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Q9JM90

- STAP1_MOUSE

UniProt

Q9JM90 - STAP1_MOUSE

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Protein

Signal-transducing adaptor protein 1

Gene
Stap1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May function as an adapter molecule downstream of KIT in the proliferation or differentiation of hematopoietic stem cells.1 Publication

GO - Molecular functioni

  1. protein binding Source: MGI
  2. SH3/SH2 adaptor activity Source: MGI

GO - Biological processi

  1. myeloid cell differentiation Source: MGI
  2. positive regulation of signal transduction Source: GOC
  3. transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Signal-transducing adaptor protein 1
Short name:
STAP-1
Alternative name(s):
Stem cell adaptor protein 1
Gene namesi
Name:Stap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1926193. Stap1.

Subcellular locationi

Nucleus By similarity. Cytoplasm Inferred. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Signal-transducing adaptor protein 1PRO_0000072238Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine by TEC By similarity. Phosphorylated on tyrosine by KIT By similarity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9JM90.
PaxDbiQ9JM90.
PRIDEiQ9JM90.

PTM databases

PhosphoSiteiQ9JM90.

Expressioni

Tissue specificityi

Expression restricted to the bone marrow.1 Publication

Gene expression databases

BgeeiQ9JM90.
CleanExiMM_STAP1.
GenevestigatoriQ9JM90.

Interactioni

Subunit structurei

Interacts with URI1; the interaction is phosphorylation-dependent occurs in a growth-dependent manner By similarity. Interacts with KIT and CSF1R.1 Publication

Protein-protein interaction databases

BioGridi208177. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9JM90.
SMRiQ9JM90. Positions 16-152, 173-270.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 12197PHAdd
BLAST
Domaini179 – 27395SH2Add
BLAST

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 SH2 domain.

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG47666.
GeneTreeiENSGT00530000063841.
HOGENOMiHOG000234375.
HOVERGENiHBG062262.
InParanoidiA6H6C6.
OMAiPMPACFY.
OrthoDBiEOG79KPFP.
PhylomeDBiQ9JM90.
TreeFamiTF332087.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000980. SH2.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JM90-1) [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

MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLVKRSDHQ EYKHYWTELR    50
GTTLFFYTDK KSTIYVGKLD IIDLVCLTGQ HSTEKNCAKF TLVLPKEEVH 100
VKTENTESGE EWRGFILTVT ELTVPQHVSL LPGQVIRLHE VLEREKKRRI 150
ETDQLPLMPP EKEKEPVQDY ADVLNPLPEC FYAVSRKEAT AMLEKNPSWG 200
NMILRPGSDS KNYSITIRQE IEMPRIKHFK VTRTGNNYTI ELEKPVTLPN 250
LFSVIDYFVK ETRGNLRPFI HSADDNFGQD PNIEDRSEKF KKNPHNA 297
Length:297
Mass (Da):34,628
Last modified:October 1, 2000 - v1
Checksum:i8033C606990AAA75
GO
Isoform 2 (identifier: Q9JM90-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-127: LTVPQH → VIRFPL
     128-297: Missing.

Note: No experimental confirmation available.

Show »
Length:127
Mass (Da):14,921
Checksum:iAFAAE1584FA79F68
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei122 – 1276LTVPQH → VIRFPL in isoform 2. VSP_013399
Alternative sequencei128 – 297170Missing in isoform 2. VSP_013400Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB036058 mRNA. Translation: BAA92531.1.
AK041474 mRNA. Translation: BAC30953.1.
AK162655 mRNA. Translation: BAE37007.1.
BC057898 mRNA. Translation: AAH57898.1.
BC145828 mRNA. Translation: AAI45829.1.
BC145830 mRNA. Translation: AAI45831.1.
CCDSiCCDS19377.1. [Q9JM90-1]
RefSeqiNP_064376.1. NM_019992.3. [Q9JM90-1]
XP_006535224.1. XM_006535161.1. [Q9JM90-2]
UniGeneiMm.131237.

Genome annotation databases

EnsembliENSMUST00000031171; ENSMUSP00000031171; ENSMUSG00000029254. [Q9JM90-1]
GeneIDi56792.
KEGGimmu:56792.
UCSCiuc008xxf.1. mouse. [Q9JM90-2]
uc008xxg.1. mouse. [Q9JM90-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB036058 mRNA. Translation: BAA92531.1 .
AK041474 mRNA. Translation: BAC30953.1 .
AK162655 mRNA. Translation: BAE37007.1 .
BC057898 mRNA. Translation: AAH57898.1 .
BC145828 mRNA. Translation: AAI45829.1 .
BC145830 mRNA. Translation: AAI45831.1 .
CCDSi CCDS19377.1. [Q9JM90-1 ]
RefSeqi NP_064376.1. NM_019992.3. [Q9JM90-1 ]
XP_006535224.1. XM_006535161.1. [Q9JM90-2 ]
UniGenei Mm.131237.

3D structure databases

ProteinModelPortali Q9JM90.
SMRi Q9JM90. Positions 16-152, 173-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208177. 4 interactions.

PTM databases

PhosphoSitei Q9JM90.

Proteomic databases

MaxQBi Q9JM90.
PaxDbi Q9JM90.
PRIDEi Q9JM90.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031171 ; ENSMUSP00000031171 ; ENSMUSG00000029254 . [Q9JM90-1 ]
GeneIDi 56792.
KEGGi mmu:56792.
UCSCi uc008xxf.1. mouse. [Q9JM90-2 ]
uc008xxg.1. mouse. [Q9JM90-1 ]

Organism-specific databases

CTDi 26228.
MGIi MGI:1926193. Stap1.

Phylogenomic databases

eggNOGi NOG47666.
GeneTreei ENSGT00530000063841.
HOGENOMi HOG000234375.
HOVERGENi HBG062262.
InParanoidi A6H6C6.
OMAi PMPACFY.
OrthoDBi EOG79KPFP.
PhylomeDBi Q9JM90.
TreeFami TF332087.

Miscellaneous databases

NextBioi 313336.
PROi Q9JM90.
SOURCEi Search...

Gene expression databases

Bgeei Q9JM90.
CleanExi MM_STAP1.
Genevestigatori Q9JM90.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000980. SH2.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of murine STAP-1, the stem-cell-specific adaptor protein containing PH and SH2 domains."
    Masuhara M., Nagao K., Nishikawa M., Sasaki M., Yoshimura A., Osawa M.
    Biochem. Biophys. Res. Commun. 268:697-703(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, INTERACTION WITH KIT AND CSF1R, TISSUE SPECIFICITY.
  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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone and Thymus.
  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 1 AND 2).
    Strain: FVB/N.
    Tissue: Brain and Mammary gland.
  4. "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-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.

Entry informationi

Entry nameiSTAP1_MOUSE
AccessioniPrimary (citable) accession number: Q9JM90
Secondary accession number(s): A6H6C6, Q3TRM1, Q6PES6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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