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Hematopoietic SH2 domain-containing protein (Hematopoietic SH2 protein) (Adaptor in lymphocytes of unknown function X)

 HSH2D_HUMAN             Reviewed;         352 AA.
Q96JZ2; B5ME72; Q6ZNG7;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
20-JUN-2018, entry version 128.
RecName: Full=Hematopoietic SH2 domain-containing protein;
Short=Hematopoietic SH2 protein;
AltName: Full=Adaptor in lymphocytes of unknown function X;
Name=HSH2D; Synonyms=ALX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
INTERACTION WITH FES AND TNK2, SUBCELLULAR LOCATION, PHOSPHORYLATION,
AND FUNCTION.
PubMed=11700021; DOI=10.1006/bbrc.2001.5890;
Oda T., Muramatsu M.-A., Isogai T., Masuho Y., Asano S., Yamashita T.;
"HSH2: a novel SH2 domain-containing adapter protein involved in
tyrosine kinase signaling in hematopoietic cells.";
Biochem. Biophys. Res. Commun. 288:1078-1086(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=Spleen;
PubMed=12960172; DOI=10.1074/jbc.M306283200;
Greene T.A., Powell P., Nzerem C., Shapiro M.J., Shapiro V.S.;
"Cloning and characterization of ALX, an adaptor downstream of CD28.";
J. Biol. Chem. 278:45128-45134(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
MUTAGENESIS OF 10-PRO--PRO-13; PRO-116; TYR-135; 192-PRO--PRO-195;
TYR-341 AND 346-PRO--PRO-349, FUNCTION, PHOSPHORYLATION, AND
SUBCELLULAR LOCATION.
PubMed=15284240; DOI=10.1074/jbc.M404198200;
Shapiro M.J., Powell P., Ndubuizu A., Nzerem C., Shapiro V.S.;
"The ALX Src homology 2 domain is both necessary and sufficient to
inhibit T cell receptor/CD28-mediated up-regulation of RE/AP.";
J. Biol. Chem. 279:40647-40652(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=16169852; DOI=10.1074/jbc.M507441200;
Shapiro M.J., Chen Y.-Y., Shapiro V.S.;
"The carboxyl-terminal segment of the adaptor protein ALX directs its
nuclear export during T cell activation.";
J. Biol. Chem. 280:38242-38246(2005).
[9]
STRUCTURE BY NMR OF 24-129.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH2 domain of human HSH2D protein.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: May be a modulator of the apoptotic response through its
ability to affect mitochondrial stability (By similarity). Adapter
protein involved in tyrosine kinase and CD28 signaling. Seems to
affect CD28-mediated activation of the RE/AP element of the
interleukin-2 promoter. {ECO:0000250, ECO:0000269|PubMed:11700021,
ECO:0000269|PubMed:12960172, ECO:0000269|PubMed:15284240}.
-!- SUBUNIT: Interacts with FES and TNK2.
{ECO:0000269|PubMed:11700021}.
-!- INTERACTION:
P10721:KIT; NbExp=5; IntAct=EBI-3919324, EBI-1379503;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96JZ2-1; Sequence=Displayed;
Name=2;
IsoId=Q96JZ2-2; Sequence=VSP_018052;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in spleen and
hematopoietic cells such as peripheral blood leukocytes and weakly
expressed in prostate, thymus, heart, small intestine and
placenta. {ECO:0000269|PubMed:11700021,
ECO:0000269|PubMed:12960172}.
-!- PTM: May be phosphorylated by FES and ACK1.
{ECO:0000269|PubMed:11700021, ECO:0000269|PubMed:15284240}.
-----------------------------------------------------------------------
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EMBL; AY319652; AAQ81285.1; -; mRNA.
EMBL; AK027792; BAB55372.1; -; mRNA.
EMBL; AK131222; BAD18408.1; -; mRNA.
EMBL; AC008894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC020911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84529.1; -; Genomic_DNA.
EMBL; BC025237; AAH25237.1; -; mRNA.
CCDS; CCDS74304.1; -. [Q96JZ2-1]
PIR; JC7781; JC7781.
RefSeq; NP_001278203.1; NM_001291274.1. [Q96JZ2-2]
RefSeq; NP_116244.1; NM_032855.3. [Q96JZ2-1]
UniGene; Hs.631617; -.
PDB; 2CS0; NMR; -; A=24-129.
PDBsum; 2CS0; -.
ProteinModelPortal; Q96JZ2; -.
SMR; Q96JZ2; -.
BioGrid; 124375; 12.
IntAct; Q96JZ2; 15.
STRING; 9606.ENSP00000253680; -.
iPTMnet; Q96JZ2; -.
PhosphoSitePlus; Q96JZ2; -.
BioMuta; HSH2D; -.
DMDM; 74732160; -.
EPD; Q96JZ2; -.
MaxQB; Q96JZ2; -.
PaxDb; Q96JZ2; -.
PeptideAtlas; Q96JZ2; -.
PRIDE; Q96JZ2; -.
ProteomicsDB; 77021; -.
ProteomicsDB; 77022; -. [Q96JZ2-2]
DNASU; 84941; -.
Ensembl; ENST00000613986; ENSP00000483354; ENSG00000196684. [Q96JZ2-1]
Ensembl; ENST00000616645; ENSP00000482604; ENSG00000196684. [Q96JZ2-1]
GeneID; 84941; -.
KEGG; hsa:84941; -.
UCSC; uc032hot.2; human. [Q96JZ2-1]
CTD; 84941; -.
DisGeNET; 84941; -.
EuPathDB; HostDB:ENSG00000196684.12; -.
GeneCards; HSH2D; -.
HGNC; HGNC:24920; HSH2D.
HPA; HPA036616; -.
MIM; 608349; gene.
neXtProt; NX_Q96JZ2; -.
OpenTargets; ENSG00000196684; -.
PharmGKB; PA134927763; -.
eggNOG; ENOG410IXE0; Eukaryota.
eggNOG; ENOG4111Y35; LUCA.
GeneTree; ENSGT00570000079047; -.
HOGENOM; HOG000112961; -.
HOVERGEN; HBG081611; -.
InParanoid; Q96JZ2; -.
OMA; LTQPCGQ; -.
OrthoDB; EOG091G0C3M; -.
PhylomeDB; Q96JZ2; -.
TreeFam; TF336893; -.
SignaLink; Q96JZ2; -.
ChiTaRS; HSH2D; human.
EvolutionaryTrace; Q96JZ2; -.
GenomeRNAi; 84941; -.
PRO; PR:Q96JZ2; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000196684; -.
CleanEx; HS_HSH2D; -.
ExpressionAtlas; Q96JZ2; baseline and differential.
Genevisible; Q96JZ2; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IEA:Ensembl.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; IEA:Ensembl.
GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0042110; P:T cell activation; IEA:Ensembl.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035047; HSH2D.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
PANTHER; PTHR14388:SF3; PTHR14388:SF3; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Nucleus; Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1 352 Hematopoietic SH2 domain-containing
protein.
/FTId=PRO_0000233129.
DOMAIN 34 125 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
VAR_SEQ 1 72 MTEAGKLPLPLPPRLDWFVHTQMGQLAQDGVPEWFHGAISR
EDAENLLESQPLGSFLIRVSHSHVGYTLSYK -> MRGSRM
SQPPQCLRR (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_018052.
MUTAGEN 10 13 PLPP->ALPA: No change in the ability to
inhibit RE/AP up-regulation in response
to TCR/CD28 stimulation.
{ECO:0000269|PubMed:15284240}.
MUTAGEN 59 59 R->K: Loss of the ability to inhibit
RE/AP up-regulation in response to
TCR/CD28 stimulation.
MUTAGEN 116 116 P->A: No change in the ability to inhibit
RE/AP up-regulation in response to
TCR/CD28 stimulation.
{ECO:0000269|PubMed:15284240}.
MUTAGEN 135 135 Y->F: No change in the ability to inhibit
RE/AP up-regulation in response to
TCR/CD28 stimulation.
{ECO:0000269|PubMed:15284240}.
MUTAGEN 192 195 PKSP->AKSA: No change in the ability to
inhibit RE/AP up-regulation in response
to TCR/CD28 stimulation.
{ECO:0000269|PubMed:15284240}.
MUTAGEN 341 341 Y->F: No change in the ability to inhibit
RE/AP up-regulation in response to
TCR/CD28 stimulation.
{ECO:0000269|PubMed:15284240}.
MUTAGEN 346 349 PFAP->AFAA: No change in the ability to
inhibit RE/AP up-regulation in response
to TCR/CD28 stimulation.
{ECO:0000269|PubMed:15284240}.
CONFLICT 180 180 R -> G (in Ref. 3; BAD18408).
{ECO:0000305}.
STRAND 28 30 {ECO:0000244|PDB:2CS0}.
STRAND 33 35 {ECO:0000244|PDB:2CS0}.
HELIX 41 49 {ECO:0000244|PDB:2CS0}.
STRAND 56 60 {ECO:0000244|PDB:2CS0}.
STRAND 62 71 {ECO:0000244|PDB:2CS0}.
STRAND 74 76 {ECO:0000244|PDB:2CS0}.
STRAND 78 84 {ECO:0000244|PDB:2CS0}.
STRAND 99 101 {ECO:0000244|PDB:2CS0}.
HELIX 102 109 {ECO:0000244|PDB:2CS0}.
SEQUENCE 352 AA; 39002 MW; CB6B7EAE424A08C3 CRC64;
MTEAGKLPLP LPPRLDWFVH TQMGQLAQDG VPEWFHGAIS REDAENLLES QPLGSFLIRV
SHSHVGYTLS YKAQSSCCHF MVKLLDDGTF MIPGEKVAHT SLDALVTFHQ QKPIEPRREL
LTQPCRQKDP ANVDYEDLFL YSNAVAEEAA CPVSAPEEAS PKPVLCHQSK ERKPSAEMNR
ITTKEATSSC PPKSPLGETR QKLWRSLKML PERGQRVRQQ LKSHLATVNL SSLLDVRRST
VISGPGTGKG SQDHSGDPTS GDRGYTDPCV ATSLKSPSQP QAPKDRKVPT RKAERSVSCI
EVTPGDRSWH QMVVRALSSQ ESKPEHQGLA EPENDQLPEE YQQPPPFAPG YC


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