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Q3UND0

- SKAP2_MOUSE

UniProt

Q3UND0 - SKAP2_MOUSE

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Protein
Src kinase-associated phosphoprotein 2
Gene
Skap2, Prap, Ra70, Saps, Scap2, Skap55r
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.3 Publications

GO - Biological processi

  1. B cell activation Source: UniProtKB-KW
  2. negative regulation of cell proliferation Source: MGI
Complete GO annotation...

Keywords - Biological processi

B-cell activation

Enzyme and pathway databases

ReactomeiREACT_215628. Signal regulatory protein (SIRP) family interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Src kinase-associated phosphoprotein 2
Alternative name(s):
Pyk2/RAFTK-associated protein
SKAP55 homolog
Short name:
SKAP-HOM
Src family-associated phosphoprotein 2
Src kinase-associated phosphoprotein 55-related protein
Src-associated adapter protein with PH and SH3 domains
Gene namesi
Name:Skap2
Synonyms:Prap, Ra70, Saps, Scap2, Skap55r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1889206. Skap2.

Subcellular locationi

Cytoplasm
Note: Membrane ruffles of macrophages. Perikarya and dendrites from neurons.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice are healthy and do not display any obvious abnormality. They have normal T-cell, platelet and macrophage function, but show reduced levels of spontaneous immunoglobulins in the serum, and defects in B-cell proliferation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi260 – 2601Y → F: Abolishes interaction with FYN, phosphorylation by FYN, and effects on cell growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Src kinase-associated phosphoprotein 2
PRO_0000270180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751Phosphotyrosine2 Publications
Modified residuei151 – 1511Phosphotyrosine1 Publication
Modified residuei260 – 2601Phosphotyrosine; by FYN3 Publications

Post-translational modificationi

Dephosphorylated on Tyr-75 by PTPN22 By similarity. Phosphorylated by FYN on Tyr-260. In case of infection with Y.pseudotuberculosis, dephosphorylated by bacterial phosphatase yopH.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3UND0.
PaxDbiQ3UND0.
PRIDEiQ3UND0.

Expressioni

Tissue specificityi

Expressed in kidney, lung, liver, spleen, bone marrow and testis. Present in T-cells, B-cells, and all cells of the myelomonocytic lineage. Present in all brain regions, with highest levels in neurons from the Purkinje cell layer, hippocampal gyrus, cortex and substantia nigra (at protein level).4 Publications

Inductioni

By IL-6 in myeloid cells.1 Publication

Gene expression databases

BgeeiQ3UND0.
CleanExiMM_SKAP2.
GenevestigatoriQ3UND0.

Interactioni

Subunit structurei

Interacts with LAT, GRB2, PTK2B and PRAM1 By similarity. Homodimer. Interacts with FYB, which is required for SKAP2 protein stability. Interacts with PTPNS1. Part of a complex consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting of SKAP2, FYB and LILRB3. May interact with actin. May interact with FYN, HCK and LYN. Interacts with FASLG By similarity.6 Publications

Protein-protein interaction databases

BioGridi207619. 1 interaction.
IntActiQ3UND0. 1 interaction.
MINTiMINT-263820.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2915
Turni30 – 345
Helixi39 – 5517
Helixi56 – 594
Helixi61 – 633
Helixi111 – 1133
Beta strandi115 – 12612
Beta strandi128 – 1303
Turni132 – 1343
Beta strandi136 – 14510
Beta strandi148 – 1547
Beta strandi161 – 1655
Beta strandi170 – 1734
Helixi175 – 1773
Helixi183 – 1853
Beta strandi186 – 1905
Beta strandi192 – 1943
Beta strandi196 – 2005
Helixi204 – 21714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5EX-ray2.60A/B14-222[»]
1U5FX-ray1.90A111-248[»]
1U5GX-ray2.10A/B/C/D103-222[»]
2OTXX-ray2.60A/B12-222[»]
ProteinModelPortaliQ3UND0.
SMRiQ3UND0. Positions 14-222, 304-355.

Miscellaneous databases

EvolutionaryTraceiQ3UND0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 219104PH
Add
BLAST
Domaini296 – 35762SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 6451Homodimerization
Add
BLAST

Domaini

The SH3 domain interacts with FYB and PTK2B By similarity.

Sequence similaritiesi

Belongs to the SKAP family.
Contains 1 PH domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG46742.
GeneTreeiENSGT00390000017856.
HOGENOMiHOG000231109.
HOVERGENiHBG052827.
InParanoidiQ3UND0.
OMAiWDCTGAL.
OrthoDBiEOG7K6PVB.
PhylomeDBiQ3UND0.
TreeFamiTF331055.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3UND0-1) [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

MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK    50
KIKDVKSVYL QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP 100
SDGNQFPPIA AQDLPFVIKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY 150
YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD GKKDCCFEIC APDKRIYQFT 200
AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV DHPAAVSSPQ 250
RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF 300
YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA 350
YLMEMYDI 358
Length:358
Mass (Da):40,712
Last modified:January 9, 2007 - v2
Checksum:iB66973A656E44E05
GO
Isoform 2 (identifier: Q3UND0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     22-28: Missing.

Note: No experimental confirmation available.

Show »
Length:351
Mass (Da):39,950
Checksum:iA6C08305272498D8
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei22 – 287Missing in isoform 2.
VSP_022184

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161E → K in BAE25817. 1 Publication
Sequence conflicti104 – 1041N → P AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051324 mRNA. Translation: AAC99297.1.
AB014485 mRNA. Translation: BAA77253.1.
AK076000 mRNA. Translation: BAC36111.1.
AK144289 mRNA. Translation: BAE25817.1.
BC003711 mRNA. Translation: AAH03711.1.
CCDSiCCDS20137.1. [Q3UND0-1]
RefSeqiNP_061243.1. NM_018773.2. [Q3UND0-1]
UniGeneiMm.221479.
Mm.392558.

Genome annotation databases

EnsembliENSMUST00000078214; ENSMUSP00000077342; ENSMUSG00000059182. [Q3UND0-1]
GeneIDi54353.
KEGGimmu:54353.
UCSCiuc009bxv.1. mouse. [Q3UND0-1]
uc009bxw.1. mouse. [Q3UND0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051324 mRNA. Translation: AAC99297.1 .
AB014485 mRNA. Translation: BAA77253.1 .
AK076000 mRNA. Translation: BAC36111.1 .
AK144289 mRNA. Translation: BAE25817.1 .
BC003711 mRNA. Translation: AAH03711.1 .
CCDSi CCDS20137.1. [Q3UND0-1 ]
RefSeqi NP_061243.1. NM_018773.2. [Q3UND0-1 ]
UniGenei Mm.221479.
Mm.392558.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U5E X-ray 2.60 A/B 14-222 [» ]
1U5F X-ray 1.90 A 111-248 [» ]
1U5G X-ray 2.10 A/B/C/D 103-222 [» ]
2OTX X-ray 2.60 A/B 12-222 [» ]
ProteinModelPortali Q3UND0.
SMRi Q3UND0. Positions 14-222, 304-355.
ModBasei Search...

Protein-protein interaction databases

BioGridi 207619. 1 interaction.
IntActi Q3UND0. 1 interaction.
MINTi MINT-263820.

Proteomic databases

MaxQBi Q3UND0.
PaxDbi Q3UND0.
PRIDEi Q3UND0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000078214 ; ENSMUSP00000077342 ; ENSMUSG00000059182 . [Q3UND0-1 ]
GeneIDi 54353.
KEGGi mmu:54353.
UCSCi uc009bxv.1. mouse. [Q3UND0-1 ]
uc009bxw.1. mouse. [Q3UND0-2 ]

Organism-specific databases

CTDi 8935.
MGIi MGI:1889206. Skap2.

Phylogenomic databases

eggNOGi NOG46742.
GeneTreei ENSGT00390000017856.
HOGENOMi HOG000231109.
HOVERGENi HBG052827.
InParanoidi Q3UND0.
OMAi WDCTGAL.
OrthoDBi EOG7K6PVB.
PhylomeDBi Q3UND0.
TreeFami TF331055.

Enzyme and pathway databases

Reactomei REACT_215628. Signal regulatory protein (SIRP) family interactions.

Miscellaneous databases

EvolutionaryTracei Q3UND0.
NextBioi 311138.
PROi Q3UND0.
SOURCEi Search...

Gene expression databases

Bgeei Q3UND0.
CleanExi MM_SKAP2.
Genevestigatori Q3UND0.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Adaptor protein SKAP55R is associated with myeloid differentiation and growth arrest."
    Curtis D.J., Jane S.M., Hilton D.J., Dougherty L., Bodine D.M., Begley C.G.
    Exp. Hematol. 28:1250-1259(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK AND LYN, PHOSPHORYLATION AT TYR-260, MUTAGENESIS OF TYR-260, FUNCTION.
    Tissue: Testis.
  2. "Mouse Saps, Src-associated adaptor protein with PH and SH3 domain."
    Lee J.-S., Suh K.S., Burr J.G.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "RA70, retinoic acid responsive gene, is expressed specifically in spermatocyte in mouse testis."
    Momoi T., Urase K., Mukasa T., Fujita E., Kouroku Y., Miho Y., Soyama A., Momoi M.Y.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Lymph node.
  5. "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 1 AND 2).
  6. "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55."
    Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.
    FEBS Lett. 435:55-60(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Tissue: T-cell.
  7. "The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages."
    Black D.S., Marie-Cardine A., Schraven B., Bliska J.B.
    Cell. Microbiol. 2:401-414(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 93-114; 129-139 AND 147-158, PHOSPHORYLATION, INTERACTION WITH FYB, IDENTIFICATION IN A COMPLEX WITH FYB AND PTPNS1, IDENTIFICATION IN A COMPLEX WITH FYB AND LILRB3.
  8. "SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages."
    Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E., Schraven B., Neel B.G.
    Curr. Biol. 9:927-930(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPNS1, IDENTIFICATION IN A COMPLEX WITH FYB AND PTPNS1.
  9. "Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation."
    Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H., Avraham S., Yasuda M., Matsumoto M.
    J. Biol. Chem. 278:42225-42233(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "Macrophage colony-stimulating factor receptor induces tyrosine phosphorylation of SKAP55R adaptor and its association with actin."
    Bourette R.P., Therier J., Mouchiroud G.
    Cell. Signal. 17:941-949(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH ACTIN, FUNCTION.
  11. "Regulation of in vitro and in vivo immune functions by the cytosolic adaptor protein SKAP-HOM."
    Togni M., Swanson K.D., Reimann S., Kliche S., Pearce A.C., Simeoni L., Reinhold D., Wienands J., Neel B.G., Schraven B., Gerber A.
    Mol. Cell. Biol. 25:8052-8063(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75 AND TYR-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "ADAP is required for normal alphaIIb-beta3 activation by VWF/GP Ib-IX-V and other agonists."
    Kasirer-Friede A., Moran B., Nagrampa-Orje J., Swanson K., Ruggeri Z.M., Schraven B., Neel B.G., Koretzky G., Shattil S.J.
    Blood 109:1018-1025(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYB.
  14. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; TYR-151 AND TYR-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  15. "The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch."
    Swanson K.D., Tang Y., Ceccarelli D.F., Poy F., Sliwa J.P., Neel B.G., Eck M.J.
    Mol. Cell 32:564-575(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-222, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSKAP2_MOUSE
AccessioniPrimary (citable) accession number: Q3UND0
Secondary accession number(s): Q8BK74, Q9Z2K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi