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O88811

- STAM2_MOUSE

UniProt

O88811 - STAM2_MOUSE

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Protein

Signal transducing adapter molecule 2

Gene

Stam2

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

Functioni

Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity).By similarity

GO - Biological processi

  1. intracellular protein transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_203917. EGFR downregulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducing adapter molecule 2
Short name:
STAM-2
Alternative name(s):
Hrs-binding protein
Gene namesi
Name:Stam2
Synonyms:Hbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1929100. Stam2.

Subcellular locationi

Cytoplasm 2 Publications. Early endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

  1. endosome Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Adult mice lacking Stam1 and Stam2 due to inducible gene targeting exhibit significant reduction in T-cell development in the thymus and profound reduction in the peripheral mature T-cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Signal transducing adapter molecule 2PRO_0000190148Add
BLAST

Post-translational modificationi

Phosphorylated in response to IL-2, GM-CSF, EGF and PDGF.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO88811.
PaxDbiO88811.
PRIDEiO88811.

PTM databases

PhosphoSiteiO88811.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in testis.1 Publication

Gene expression databases

BgeeiO88811.
ExpressionAtlasiO88811. baseline and differential.
GenevestigatoriO88811.

Interactioni

Subunit structurei

Component of the ESCRT-0 complex composed of STAM or STAM2 and HGS. Part of a complex at least composed of HSG, STAM2 and EPS15. Interacts with JAK2 and JAK3. Interacts with ubiquitinated proteins and the deubiquitinating enzyme USP8/UBPY. Interacts (via the via the PxVxL motif) with CBX5; the interaction is direct. Interacts with VPS37C. Interacts with ubiquitin; the interaction is direct (By similarity).By similarity

Protein-protein interaction databases

BioGridi207904. 8 interactions.
IntActiO88811. 5 interactions.
MINTiMINT-144894.

Structurei

Secondary structure

1
523
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi205 – 2117Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi236 – 2449Combined sources
Beta strandi247 – 2526Combined sources
Helixi253 – 2553Combined sources
Beta strandi256 – 2583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJ0X-ray1.70A204-261[»]
ProteinModelPortaliO88811.
SMRiO88811. Positions 1-150, 204-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88811.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 144129VHSPROSITE-ProRule annotationAdd
BLAST
Repeati165 – 18420UIMAdd
BLAST
Domaini202 – 26160SH3PROSITE-ProRule annotationAdd
BLAST
Domaini360 – 37718ITAMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2202Interaction with USP8
Regioni334 – 36835Interaction with HGSAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi54 – 6714PxVxL motifAdd
BLAST

Domaini

The VHS and UIM domains mediate the interaction with ubiquitinated proteins.1 Publication
The SH3 domain mediates the interaction with USP8.1 Publication
Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.1 Publication

Sequence similaritiesi

Belongs to the STAM family.Curated
Contains 1 ITAM domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 UIM (ubiquitin-interacting motif) repeat.PROSITE-ProRule annotation
Contains 1 VHS domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG309509.
GeneTreeiENSGT00700000104139.
HOGENOMiHOG000231952.
HOVERGENiHBG053175.
InParanoidiO88811.
KOiK04705.
OMAiHYPPASS.
OrthoDBiEOG7353WJ.
PhylomeDBiO88811.
TreeFamiTF315007.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR001452. SH3_domain.
IPR003903. Ubiquitin-int_motif.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
PF02809. UIM. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
SM00726. UIM. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
PS50330. UIM. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O88811-1) [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

        10         20         30         40         50
MPLFTANPFE QDVEKATNEY NTTEDWSLIM DICDRVGSTP SGAKDCLKAI
60 70 80 90 100
MKRVNHKVPH VALQALTLLG ACVANCGKIF HLEVCSRDFA TEVRSVIKNK
110 120 130 140 150
AHPKVCEKLK SLMVEWSEEF QKDPQFSLIS ATIKSMKEEG VTFPSAGSQT
160 170 180 190 200
VAAAAKNGTS LNKNKEDEDI AKAIELSLQE QKQQYTETKA LYPPAESQLN
210 220 230 240 250
NKAARRVRAL YDFEAVEDNE LTFKHGELIT VLDDSDANWW QGENHRGTGL
260 270 280 290 300
FPSNFVTTDL STEVETATVD KLNVIDDDVE EIKKSEPEPV YIDEGKMDRA
310 320 330 340 350
LQILQSIDPK ESKPDSQDLL DLEDVCQQMG PMIDEKLEEI DRKHSELSEL
360 370 380 390 400
NVKVLEALDL YNKLVNEAPV YSVYSKLHPA HYPPAAAGVP VQTYPVQSHG
410 420 430 440 450
GNYLGHGIHQ VSVAQNYNLG PDPMGSLRSL PPNMNSVTAH TVQPPYLSTG
460 470 480 490 500
QDTVSNPSYM NQSSRLQAAA GTAAYTQPVG MSTDVSSFQN TASGLPQLAG
510 520
FPVAVPAPVA AQPQASYHQQ PLL
Length:523
Mass (Da):57,455
Last modified:November 1, 1998 - v1
Checksum:iCE00B59F10BA0161
GO
Isoform 2 (identifier: O88811-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-100: Missing.
     448-448: S → R
     449-523: Missing.

Show »
Length:415
Mass (Da):46,260
Checksum:i305B94A59C0CA08B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 10033Missing in isoform 2. 1 PublicationVSP_014849Add
BLAST
Alternative sequencei448 – 4481S → R in isoform 2. 1 PublicationVSP_014850
Alternative sequencei449 – 52375Missing in isoform 2. 1 PublicationVSP_014851Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012611 mRNA. Translation: BAA33547.1.
AK004604 mRNA. Translation: BAB23403.1.
AK044230 mRNA. Translation: BAC31830.1.
AL928960 Genomic DNA. Translation: CAM23666.1.
BC013818 mRNA. Translation: AAH13818.1.
CCDSiCCDS16037.1. [O88811-1]
RefSeqiNP_062641.1. NM_019667.2. [O88811-1]
UniGeneiMm.263639.

Genome annotation databases

EnsembliENSMUST00000102759; ENSMUSP00000099820; ENSMUSG00000055371. [O88811-1]
ENSMUST00000127316; ENSMUSP00000121898; ENSMUSG00000055371. [O88811-2]
GeneIDi56324.
KEGGimmu:56324.
UCSCiuc008jre.1. mouse. [O88811-1]
uc008jrf.1. mouse. [O88811-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012611 mRNA. Translation: BAA33547.1 .
AK004604 mRNA. Translation: BAB23403.1 .
AK044230 mRNA. Translation: BAC31830.1 .
AL928960 Genomic DNA. Translation: CAM23666.1 .
BC013818 mRNA. Translation: AAH13818.1 .
CCDSi CCDS16037.1. [O88811-1 ]
RefSeqi NP_062641.1. NM_019667.2. [O88811-1 ]
UniGenei Mm.263639.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UJ0 X-ray 1.70 A 204-261 [» ]
ProteinModelPortali O88811.
SMRi O88811. Positions 1-150, 204-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207904. 8 interactions.
IntActi O88811. 5 interactions.
MINTi MINT-144894.

PTM databases

PhosphoSitei O88811.

Proteomic databases

MaxQBi O88811.
PaxDbi O88811.
PRIDEi O88811.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102759 ; ENSMUSP00000099820 ; ENSMUSG00000055371 . [O88811-1 ]
ENSMUST00000127316 ; ENSMUSP00000121898 ; ENSMUSG00000055371 . [O88811-2 ]
GeneIDi 56324.
KEGGi mmu:56324.
UCSCi uc008jre.1. mouse. [O88811-1 ]
uc008jrf.1. mouse. [O88811-2 ]

Organism-specific databases

CTDi 10254.
MGIi MGI:1929100. Stam2.

Phylogenomic databases

eggNOGi NOG309509.
GeneTreei ENSGT00700000104139.
HOGENOMi HOG000231952.
HOVERGENi HBG053175.
InParanoidi O88811.
KOi K04705.
OMAi HYPPASS.
OrthoDBi EOG7353WJ.
PhylomeDBi O88811.
TreeFami TF315007.

Enzyme and pathway databases

Reactomei REACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_203917. EGFR downregulation.

Miscellaneous databases

ChiTaRSi Stam2. mouse.
EvolutionaryTracei O88811.
NextBioi 312298.
PROi O88811.
SOURCEi Search...

Gene expression databases

Bgeei O88811.
ExpressionAtlasi O88811. baseline and differential.
Genevestigatori O88811.

Family and domain databases

Gene3Di 1.25.40.90. 1 hit.
InterProi IPR008942. ENTH_VHS.
IPR001452. SH3_domain.
IPR003903. Ubiquitin-int_motif.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view ]
Pfami PF00018. SH3_1. 1 hit.
PF02809. UIM. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00326. SH3. 1 hit.
SM00726. UIM. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view ]
SUPFAMi SSF48464. SSF48464. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
PS50330. UIM. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A hrs binding protein having a Src homology 3 domain is involved in intracellular degradation of growth factors and their receptors."
    Takata H., Kato M., Denda K., Kitamura N.
    Genes Cells 5:57-69(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH HGS, DOMAIN, SUBCELLULAR LOCATION.
    Tissue: Liver.
  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 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Lung.
  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).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP."
    Kato M., Miyazawa K., Kitamura N.
    J. Biol. Chem. 275:37481-37487(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP8.
  6. "Signal-transducing adaptor molecules STAM1 and STAM2 are required for T-cell development and survival."
    Yamada M., Ishii N., Asao H., Murata K., Kanazawa C., Sasaki H., Sugamura K.
    Mol. Cell. Biol. 22:8648-8658(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes."
    Bache K.G., Raiborg C., Mehlum A., Stenmark H.
    J. Biol. Chem. 278:12513-12521(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HGS; EPS15 AND UBIQUITIN, SUBCELLULAR LOCATION.
  8. "STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif."
    Mizuno E., Kawahata K., Kato M., Kitamura N., Komada M.
    Mol. Biol. Cell 14:3675-3689(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBIQUITIN, FUNCTION.
  9. "Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain."
    Kaneko T., Kumasaka T., Ganbe T., Sato T., Miyazawa K., Kitamura N., Tanaka N.
    J. Biol. Chem. 278:48162-48168(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 203-260 IN COMPLEX WITH USP8.

Entry informationi

Entry nameiSTAM2_MOUSE
AccessioniPrimary (citable) accession number: O88811
Secondary accession number(s): A2AU00, Q8C8Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 124 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

3D-structure, Complete proteome, 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