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Q8WYL5 (SSH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase Slingshot homolog 1

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
SSH-like protein 1
Short name=SSH-1L
Short name=hSSH-1L
Gene names
Name:SSH1
Synonyms:KIAA1298, SSH1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1049 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Interacts with actin and this stimulates phosphatase activity. Also interacts with LIMK1 and with the 14-3-3 proteins YWHAB, YWHAG, YWHAQ, and YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase activity and also blocks recruitment to lamellipodia and stimulation by actin. Ref.1 Ref.5 Ref.10 Ref.11

Subcellular location

Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cleavage furrow. Midbody. Note: Also recruited to actin rich membrane protrusions such as lamellipodia, which may allow local control of actin dynamics at sites of cell locomotion. Also localized to the cleavage furrow and the midbody during cytokinesis. Ref.6 Ref.8 Ref.9 Ref.10 Ref.13

Post-translational modification

Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-978 is decreased by stimuli which promote actin reorganization and lamellipodia formation. Can be dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation decreases immediately prior to telophase. Ref.6 Ref.10 Ref.11 Ref.12

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 BAA92536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

cell morphogenesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cellular response to ATP

Inferred from direct assay PubMed 19000834. Source: MGI

protein dephosphorylation

Inferred from mutant phenotype Ref.1Ref.9. 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 cellular protein metabolic process

Inferred from direct assay PubMed 19000834. Source: MGI

regulation of lamellipodium assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   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 binding

Inferred from physical interaction Ref.10Ref.11PubMed 17350576PubMed 19329994PubMed 19371722PubMed 21525957. Source: IntAct

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 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WYL5-1)

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: Q8WYL5-2)

Also known as: S;

The sequence of this isoform differs from the canonical sequence as follows:
     632-692: DDAIFGILNK...LPHITSSPVA → VGRARPAGWH...LQGPEGSFTG
     693-1049: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: Q8WYL5-3)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
     74-93: LPQHLQVMINLLRCEDRIKL → MGGRHHLQRQVSESMSALFQ
     135-157: Missing.
     245-1049: Missing.
Note: Due to intron retention. No experimental confirmation available.
Isoform 4 (identifier: Q8WYL5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-312: Missing.
     313-334: FDHLYLGSEWNASNLEELQGSG → MRCYLSWDRWTSPPLSSIIFIS
Isoform 5 (identifier: Q8WYL5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MALVTLQRSP...SEEDRKLNLS → MARARRAVVG...CCPEVSSSNY
     632-692: DDAIFGILNK...LPHITSSPVA → VGRARPAGWH...LQGPEGSFTG
     693-1049: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 10491048Protein phosphatase Slingshot homolog 1
PRO_0000094841

Regions

Domain308 – 448141Tyrosine-protein phosphatase
Region897 – 1049153Interaction with YWHAG

Sites

Active site3931Phosphocysteine intermediate Probable

Amino acid modifications

Modified residue21N-acetylalanine Ref.15
Modified residue371Phosphoserine Ref.16
Modified residue571Phosphoserine Ref.16
Modified residue9781Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 312312Missing in isoform 4.
VSP_016311
Alternative sequence1 – 7373Missing in isoform 3.
VSP_016312
Alternative sequence1 – 3737MALVT…KLNLS → MARARRAVVGSVRDVSTAAT NLFYFTDFCIFLQPTHCFCC PEVSSSNY in isoform 5.
VSP_016313
Alternative sequence74 – 9320LPQHL…DRIKL → MGGRHHLQRQVSESMSALFQ in isoform 3.
VSP_016314
Alternative sequence135 – 15723Missing in isoform 3.
VSP_016315
Alternative sequence245 – 1049805Missing in isoform 3.
VSP_016316
Alternative sequence313 – 33422FDHLY…LQGSG → MRCYLSWDRWTSPPLSSIIF IS in isoform 4.
VSP_016317
Alternative sequence632 – 69261DDAIF…SSPVA → VGRARPAGWHTPSLPSHSNW PTSASVVGTTGTRHHTQLIF FYCLLWAPSSHLQGPEGSFT G in isoform 2 and isoform 5.
VSP_016318
Alternative sequence693 – 1049357Missing in isoform 2 and isoform 5.
VSP_016319

