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Q76I76 (SSH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase Slingshot homolog 2

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
SSH-like protein 2
Short name=SSH-2L
Short name=hSSH-2L
Gene names
Name:SSH2
Synonyms:KIAA1725, SSH2L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1423 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with filamentous actin. Ref.1

Subcellular location

Cytoplasmcytoskeleton.

Miscellaneous

Tyrosine phosphatase activity has not been demonstrated for this protein to date.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence AAH11636.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAL92027.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandActin-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

protein dephosphorylation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of actin polymerization or depolymerization

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of lamellipodium assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

actin binding

Inferred from direct assay Ref.1. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q76I76-1)

Also known as: L;

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: Q76I76-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MALVTVQRSP...EEECRSQPRS → MTLSTLARKR...VISQNAINQL
     179-195: SALQSLHKACEVARAHN → VDRDSRNKHCYVLLVEE
     196-1423: Missing.
Isoform 3 (identifier: Q76I76-3)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     179-195: SALQSLHKACEVARAHN → VDRDSRNKHCYVLLVEE
     196-1423: Missing.
Isoform 4 (identifier: Q76I76-4)

The sequence of this isoform differs from the canonical sequence as follows:
     449-449: S → R
     450-1423: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14231423Protein phosphatase Slingshot homolog 2
PRO_0000094843

Regions

Domain307 – 447141Tyrosine-protein phosphatase

Sites

Active site3921Phosphocysteine intermediate Ref.10

Amino acid modifications

Modified residue361Phosphoserine Ref.6
Modified residue4871Phosphoserine Ref.8
Modified residue14221Phosphothreonine Ref.6 Ref.8

Natural variations

Alternative sequence1 – 3636MALVT…SQPRS → MTLSTLARKRKAPLACTCSL GGPDMIPYFSANAVISQNAI NQL in isoform 2.
VSP_016321
Alternative sequence179 – 19517SALQS…ARAHN → VDRDSRNKHCYVLLVEE in isoform 2 and isoform 3.
VSP_016322
Alternative sequence196 – 14231228Missing in isoform 2 and isoform 3.
VSP_016323
Alternative sequence4491S → R in isoform 4.
VSP_016324
Alternative sequence450 – 1423974Missing in isoform 4.
VSP_016325
Natural variant7431S → L.
Corresponds to variant rs2289629 [ dbSNP | Ensembl ].
VAR_051758
Natural variant7631V → A.
Corresponds to variant rs6505140 [ dbSNP | Ensembl ].
VAR_051759
Natural variant13001H → Q.
Corresponds to variant rs8080046 [ dbSNP | Ensembl ].
VAR_051760

Experimental info

Mutagenesis3921C → S: Abrogates phosphatase activity. Ref.1

Secondary structure

........................... 1423
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (L) [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 23D0B59C97D6BE38

FASTA1,423158,216
        10         20         30         40         50         60 
MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF LPRGNGSSTP 

        70         80         90        100        110        120 
RISHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY QNRTRYMVVV STNGRQDTEE 

       130        140        150        160        170        180 
SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI HLDGDGGFSV STDNRVHIFK PVSVQAMWSA 

       190        200        210        220        230        240 
LQSLHKACEV ARAHNYYPGS LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF 

       250        260        270        280        290        300 
TDIPTERERT ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV 

       310        320        330        340        350        360 
ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG VFEYHNIRVY 

       370        380        390        400        410        420 
DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA STVIAYAMKE YGWNLDRAYD 

       430        440        450        460        470        480 
YVKERRTVTK PNPSFMRQLE EYQGILLASK QRHNKLWRSH SDSDLSDHHE PICKPGLELN 

       490        500        510        520        530        540 
KKDITTSADQ IAEVKTMESH PPIPPVFVEH MVPQDANQKG LCTKERMICL EFTSREFHAG 

       550        560        570        580        590        600 
QIEDELNLND INGCSSGCCL NESKFPLDNC HASKALIQPG HVPEMANKFP DLTVEDLETD 

       610        620        630        640        650        660 
ALKADMNVHL LPMEELTSPL KDPPMSPDPE SPSPQPSCQT EISDFSTDRI DFFSALEKFV 

       670        680        690        700        710        720 
ELSQETRSRS FSHSRMEELG GGRNESCRLS VVEVAPSKVT ADDQRSSSLS NTPHASEESS 

       730        740        750        760        770        780 
MDEEQSKAIS ELVSPDIFMQ SHSENAISVK EIVTEIESIS QGVGQIQLKG DILPNPCHTP 

       790        800        810        820        830        840 
KKNSIHELLL ERAQTPENKP GHMEQDEDSC TAQPELAKDS GMCNPEGCLT THSSIADLEE 

       850        860        870        880        890        900 
GEPAEGEQEL QGSGMHPGAK WYPGSVRRAT LEFEERLRQE QEHHGAAPTC TSLSTRKNSK 

       910        920        930        940        950        960 
NDSSVADLAP KGKSDEAPPE HSFVLKEPEM SKGKGKYSGS EAGSLSHSEQ NATVPAPRVL 

       970        980        990       1000       1010       1020 
EFDHLPDPQE GPGSDTGTQQ EGVLKDLRTV IPYQESETQA VPLPLPKRVE IIEYTHIVTS 

