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Q5SW75

- SSH2_MOUSE

UniProt

Q5SW75 - SSH2_MOUSE

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Protein
Protein phosphatase Slingshot homolog 2
Gene
Ssh2, Kiaa1725, Ssh2l
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei392 – 3921Phosphocysteine intermediate Inferred

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. actin binding Source: RefGenome
  3. protein tyrosine phosphatase activity Source: UniProtKB-EC
  4. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. protein dephosphorylation Source: RefGenome
  3. regulation of actin polymerization or depolymerization Source: RefGenome
  4. regulation of axonogenesis Source: RefGenome
  5. regulation of lamellipodium assembly Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended 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:
mSSH-2L
Gene namesi
Name:Ssh2
Synonyms:Kiaa1725, Ssh2l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2679255. Ssh2.

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctionfocal adhesion
Note: Colocalizes with filamentous actin in the cytoplasm and the cell periphery. Also localizes to focal adhesions.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytoskeleton Source: UniProtKB-SubCell
  3. focal adhesion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi392 – 3921C → S: Abrogates phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14231423Protein phosphatase Slingshot homolog 2
PRO_0000094844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361Phosphoserine By similarity
Modified residuei487 – 4871Phosphoserine By similarity
Modified residuei1422 – 14221Phosphothreonine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5SW75.
PRIDEiQ5SW75.

PTM databases

PhosphoSiteiQ5SW75.

Expressioni

Tissue specificityi

Expressed in brain, heart, liver, skeletal muscle, testis and thymus. Also expressed at lower levels in kidney, small intestine and spleen.1 Publication

Developmental stagei

Expressed in the nervous system at E14.5.1 Publication

Gene expression databases

BgeeiQ5SW75.
CleanExiMM_SSH2.
GenevestigatoriQ5SW75.

Interactioni

Subunit structurei

Interacts with filamentous actin.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000104034.

Structurei

3D structure databases

ProteinModelPortaliQ5SW75.
SMRiQ5SW75. Positions 307-448.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 447141Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00750000117282.
HOVERGENiHBG094002.
KOiK05766.
OrthoDBiEOG7B8S33.
PhylomeDBiQ5SW75.
TreeFamiTF319444.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR014876. 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]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5SW75-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF     50
LPRGNGSSTP RVSHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY 100
QNRTRYMVVV STNGRQDTEE SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI 150
HLDGDGGFSV STDNRVHIFK PVSVQAMWSA LQSLHKACEV ARMHNYYPGS 200
LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF TDIPTERERT 250
ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV 300
ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG 350
VFEYHNIRVY DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA 400
STVIAYAMKE YGWNLDRAYD YVKERRTVTK PNPSFMRQLE EYQGILLASK 450
QRHNKLWRSH SDSDLSDHHE PICKPGLELN KKEMTTSADQ IAEVKTVENL 500
AAMPTVFMEH VVPQDANQKG LHTKERVICL EFSSQEFRAG QIEDELNLND 550
INGCSSGCCL SESKLPLDNC HASKALLQPG QAPDIANKFP DLAVEDLETD 600
ALKADMNVHL LPMEELTSRL KDLPMSPDLE SPSPQASCQA AISDFSTDRI 650
DFFSALEKFV ELSQETRSRS FSHSRIEELG GGRSEGCRLS VIEVAASEMA 700
ADDQRSSSLS NTPHASEESS VDEDQSKAIT ELVSPDIIMQ SHSENAISVK 750
EIVTEIESIS QGVGQVQLKG DILSNPCHTP KKSTIHELPL ERVPAPESKP 800
GHWEQDESFC SVQPELARDS GKCAPEEGCL TTHSSTADLE EEEPVEGEHD 850
WGPGMHSGAK WCPGSVRRAT LEFEERLRQE QENHGTASAG PTLSNRKNSK 900
NDSSVADLMP KWKSDETTPE HSFFLKEAEP SKGKGKCSGS EAGSLSHCER 950
NPTMPDCELL EHHSLPAPQD CLGSDSRSKK QEGDLKKQRA VVPNQECDTQ 1000
AILLPLPKKI EIIEYTPTVT SLGHTEPGGE ATPSKEGEKQ GLRKVKMEQS 1050
ITMFCALDEN LNRTLEPSQV SLHPQVLPLP HSSSECDRPA DPNPMLSSPQ 1100
DKGDCPSTPF KTAAPFVSCS TQGASFSLDY LLPHSVVHLE GCTEQSSATD 1150
NELSPEQASW EDSRGHFLSS GSGMAHTSSP LTNEDLSLIN KLGDSVGVLQ 1200
KKLDPSPEAC RIPHSSSSEN IRDLSHSRGV VKEHAKEIES RVIFQAGFSK 1250
TSQMKRSASL AKLGYLDLCK DYLPDRELVS SESPHLKLLQ PFLRTDSGMH 1300
ALMAHEPSES AGAQQNPQPT KYSVEQLKTS ECIVQSKPVE RPSVQYAKEF 1350
GYSQQCLLPK ARPELTSSEG GLPLLQTQGL QYTGPSPGLA VAPRQQHGRT 1400
HPLRRLKRAN DKKRTTNPFY NTM 1423
Length:1,423
Mass (Da):158,230
Last modified:March 15, 2005 - v2
Checksum:i7F2608E87A72BAFD
GO
Isoform 2 (identifier: Q5SW75-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MALVTVQRSP...EEECRSQPRS → MTLSTLAGER...VISQNAINQL

Show »
Length:1,430
Mass (Da):158,900
Checksum:iDC554069F95CD99D
GO
Isoform 3 (identifier: Q5SW75-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MALVTVQRSP...EEECRSQPRS → MTLSTLAGER...VISQNAINQL
     133-133: S → R
     134-1423: Missing.

Note: No experimental confirmation available.

Show »
Length:140
Mass (Da):15,439
Checksum:i05F40C9021BA2B9D
GO
Isoform 4 (identifier: Q5SW75-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     21-21: S → SSSYLEDSESAALLCCEYGESEIFSDFN

Note: Gene prediction based on EST data. No experimental confirmation available.

Show »
Length:1,450
Mass (Da):161,221
Checksum:iA76802D4C70636BF
GO

Sequence cautioni

The sequence BAE41593.1 differs from that shown. Reason: Intron retention.
The sequence CAI24907.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI35940.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI51882.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MALVT…SQPRS → MTLSTLAGERKALPASTCSL GGPDMIPYFSANAVISQNAI NQL in isoform 2 and isoform 3.
VSP_016326Add
BLAST
Alternative sequencei21 – 211S → SSSYLEDSESAALLCCEYGE SEIFSDFN in isoform 4.
VSP_016327
Alternative sequencei133 – 1331S → R in isoform 3.
VSP_016328
Alternative sequencei134 – 14231290Missing in isoform 3.
VSP_016329Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331Missing in BAE33137. 1 Publication
Sequence conflicti325 – 3251N → D in BAE41593. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB099288 mRNA. Translation: BAC97811.1.
AK155232 mRNA. Translation: BAE33137.1.
AK158449 mRNA. Translation: BAE34514.1.
AK170142 mRNA. Translation: BAE41593.1. Sequence problems.
AL606724, AL607072, AL663066 Genomic DNA. Translation: CAI24906.2.
AL606724, AL663066 Genomic DNA. Translation: CAI24907.1. Sequence problems.
AL663066, AL606724, AL607072 Genomic DNA. Translation: CAI35939.2.
AL663066, AL606724 Genomic DNA. Translation: CAI35940.1. Sequence problems.
AL606724 Genomic DNA. Translation: CAI51882.1. Sequence problems.
AL607072, AL606724, AL663066 Genomic DNA. Translation: CAI52040.1.
BC141392 mRNA. Translation: AAI41393.1.
BC141393 mRNA. Translation: AAI41394.1.
AK173243 mRNA. Translation: BAD32521.1.
CCDSiCCDS25076.1. [Q5SW75-1]
RefSeqiNP_001278119.1. NM_001291190.1.
NP_808378.2. NM_177710.4. [Q5SW75-1]
XP_006533290.1. XM_006533227.1. [Q5SW75-4]
XP_006533292.1. XM_006533229.1. [Q5SW75-2]
UniGeneiMm.440381.

Genome annotation databases

EnsembliENSMUST00000037912; ENSMUSP00000042625; ENSMUSG00000037926. [Q5SW75-1]
ENSMUST00000181283; ENSMUSP00000137933; ENSMUSG00000037926.
GeneIDi237860.
KEGGimmu:237860.
UCSCiuc007kgl.2. mouse. [Q5SW75-1]
uc007kgo.2. mouse. [Q5SW75-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB099288 mRNA. Translation: BAC97811.1 .
AK155232 mRNA. Translation: BAE33137.1 .
AK158449 mRNA. Translation: BAE34514.1 .
AK170142 mRNA. Translation: BAE41593.1 . Sequence problems.
AL606724 , AL607072 , AL663066 Genomic DNA. Translation: CAI24906.2 .
AL606724 , AL663066 Genomic DNA. Translation: CAI24907.1 . Sequence problems.
AL663066 , AL606724 , AL607072 Genomic DNA. Translation: CAI35939.2 .
AL663066 , AL606724 Genomic DNA. Translation: CAI35940.1 . Sequence problems.
AL606724 Genomic DNA. Translation: CAI51882.1 . Sequence problems.
AL607072 , AL606724 , AL663066 Genomic DNA. Translation: CAI52040.1 .
BC141392 mRNA. Translation: AAI41393.1 .
BC141393 mRNA. Translation: AAI41394.1 .
AK173243 mRNA. Translation: BAD32521.1 .
CCDSi CCDS25076.1. [Q5SW75-1 ]
RefSeqi NP_001278119.1. NM_001291190.1.
NP_808378.2. NM_177710.4. [Q5SW75-1 ]
XP_006533290.1. XM_006533227.1. [Q5SW75-4 ]
XP_006533292.1. XM_006533229.1. [Q5SW75-2 ]
UniGenei Mm.440381.

3D structure databases

ProteinModelPortali Q5SW75.
SMRi Q5SW75. Positions 307-448.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000104034.

PTM databases

PhosphoSitei Q5SW75.

Proteomic databases

PaxDbi Q5SW75.
PRIDEi Q5SW75.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000037912 ; ENSMUSP00000042625 ; ENSMUSG00000037926 . [Q5SW75-1 ]
ENSMUST00000181283 ; ENSMUSP00000137933 ; ENSMUSG00000037926 .
GeneIDi 237860.
KEGGi mmu:237860.
UCSCi uc007kgl.2. mouse. [Q5SW75-1 ]
uc007kgo.2. mouse. [Q5SW75-2 ]

Organism-specific databases

CTDi 85464.
MGIi MGI:2679255. Ssh2.
Rougei Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00750000117282.
HOVERGENi HBG094002.
KOi K05766.
OrthoDBi EOG7B8S33.
PhylomeDBi Q5SW75.
TreeFami TF319444.

Miscellaneous databases

NextBioi 383532.
PROi Q5SW75.
SOURCEi Search...

Gene expression databases

Bgeei Q5SW75.
CleanExi MM_SSH2.
Genevestigatori Q5SW75.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR014876. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view ]
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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), FUNCTION, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-392.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: NOD.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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: Brain.
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1423 (ISOFORMS 1/2).
    Tissue: Brain.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.

Entry informationi

Entry nameiSSH2_MOUSE
AccessioniPrimary (citable) accession number: Q5SW75
Secondary accession number(s): B9EJ94
, Q3TDK8, Q3TYP8, Q3U2K3, Q5F268, Q5SW74, Q69ZC3, Q76I78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi