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Protein

Hematopoietic SH2 domain-containing protein

Gene

Hsh2d

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Adapter protein involved in tyrosine kinase and CD28 signaling (By similarity). May be a modulator of the apoptotic response through its ability to affect mitochondrial stability.By similarity1 Publication

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: MGI

GO - Biological processi

  • negative regulation of B cell apoptotic process Source: MGI
  • negative regulation of mitochondrial depolarization Source: MGI
  • positive regulation of signal transduction Source: GOC
  • T cell activation Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Hematopoietic SH2 domain-containing protein
Short name:
Hematopoietic SH2 protein
Alternative name(s):
Adaptor in lymphocytes of unknown function X
Gene namesi
Name:Hsh2d
Synonyms:Alx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2676364. Hsh2d.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Hematopoietic SH2 domain-containing proteinPRO_0000233130Add
BLAST

Post-translational modificationi

May be phosphorylated by FES and ACK1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ6VYH9.
PRIDEiQ6VYH9.

PTM databases

iPTMnetiQ6VYH9.
PhosphoSiteiQ6VYH9.

Expressioni

Tissue specificityi

Predominantly expressed in spleen and thymus. Appears not to be expressed in heart, brain, liver, kidney, embryo, lung and ovary.1 Publication

Gene expression databases

BgeeiQ6VYH9.
CleanExiMM_HSH2D.
GenevisibleiQ6VYH9. MM.

Interactioni

Subunit structurei

Interacts with FES and TNK2.By similarity

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071970.

Structurei

3D structure databases

ProteinModelPortaliQ6VYH9.
SMRiQ6VYH9. Positions 26-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 12592SH2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi326 – 3294Poly-Pro

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiENOG410IXE0. Eukaryota.
ENOG4111Y35. LUCA.
GeneTreeiENSGT00570000079047.
HOGENOMiHOG000112961.
HOVERGENiHBG081611.
InParanoidiQ6VYH9.
OMAiKLWRNLK.
OrthoDBiEOG751NG5.
PhylomeDBiQ6VYH9.
TreeFamiTF336893.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6VYH9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEARRLPPP LPPRLDWFVH TQADLLAQSG IPEWFHGTIS REAAENMLES
60 70 80 90 100
QPLGTFLIRV SHSHVGYTLS YKAQTCCRHF MVKLSEDGTC AFAGDHMTHA
110 120 130 140 150
SLHALVTFHQ QKPIRPFGEL LTQACGQEDP ANVDYEDLFL YSNALVQDAE
160 170 180 190 200
SQILRTEVQR SSCPPEEASE RKPSTTTKGE FASASCSPKA LFEDSGQKLW
210 220 230 240 250
KNLRSLPQTS QRVKQRLTSH LLAMNLLGDA RQVAQQHHSP VTRAFSWDST
260 270 280 290 300
SHSEDSCAAT TSLQNPAEPQ ALRGREATFR DSRPASWRKA FSGVKAWRGK
310 320 330
VVRALSAQEP VDFPEAQGWL PEEYLPPPPF APGY
Length:334
Mass (Da):37,233
Last modified:July 5, 2004 - v1
Checksum:i32C3B3728C33F560
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911A → T in AAH94291 (PubMed:15489334).Curated
Sequence conflicti153 – 1531I → F in AAH94291 (PubMed:15489334).Curated
Sequence conflicti162 – 1621S → SS in AAH94291 (PubMed:15489334).Curated
Sequence conflicti216 – 2161R → Q in AAH94291 (PubMed:15489334).Curated
Sequence conflicti222 – 2221L → S in AAH94291 (PubMed:15489334).Curated
Sequence conflicti232 – 2321Q → R in AAH94291 (PubMed:15489334).Curated
Sequence conflicti256 – 2561S → P in AAH94291 (PubMed:15489334).Curated
Sequence conflicti294 – 2941V → I in AAH94291 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY319653 mRNA. Translation: AAQ81286.1.
AK157000 mRNA. Translation: BAE33927.1.
BC094291 mRNA. Translation: AAH94291.1.
CCDSiCCDS22410.1.
RefSeqiNP_922935.1. NM_197944.1.
UniGeneiMm.157431.

Genome annotation databases

EnsembliENSMUST00000072097; ENSMUSP00000071970; ENSMUSG00000062007.
ENSMUST00000165324; ENSMUSP00000127575; ENSMUSG00000062007.
GeneIDi209488.
KEGGimmu:209488.
UCSCiuc009mfl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY319653 mRNA. Translation: AAQ81286.1.
AK157000 mRNA. Translation: BAE33927.1.
BC094291 mRNA. Translation: AAH94291.1.
CCDSiCCDS22410.1.
RefSeqiNP_922935.1. NM_197944.1.
UniGeneiMm.157431.

3D structure databases

ProteinModelPortaliQ6VYH9.
SMRiQ6VYH9. Positions 26-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071970.

PTM databases

iPTMnetiQ6VYH9.
PhosphoSiteiQ6VYH9.

Proteomic databases

PaxDbiQ6VYH9.
PRIDEiQ6VYH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072097; ENSMUSP00000071970; ENSMUSG00000062007.
ENSMUST00000165324; ENSMUSP00000127575; ENSMUSG00000062007.
GeneIDi209488.
KEGGimmu:209488.
UCSCiuc009mfl.1. mouse.

Organism-specific databases

CTDi84941.
MGIiMGI:2676364. Hsh2d.

Phylogenomic databases

eggNOGiENOG410IXE0. Eukaryota.
ENOG4111Y35. LUCA.
GeneTreeiENSGT00570000079047.
HOGENOMiHOG000112961.
HOVERGENiHBG081611.
InParanoidiQ6VYH9.
OMAiKLWRNLK.
OrthoDBiEOG751NG5.
PhylomeDBiQ6VYH9.
TreeFamiTF336893.

Miscellaneous databases

PROiQ6VYH9.
SOURCEiSearch...

Gene expression databases

BgeeiQ6VYH9.
CleanExiMM_HSH2D.
GenevisibleiQ6VYH9. MM.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of ALX, an adaptor downstream of CD28."
    Greene T.A., Powell P., Nzerem C., Shapiro M.J., Shapiro V.S.
    J. Biol. Chem. 278:45128-45134(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Spleen.
  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].
    Strain: NOD.
    Tissue: Spleen.
  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].
    Strain: 129.
    Tissue: Mammary gland.
  4. "The adaptor protein HSH2 attenuates apoptosis in response to ligation of the B cell antigen receptor complex on the B lymphoma cell line, WEHI-231."
    Herrin B.R., Groeger A.L., Justement L.B.
    J. Biol. Chem. 280:3507-3515(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiHSH2D_MOUSE
AccessioniPrimary (citable) accession number: Q6VYH9
Secondary accession number(s): Q52KL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 79 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.