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Q9JM90 (STAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal-transducing adaptor protein 1

Short name=STAP-1
Alternative name(s):
Stem cell adaptor protein 1
Gene names
Name:Stap1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Nucleus By similarity. Cytoplasm Probable. Mitochondrion By similarity.

Tissue specificity

Expression restricted to the bone marrow. Ref.1

Post-translational modification

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

Sequence similarities

Contains 1 PH domain.

Contains 1 SH2 domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JM90-1)

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: Q9JM90-2)

The sequence of this isoform differs from the canonical sequence as follows:
     122-127: LTVPQH → VIRFPL
     128-297: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Signal-transducing adaptor protein 1
PRO_0000072238

Regions

Domain25 – 12197PH
Domain179 – 27395SH2

Amino acid modifications

Modified residue1701Phosphotyrosine Ref.4

Natural variations

Alternative sequence122 – 1276LTVPQH → VIRFPL in isoform 2.
VSP_013399
Alternative sequence128 – 297170Missing in isoform 2.
VSP_013400

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: 8033C606990AAA75

FASTA29734,628
        10         20         30         40         50         60 
MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLVKRSDHQ EYKHYWTELR GTTLFFYTDK 

        70         80         90        100        110        120 
KSTIYVGKLD IIDLVCLTGQ HSTEKNCAKF TLVLPKEEVH VKTENTESGE EWRGFILTVT 

       130        140        150        160        170        180 
ELTVPQHVSL LPGQVIRLHE VLEREKKRRI ETDQLPLMPP EKEKEPVQDY ADVLNPLPEC 

       190        200        210        220        230        240 
FYAVSRKEAT AMLEKNPSWG NMILRPGSDS KNYSITIRQE IEMPRIKHFK VTRTGNNYTI 

       250        260        270        280        290 
ELEKPVTLPN LFSVIDYFVK ETRGNLRPFI HSADDNFGQD PNIEDRSEKF KKNPHNA 

« Hide

Isoform 2 [UniParc].

Checksum: AFAAE1584FA79F68
Show »

FASTA12714,921

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_064376.1. NM_019992.3.
XP_006535224.1. XM_006535161.1.
UniGeneMm.131237.

3D structure databases

ProteinModelPortalQ9JM90.
SMRQ9JM90. Positions 16-152, 173-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208177. 4 interactions.

PTM databases

PhosphoSiteQ9JM90.

Proteomic databases

PaxDbQ9JM90.
PRIDEQ9JM90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031171; ENSMUSP00000031171; ENSMUSG00000029254. [Q9JM90-1]
GeneID56792.
KEGGmmu:56792.
UCSCuc008xxf.1. mouse. [Q9JM90-2]
uc008xxg.1. mouse. [Q9JM90-1]

Organism-specific databases

CTD26228.
MGIMGI:1926193. Stap1.

Phylogenomic databases

eggNOGNOG47666.
GeneTreeENSGT00530000063841.
HOGENOMHOG000234375.
HOVERGENHBG062262.
InParanoidA6H6C6.
OMAALPLYFE.
OrthoDBEOG79KPFP.
PhylomeDBQ9JM90.
TreeFamTF332087.

Gene expression databases

BgeeQ9JM90.
CleanExMM_STAP1.
GenevestigatorQ9JM90.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR000980. SH2.
[Graphical view]
PfamPF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio313336.
PROQ9JM90.
SOURCESearch...

Entry information

Entry nameSTAP1_MOUSE
AccessionPrimary (citable) accession number: Q9JM90
Secondary accession number(s): A6H6C6, Q3TRM1, Q6PES6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot