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Q8TE77

- SSH3_HUMAN

UniProt

Q8TE77 - SSH3_HUMAN

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Protein

Protein phosphatase Slingshot homolog 3

Gene

SSH3

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

Functioni

Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei413 – 4131Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase Slingshot homolog 3 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
SSH-like protein 3
Short name:
SSH-3L
Short name:
hSSH-3L
Gene namesi
Name:SSH3
Synonyms:SSH3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:30581. SSH3.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134929326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 659658Protein phosphatase Slingshot homolog 3PRO_0000094845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei85 – 851Phosphoserine1 Publication
Modified residuei87 – 871Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8TE77.
PaxDbiQ8TE77.
PRIDEiQ8TE77.

PTM databases

PhosphoSiteiQ8TE77.

Expressioni

Gene expression databases

BgeeiQ8TE77.
CleanExiHS_SSH3.
ExpressionAtlasiQ8TE77. baseline and differential.
GenevestigatoriQ8TE77.

Organism-specific databases

HPAiHPA019949.
HPA019957.

Interactioni

Subunit structurei

Does not bind to, or colocalize with, filamentous actin.By similarity

Protein-protein interaction databases

BioGridi120299. 2 interactions.
IntActiQ8TE77. 2 interactions.
MINTiMINT-5006487.
STRINGi9606.ENSP00000312081.

Structurei

3D structure databases

ProteinModelPortaliQ8TE77.
SMRiQ8TE77. Positions 330-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini328 – 468141Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG089321.
InParanoidiQ8TE77.
KOiK05766.
OMAiPHWKETH.
OrthoDBiEOG7B8S33.
PhylomeDBiQ8TE77.
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 (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TE77-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MALVTVSRSP PGSGASTPVG PWDQAVQRRS RLQRRQSFAV LRGAVLGLQD
60 70 80 90 100
GGDNDDAAEA SSEPTEKAPS EEELHGDQTD FGQGSQSPQK QEEQRQHLHL
110 120 130 140 150
MVQLLRPQDD IRLAAQLEAP RPPRLRYLLV VSTREGEGLS QDETVLLGVD
160 170 180 190 200
FPDSSSPSCT LGLVLPLWSD TQVYLDGDGG FSVTSGGQSR IFKPISIQTM
210 220 230 240 250
WATLQVLHQA CEAALGSGLV PGGSALTWAS HYQERLNSEQ SCLNEWTAMA
260 270 280 290 300
DLESLRPPSA EPGGSSEQEQ MEQAIRAELW KVLDVSDLES VTSKEIRQAL
310 320 330 340 350
ELRLGLPLQQ YRDFIDNQML LLVAQRDRAS RIFPHLYLGS EWNAANLEEL
360 370 380 390 400
QRNRVTHILN MAREIDNFYP ERFTYHNVRL WDEESAQLLP HWKETHRFIE
410 420 430 440 450
AARAQGTHVL VHCKMGVSRS AATVLAYAMK QYECSLEQAL RHVQELRPIA
460 470 480 490 500
RPNPGFLRQL QIYQGILTAS RQSHVWEQKV GGVSPEEHPA PEVSTPFPPL
510 520 530 540 550
PPEPEGGGEE KVVGMEESQA APKEEPGPRP RINLRGVMRS ISLLEPSLEL
560 570 580 590 600
ESTSETSDMP EVFSSHESSH EEPLQPFPQL ARTKGGQQVD RGPQPALKSR
610 620 630 640 650
QSVVTLQGSA VVANRTQAFQ EQEQGQGQGQ GEPCISSTPR FRKVVRQASV

HDSGEEGEA
Length:659
Mass (Da):72,996
Last modified:November 22, 2005 - v2
Checksum:i0D96F86EAFE81D3B
GO
Isoform 2 (identifier: Q8TE77-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     470-471: SR → RT
     472-659: Missing.

Show »
Length:471
Mass (Da):52,713
Checksum:i826A8914B638DCC0
GO
Isoform 3 (identifier: Q8TE77-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-146: Missing.
     147-154: LGVDFPDS → MAFPLSPA

Show »
Length:514
Mass (Da):57,113
Checksum:iCA4F7CD4CE02B99F
GO
Isoform 4 (identifier: Q8TE77-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-547: Missing.

Note: No experimental confirmation available.

Show »
Length:394
Mass (Da):42,724
Checksum:iF87C7F5A29048AAE
GO
Isoform 5 (identifier: Q8TE77-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-330: Missing.
     331-360: RIFPHLYLGSEWNAANLEELQRNRVTHILN → MEGTMMMQQRPVLSQQHPSFILNSSPAHSP
     470-471: SR → RT
     472-659: Missing.

Note: No experimental confirmation available.