Experimental info

Mutagenesis3931C → S: Abrogates phosphatase activity. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13
Mutagenesis4581W → A: Impairs stimulation of phosphatase activity by actin but does not affect basal activity. Ref.13
Mutagenesis9371S → A: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-978. Ref.10
Mutagenesis9781S → A: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-937. Ref.10
Sequence conflict21A → V in AAH62341. Ref.4
Sequence conflict2301L → P in BAB84116. Ref.1

Sequences

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

Last modified November 22, 2005. Version 2.
Checksum: 0600B9690F0E6F9C

FASTA1,049115,511
        10         20         30         40         50         60 
MALVTLQRSP TPSAASSSAS NSELEAGSEE DRKLNLSLSE SFFMVKGAAL FLQQGSSPQG 

        70         80         90        100        110        120 
QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESA WADRVRYMVV VYSSGRQDTE 

       130        140        150        160        170        180 
ENILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS 

       190        200        210        220        230        240 
ALQVLHKACE VARRHNYFPG GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL 

       250        260        270        280        290        300 
FVDKPTEGER TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE LKEFIDNEML 

       310        320        330        340        350        360 
LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP GLFAYHNIRV 

       370        380        390        400        410        420 
YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS ASTVIAYAMK EFGWPLEKAY 

       430        440        450        460        470        480 
NYVKQKRSIT RPNAGFMRQL SEYEGILDAS KQRHNKLWRQ QTDSSLQQPV DDPAGPGDFL 

       490        500        510        520        530        540 
PETPDGTPES QLPFLDDAAQ PGLGPPLPCC FRRLSDPLLP SPEDETGSLV HLEDPEREAL 

       550        560        570        580        590        600 
LEEAAPPAEV HRPARQPQQG SGLCEKDVKK KLEFGSPKGR SGSLLQVEET EREEGLGAGR 

       610        620        630        640        650        660 
WGQLPTQLDQ NLLNSENLNN NSKRSCPNGM EDDAIFGILN KVKPSYKSCA DCMYPTASGA 

       670        680        690        700        710        720 
PEASRERCED PNAPAICTQP AFLPHITSSP VAHLASRSRV PEKPASGPTE PPPFLPPAGS 

       730        740        750        760        770        780 
RRADTSGPGA GAALEPPASL LEPSRETPKV LPKSLLLKNS HCDKNPPSTE VVIKEESSPK 

       790        800        810        820        830        840 
KDMKPAKDLR LLFSNESEKP TTNSYLMQHQ ESIIQLQKAG LVRKHTKELE RLKSVPADPA 

       850        860        870        880        890        900 
PPSRDGPASR LEASIPEESQ DPAALHELGP LVMPSQAGSD EKSEAAPASL EGGSLKSPPP 

       910        920        930        940        950        960 
FFYRLDHTSS FSKDFLKTIC YTPTSSSMSS NLTRSSSSDS IHSVRGKPGL VKQRTQEIET 

       970        980        990       1000       1010       1020 
RLRLAGLTVS SPLKRSHSLA KLGSLTFSTE DLSSEADPST VADSQDTTLS ESSFLHEPQG 

      1030       1040 
TPRDPAATSK PSGKPAPENL KSPSWMSKS 

« Hide

Isoform 2 (S) [UniParc].

Checksum: 9DC1FF2FC8984384
Show »

FASTA69277,430
Isoform 3 (B) [UniParc].

Checksum: 3EF171D933E3424D
Show »

FASTA14816,695
Isoform 4 [UniParc].

Checksum: E3825E2328B088D2
Show »

FASTA73780,684
Isoform 5 [UniParc].

Checksum: 3ACFAB4B97CBDF7A
Show »

FASTA70378,978

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 1; 2 AND 3), FUNCTION, INTERACTION WITH ACTIN, MUTAGENESIS OF CYS-393.
[2]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[4]"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] (ISOFORM 1).
Tissue: Eye.
[5]"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: FUNCTION, INTERACTION WITH ACTIN.
[6]"Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells."
Kaji N., Ohashi K., Shuin M., Niwa R., Uemura T., Mizuno K.
J. Biol. Chem. 278:33450-33455(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF CYS-393.
[7]"Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin."
Endo M., Ohashi K., Sasaki Y., Goshima Y., Niwa R., Uemura T., Mizuno K.
J. Neurosci. 23:2527-2537(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-393.
[8]"Efficient Salmonella entry requires activity cycles of host ADF and cofilin."
Dai S., Sarmiere P.D., Wiggan O., Bamburg J.R., Zhou D.
Cell. Microbiol. 6:459-471(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-393.
[9]"Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion."
Nishita M., Wang Y., Tomizawa C., Suzuki A., Niwa R., Uemura T., Mizuno K.
J. Biol. Chem. 279:7193-7198(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia."
Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.
J. Cell Biol. 165:465-471(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH YWHAB; YWHAG; YWHAQ AND YWHAZ, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-978, MUTAGENESIS OF CYS-393; SER-937 AND SER-978.
[11]"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACTIN; LIMK1 AND YWHAZ, PHOSPHORYLATION, MUTAGENESIS OF CYS-393.
[12]"Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin."
Wang Y., Shibasaki F., Mizuno K.
J. Biol. Chem. 280:12683-12689(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION BY PPP3CA, MUTAGENESIS OF CYS-393.
[13]"Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration."
Nishita M., Tomizawa C., Yamamoto M., Horita Y., Ohashi K., Mizuno K.
J. Cell Biol. 171:349-359(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-393 AND TRP-458.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB072355 mRNA. Translation: BAB84114.1.
AB072356 mRNA. Translation: BAB84115.1.
AB072357 mRNA. Translation: BAB84116.1.
AB037719 mRNA. Translation: BAA92536.1. Different initiation.
AK095421 mRNA. Translation: BAC04546.1.
BC062341 mRNA. Translation: AAH62341.1.
CCDSCCDS53825.1. [Q8WYL5-5]
CCDS55882.1. [Q8WYL5-2]
CCDS9121.1. [Q8WYL5-1]
RefSeqNP_001154802.1. NM_001161330.1. [Q8WYL5-2]
NP_001154803.1. NM_001161331.1. [Q8WYL5-5]
NP_061857.3. NM_018984.3. [Q8WYL5-1]
XP_005269043.1. XM_005268986.1. [Q8WYL5-4]
UniGeneHs.199763.

3D structure databases

ProteinModelPortalQ8WYL5.
SMRQ8WYL5. Positions 309-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119950. 6 interactions.
IntActQ8WYL5. 12 interactions.
MINTMINT-1788740.
STRING9606.ENSP00000315713.

PTM databases

PhosphoSiteQ8WYL5.

Polymorphism databases

DMDM82582267.

Proteomic databases

MaxQBQ8WYL5.
PaxDbQ8WYL5.
PRIDEQ8WYL5.

Protocols and materials databases

DNASU54434.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326470; ENSP00000326107; ENSG00000084112. [Q8WYL5-5]
ENST00000326495; ENSP00000315713; ENSG00000084112. [Q8WYL5-1]
ENST00000360239; ENSP00000353374; ENSG00000084112. [Q8WYL5-4]
ENST00000551165; ENSP00000448824; ENSG00000084112. [Q8WYL5-2]
GeneID54434.
KEGGhsa:54434.
UCSCuc001tnl.3. human. [Q8WYL5-4]
uc001tnm.3. human. [Q8WYL5-1]
uc001tnn.4. human. [Q8WYL5-2]
uc001tno.1. human. [Q8WYL5-3]
uc010sxg.2. human. [Q8WYL5-5]

Organism-specific databases

CTD54434.
GeneCardsGC12M109180.
HGNCHGNC:30579. SSH1.
HPAHPA019845.
MIM606778. gene.
neXtProtNX_Q8WYL5.
PharmGKBPA134941788.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000154427.
HOVERGENHBG094001.
InParanoidQ8WYL5.
KOK05766.
OMANSHCDKN.
OrthoDBEOG7B8S33.
PhylomeDBQ8WYL5.
TreeFamTF319444.

Gene expression databases

ArrayExpressQ8WYL5.
BgeeQ8WYL5.
CleanExHS_SSH1.
GenevestigatorQ8WYL5.

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.
IPR027233. SSH1.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PTHR10159:SF138. PTHR10159:SF138. 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

GeneWikiSSH1.
GenomeRNAi54434.
NextBio56643.
PROQ8WYL5.
SOURCESearch...

Entry information

Entry nameSSH1_HUMAN
AccessionPrimary (citable) accession number: Q8WYL5
Secondary accession number(s): Q6P6C0 expand/collapse secondary AC list , Q8N9A7, Q8WYL3, Q8WYL4, Q9P2P8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: July 9, 2014
This is version 115 of the entry and version 2 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

MIM cross-references

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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM