HSH2D_MOUSE
ID HSH2D_MOUSE Reviewed; 334 AA.
AC Q6VYH9; Q52KL3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Hematopoietic SH2 domain-containing protein;
DE Short=Hematopoietic SH2 protein;
DE AltName: Full=Adaptor in lymphocytes of unknown function X;
GN Name=Hsh2d; Synonyms=Alx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=12960172; DOI=10.1074/jbc.m306283200;
RA Greene T.A., Powell P., Nzerem C., Shapiro M.J., Shapiro V.S.;
RT "Cloning and characterization of ALX, an adaptor downstream of CD28.";
RL J. Biol. Chem. 278:45128-45134(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15569688; DOI=10.1074/jbc.m407690200;
RA Herrin B.R., Groeger A.L., Justement L.B.;
RT "The adaptor protein HSH2 attenuates apoptosis in response to ligation of
RT the B cell antigen receptor complex on the B lymphoma cell line, WEHI-
RT 231.";
RL J. Biol. Chem. 280:3507-3515(2005).
CC -!- FUNCTION: Adapter protein involved in tyrosine kinase and CD28
CC signaling (By similarity). May be a modulator of the apoptotic response
CC through its ability to affect mitochondrial stability. {ECO:0000250,
CC ECO:0000269|PubMed:15569688}.
CC -!- SUBUNIT: Interacts with FES and TNK2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15569688}.
CC Mitochondrion {ECO:0000269|PubMed:15569688}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in spleen and thymus.
CC Appears not to be expressed in heart, brain, liver, kidney, embryo,
CC lung and ovary. {ECO:0000269|PubMed:12960172}.
CC -!- PTM: May be phosphorylated by FES and ACK1. {ECO:0000250}.
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DR EMBL; AY319653; AAQ81286.1; -; mRNA.
DR EMBL; AK157000; BAE33927.1; -; mRNA.
DR EMBL; BC094291; AAH94291.1; -; mRNA.
DR CCDS; CCDS22410.1; -.
DR RefSeq; NP_922935.1; NM_197944.1.
DR AlphaFoldDB; Q6VYH9; -.
DR SMR; Q6VYH9; -.
DR STRING; 10090.ENSMUSP00000127575; -.
DR iPTMnet; Q6VYH9; -.
DR PhosphoSitePlus; Q6VYH9; -.
DR EPD; Q6VYH9; -.
DR PaxDb; Q6VYH9; -.
DR PRIDE; Q6VYH9; -.
DR ProteomicsDB; 267020; -.
DR Antibodypedia; 27308; 165 antibodies from 25 providers.
DR DNASU; 209488; -.
DR Ensembl; ENSMUST00000072097; ENSMUSP00000071970; ENSMUSG00000062007.
DR Ensembl; ENSMUST00000165324; ENSMUSP00000127575; ENSMUSG00000062007.
DR GeneID; 209488; -.
DR KEGG; mmu:209488; -.
DR UCSC; uc009mfl.1; mouse.
DR CTD; 84941; -.
DR MGI; MGI:2676364; Hsh2d.
DR VEuPathDB; HostDB:ENSMUSG00000062007; -.
DR eggNOG; ENOG502RZYN; Eukaryota.
DR GeneTree; ENSGT00940000161678; -.
DR HOGENOM; CLU_067582_0_0_1; -.
DR InParanoid; Q6VYH9; -.
DR OMA; KAQSCCR; -.
DR OrthoDB; 1404128at2759; -.
DR PhylomeDB; Q6VYH9; -.
DR TreeFam; TF336893; -.
DR BioGRID-ORCS; 209488; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Fpr3; mouse.
DR PRO; PR:Q6VYH9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6VYH9; protein.
DR Bgee; ENSMUSG00000062007; Expressed in granulocyte and 22 other tissues.
DR Genevisible; Q6VYH9; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:MGI.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:MGI.
DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0042110; P:T cell activation; IDA:MGI.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035047; HSH2D.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR14388:SF3; PTHR14388:SF3; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Mitochondrion; Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..334
FT /note="Hematopoietic SH2 domain-containing protein"
FT /id="PRO_0000233130"
FT DOMAIN 34..125
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 91
FT /note="A -> T (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="I -> F (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="S -> SS (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="R -> Q (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="L -> S (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="Q -> R (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="S -> P (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="V -> I (in Ref. 3; AAH94291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37233 MW; 32C3B3728C33F560 CRC64;
MAEARRLPPP LPPRLDWFVH TQADLLAQSG IPEWFHGTIS REAAENMLES QPLGTFLIRV
SHSHVGYTLS YKAQTCCRHF MVKLSEDGTC AFAGDHMTHA SLHALVTFHQ QKPIRPFGEL
LTQACGQEDP ANVDYEDLFL YSNALVQDAE SQILRTEVQR SSCPPEEASE RKPSTTTKGE
FASASCSPKA LFEDSGQKLW KNLRSLPQTS QRVKQRLTSH LLAMNLLGDA RQVAQQHHSP
VTRAFSWDST SHSEDSCAAT TSLQNPAEPQ ALRGREATFR DSRPASWRKA FSGVKAWRGK
VVRALSAQEP VDFPEAQGWL PEEYLPPPPF APGY