Show »
Length:142
Mass (Da):16,488
Checksum:i7A1687EE220D2DD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581A → V(PubMed:11832213)Curated
Sequence conflicti58 – 581A → V(PubMed:14531860)Curated
Sequence conflicti509 – 5091E → G in BAC04314. (PubMed:14702039)Curated
Sequence conflicti641 – 6411F → S in BAB85080. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti239 – 2391E → V.
Corresponds to variant rs7114712 [ dbSNP | Ensembl ].
VAR_057132
Natural varianti600 – 6001R → H.
Corresponds to variant rs1573536 [ dbSNP | Ensembl ].
VAR_057133

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 330329Missing in isoform 5. 1 PublicationVSP_016330Add
BLAST
Alternative sequencei2 – 146145Missing in isoform 3. 1 PublicationVSP_016331Add
BLAST
Alternative sequencei147 – 1548LGVDFPDS → MAFPLSPA in isoform 3. 1 PublicationVSP_016332
Alternative sequencei283 – 547265Missing in isoform 4. 1 PublicationVSP_016333Add
BLAST
Alternative sequencei331 – 36030RIFPH…THILN → MEGTMMMQQRPVLSQQHPSF ILNSSPAHSP in isoform 5. 1 PublicationVSP_016334Add
BLAST
Alternative sequencei470 – 4712SR → RT in isoform 2 and isoform 5. 2 PublicationsVSP_016335
Alternative sequencei472 – 659188Missing in isoform 2 and isoform 5. 2 PublicationsVSP_016336Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB072360 mRNA. Translation: BAB84119.3.
AB099291 mRNA. Translation: BAC97814.1.
AK000522 mRNA. Translation: BAA91228.1.
AK001790 mRNA. Translation: BAA91913.1.
AK074432 mRNA. Translation: BAB85080.1.
AK094226 mRNA. Translation: BAC04314.1.
BC007709 mRNA. Translation: AAH07709.1.
CCDSiCCDS8157.1. [Q8TE77-1]
RefSeqiNP_060327.3. NM_017857.3. [Q8TE77-1]
UniGeneiHs.29173.

Genome annotation databases

EnsembliENST00000308127; ENSP00000312081; ENSG00000172830. [Q8TE77-1]
ENST00000532881; ENSP00000431788; ENSG00000172830. [Q8TE77-2]
GeneIDi54961.
KEGGihsa:54961.
UCSCiuc001okj.3. human. [Q8TE77-1]
uc001okl.3. human. [Q8TE77-3]

Polymorphism databases

DMDMi82582268.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB072360 mRNA. Translation: BAB84119.3 .
AB099291 mRNA. Translation: BAC97814.1 .
AK000522 mRNA. Translation: BAA91228.1 .
AK001790 mRNA. Translation: BAA91913.1 .
AK074432 mRNA. Translation: BAB85080.1 .
AK094226 mRNA. Translation: BAC04314.1 .
BC007709 mRNA. Translation: AAH07709.1 .
CCDSi CCDS8157.1. [Q8TE77-1 ]
RefSeqi NP_060327.3. NM_017857.3. [Q8TE77-1 ]
UniGenei Hs.29173.

3D structure databases

ProteinModelPortali Q8TE77.
SMRi Q8TE77. Positions 330-469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120299. 2 interactions.
IntActi Q8TE77. 2 interactions.
MINTi MINT-5006487.
STRINGi 9606.ENSP00000312081.

PTM databases

PhosphoSitei Q8TE77.

Polymorphism databases

DMDMi 82582268.

Proteomic databases

MaxQBi Q8TE77.
PaxDbi Q8TE77.
PRIDEi Q8TE77.

Protocols and materials databases

DNASUi 54961.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308127 ; ENSP00000312081 ; ENSG00000172830 . [Q8TE77-1 ]
ENST00000532881 ; ENSP00000431788 ; ENSG00000172830 . [Q8TE77-2 ]
GeneIDi 54961.
KEGGi hsa:54961.
UCSCi uc001okj.3. human. [Q8TE77-1 ]
uc001okl.3. human. [Q8TE77-3 ]

Organism-specific databases

CTDi 54961.
GeneCardsi GC11P067071.
HGNCi HGNC:30581. SSH3.
HPAi HPA019949.
HPA019957.
MIMi 606780. gene.
neXtProti NX_Q8TE77.
PharmGKBi PA134929326.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118902.
HOVERGENi HBG089321.
InParanoidi Q8TE77.
KOi K05766.
OMAi PHWKETH.
OrthoDBi EOG7B8S33.
PhylomeDBi Q8TE77.
TreeFami TF319444.

Miscellaneous databases

GeneWikii SSH3.
GenomeRNAii 54961.
NextBioi 58168.
PROi Q8TE77.
SOURCEi Search...

Gene expression databases

Bgeei Q8TE77.
CleanExi HS_SSH3.
ExpressionAtlasi Q8TE77. baseline and differential.
Genevestigatori Q8TE77.

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. "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] (ISOFORM 2).
  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. "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.
    , 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] (ISOFORMS 1; 3; 4 AND 5).
    Tissue: Cerebellum and Ovarian carcinoma.
  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: Uterus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiSSH3_HUMAN
AccessioniPrimary (citable) accession number: Q8TE77
Secondary accession number(s): Q6PK42
, Q76I75, Q8N9L8, Q8WYL0, Q9NV45, Q9NWZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: October 29, 2014
This is version 109 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

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3