      1030       1040       1050       1060       1070       1080 
PNHTGPGSEI ATSEKSGEQG LRKVNMEKSV TVLCTLDENL NRTLDPNQVS LHPQVLPLPH 

      1090       1100       1110       1120       1130       1140 
SSSPEHNRPT DHPTSILSSP EDRGSSLSTA LETAAPFVSH TTHLLSASLD YLHPQTMVHL 

      1150       1160       1170       1180       1190       1200 
EGFTEQSSTT DEPSAEQVSW EESQESPLSS GSEVPYKDSQ LSSADLSLIS KLGDNTGELQ 

      1210       1220       1230       1240       1250       1260 
EKMDPLPVAC RLPHSSSSEN IKSLSHSPGV VKERAKEIES RVVFQAGLTK PSQMRRSASL 

      1270       1280       1290       1300       1310       1320 
AKLGYLDLCK DCLPEREPAS CESPHLKLLQ PFLRTDSGMH AMEDQESLEN PGAPHNPEPT 

      1330       1340       1350       1360       1370       1380 
KSFVEQLTTT ECIVQSKPVE RPLVQYAKEF GSSQQYLLPR AGLELTSSEG GLPVLQTQGL 

      1390       1400       1410       1420 
QCACPAPGLA VAPRQQHGRT HPLRRLKKAN DKKRTTNPFY NTM 

« Hide

Isoform 2 [UniParc].

Checksum: 027BBBE4C2D6FE7B
Show »

FASTA20222,470
Isoform 3 (A) [UniParc].

Checksum: 21EB60284CB3E961
Show »

FASTA19521,685
Isoform 4 [UniParc].

Checksum: AFD156098A92A04D
Show »

FASTA44951,492

References

« Hide 'large scale' references
[1]"Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin."
Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.
Cell 108:233-246(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, INTERACTION WITH ACTIN, MUTAGENESIS OF CYS-392.
[2]"Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin."
Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y., Niwa R., Uemura T., Mizuno K.
Genes Cells 8:811-824(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] (ISOFORMS 2 AND 3).
Tissue: Brain and Lung.
[4]"Identification of genes expressed during myocardial development."
Chan S.Y., Chan A.K.W., Cheung B.P.K., Liang Y., Leung M.P.
Chin. Med. J. 116:1329-1332(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 282-409 (ISOFORMS 1/4).
[5]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1423 (ISOFORM 1).
Tissue: Brain.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-1422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND THR-1422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Crystal structure of human slingshot phosphatase 2."
Jung S.K., Jeong D.G., Yoon T.S., Kim J.H., Ryu S.E., Kim S.J.
Proteins 68:408-412(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 305-448, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB072358 mRNA. Translation: BAB84117.1.
AB072359 mRNA. Translation: BAB84118.1.
AB099290 mRNA. Translation: BAC97813.1.
BC008941 mRNA. Translation: AAH08941.1.
BC011636 mRNA. Translation: AAH11636.2. Different initiation.
BC068223 mRNA. Translation: AAH68223.1.
AF484838 mRNA. Translation: AAL92027.1. Different initiation.
AB051512 mRNA. Translation: BAB21816.1.
CCDSCCDS11253.1. [Q76I76-1]
RefSeqNP_001269058.1. NM_001282129.1.
NP_001269059.1. NM_001282130.1.
NP_001269060.1. NM_001282131.1.
NP_203747.2. NM_033389.3. [Q76I76-1]
UniGeneHs.654754.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NT2X-ray2.10A/B/C305-449[»]
ProteinModelPortalQ76I76.
SMRQ76I76. Positions 307-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124548. 5 interactions.
STRING9606.ENSP00000269033.

PTM databases

PhosphoSiteQ76I76.

Polymorphism databases

DMDM74749833.

Proteomic databases

MaxQBQ76I76.
PaxDbQ76I76.
PRIDEQ76I76.

Protocols and materials databases

DNASU85464.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269033; ENSP00000269033; ENSG00000141298. [Q76I76-1]
GeneID85464.
KEGGhsa:85464.
UCSCuc002heo.1. human. [Q76I76-1]
uc002hep.1. human. [Q76I76-4]
uc002her.3. human. [Q76I76-3]

Organism-specific databases

CTD85464.
GeneCardsGC17M027952.
HGNCHGNC:30580. SSH2.
HPACAB017189.
MIM606779. gene.
neXtProtNX_Q76I76.
PharmGKBPA134861867.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOVERGENHBG094002.
InParanoidQ76I76.
KOK05766.
OrthoDBEOG7B8S33.
PhylomeDBQ76I76.
TreeFamTF319444.

Gene expression databases

ArrayExpressQ76I76.
BgeeQ76I76.
CleanExHS_SSH2.
GenevestigatorQ76I76.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
3.90.190.10. 1 hit.
InterProIPR014876. DEK_C.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR009057. Homeodomain-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSSH2. human.
EvolutionaryTraceQ76I76.
GeneWikiSSH2.
GenomeRNAi85464.
NextBio76121.
PROQ76I76.
SOURCESearch...

Entry information

Entry nameSSH2_HUMAN
AccessionPrimary (citable) accession number: Q76I76
Secondary accession number(s): Q8TDB5 expand/collapse secondary AC list , Q8WYL1, Q8WYL2, Q96F40, Q96H36, Q9C0D8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM