNA | ||
AB099290 EMBL· GenBank· DDBJ | BAC97813.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008941 EMBL· GenBank· DDBJ | AAH08941.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011636 EMBL· GenBank· DDBJ | AAH11636.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC068223 EMBL· GenBank· DDBJ | AAH68223.1 EMBL· GenBank· DDBJ | mRNA | ||
AF484838 EMBL· GenBank· DDBJ | AAL92027.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB051512 EMBL· GenBank· DDBJ | BAB21816.1 EMBL· GenBank· DDBJ | mRNA |