SH24A_HUMAN
ID SH24A_HUMAN Reviewed; 454 AA.
AC Q9H788; B4DDR1; Q5XKC1; Q6NXE9; Q86YM2; Q96C88; Q9H7F7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=SH2 domain-containing protein 4A;
DE AltName: Full=Protein SH(2)A;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 38;
GN Name=SH2D4A; Synonyms=PPP1R38, SH2A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP GLY-209; GLY-216 AND ALA-263.
RC TISSUE=Adipose tissue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-275.
RC TISSUE=Ovary, Prostate, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 172-454 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=12476414;
RA Dai S., Zhao Y., Ding Q.;
RT "A novel member of SH(2) signaling protein family: cloning and
RT characterization of SH(2)A gene.";
RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 19:458-462(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18641339; DOI=10.4049/jimmunol.181.3.2019;
RA Lapinski P.E., Oliver J.A., Kamen L.A., Hughes E.D., Saunders T.L.,
RA King P.D.;
RT "Genetic analysis of SH2D4A, a novel adapter protein related to T cell-
RT specific adapter and adapter protein in lymphocytes of unknown function,
RT reveals a redundant function in T cells.";
RL J. Immunol. 181:2019-2027(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, AND INTERACTION WITH ESR1.
RX PubMed=19712589; DOI=10.5483/bmbrep.2009.42.8.516;
RA Li T., Li W., Lu J., Liu H., Li Y., Zhao Y.;
RT "SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC
RT pathway.";
RL BMB Rep. 42:516-522(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Inhibits estrogen-induced cell proliferation by competing
CC with PLCG for binding to ESR1, blocking the effect of estrogen on PLCG
CC and repressing estrogen-induced proliferation. May play a role in T-
CC cell development and function. {ECO:0000269|PubMed:18641339,
CC ECO:0000269|PubMed:19712589}.
CC -!- SUBUNIT: Interacts with ESR1. {ECO:0000269|PubMed:19712589}.
CC -!- INTERACTION:
CC Q9H788; P13196: ALAS1; NbExp=3; IntAct=EBI-747035, EBI-3905054;
CC Q9H788; Q7LC44: ARC; NbExp=3; IntAct=EBI-747035, EBI-750550;
CC Q9H788; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-747035, EBI-465872;
CC Q9H788; A2RRN7: CADPS; NbExp=3; IntAct=EBI-747035, EBI-10179719;
CC Q9H788; O14936: CASK; NbExp=4; IntAct=EBI-747035, EBI-1215506;
CC Q9H788; O14936-4: CASK; NbExp=3; IntAct=EBI-747035, EBI-12007726;
CC Q9H788; P0C7W6: CCDC172; NbExp=3; IntAct=EBI-747035, EBI-2548868;
CC Q9H788; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-747035, EBI-347573;
CC Q9H788; Q01850: CDR2; NbExp=6; IntAct=EBI-747035, EBI-1181367;
CC Q9H788; Q86X02: CDR2L; NbExp=3; IntAct=EBI-747035, EBI-11063830;
CC Q9H788; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-747035, EBI-739624;
CC Q9H788; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-747035, EBI-742887;
CC Q9H788; Q96M91: CFAP53; NbExp=3; IntAct=EBI-747035, EBI-742422;
CC Q9H788; Q9UJU6: DBNL; NbExp=6; IntAct=EBI-747035, EBI-751783;
CC Q9H788; Q9UJU6-2: DBNL; NbExp=3; IntAct=EBI-747035, EBI-12192777;
CC Q9H788; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-747035, EBI-11977403;
CC Q9H788; O94868-3: FCHSD2; NbExp=5; IntAct=EBI-747035, EBI-11958845;
CC Q9H788; A1L4K1: FSD2; NbExp=6; IntAct=EBI-747035, EBI-5661036;
CC Q9H788; Q08379: GOLGA2; NbExp=6; IntAct=EBI-747035, EBI-618309;
CC Q9H788; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-747035, EBI-5916454;
CC Q9H788; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-747035, EBI-473189;
CC Q9H788; Q6IC98: GRAMD4; NbExp=3; IntAct=EBI-747035, EBI-10962409;
CC Q9H788; O75791: GRAP2; NbExp=5; IntAct=EBI-747035, EBI-740418;
CC Q9H788; P62993: GRB2; NbExp=4; IntAct=EBI-747035, EBI-401755;
CC Q9H788; P14317: HCLS1; NbExp=8; IntAct=EBI-747035, EBI-750369;
CC Q9H788; Q6NT76: HMBOX1; NbExp=6; IntAct=EBI-747035, EBI-2549423;
CC Q9H788; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-747035, EBI-10961706;
CC Q9H788; O75031: HSF2BP; NbExp=3; IntAct=EBI-747035, EBI-7116203;
CC Q9H788; Q13422: IKZF1; NbExp=3; IntAct=EBI-747035, EBI-745305;
CC Q9H788; Q6A162: KRT40; NbExp=6; IntAct=EBI-747035, EBI-10171697;
CC Q9H788; O95751: LDOC1; NbExp=8; IntAct=EBI-747035, EBI-740738;
CC Q9H788; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-747035, EBI-741037;
CC Q9H788; P43364: MAGEA11; NbExp=2; IntAct=EBI-747035, EBI-739552;
CC Q9H788; P43360: MAGEA6; NbExp=6; IntAct=EBI-747035, EBI-1045155;
CC Q9H788; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-747035, EBI-12516603;
CC Q9H788; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-747035, EBI-16439278;
CC Q9H788; Q6PF18: MORN3; NbExp=3; IntAct=EBI-747035, EBI-9675802;
CC Q9H788; Q9Y605: MRFAP1; NbExp=5; IntAct=EBI-747035, EBI-995714;
CC Q9H788; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-747035, EBI-742948;
CC Q9H788; Q5JR59-3: MTUS2; NbExp=5; IntAct=EBI-747035, EBI-11522433;
CC Q9H788; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-747035, EBI-10172876;
CC Q9H788; Q9Y2I6: NINL; NbExp=3; IntAct=EBI-747035, EBI-719716;
CC Q9H788; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-747035, EBI-10178410;
CC Q9H788; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-747035, EBI-1105124;
CC Q9H788; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-747035, EBI-79165;
CC Q9H788; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-747035, EBI-949255;
CC Q9H788; Q8ND90: PNMA1; NbExp=6; IntAct=EBI-747035, EBI-302345;
CC Q9H788; P62136: PPP1CA; NbExp=3; IntAct=EBI-747035, EBI-357253;
CC Q9H788; P62140: PPP1CB; NbExp=18; IntAct=EBI-747035, EBI-352350;
CC Q9H788; P31321: PRKAR1B; NbExp=3; IntAct=EBI-747035, EBI-2805516;
CC Q9H788; O43586: PSTPIP1; NbExp=3; IntAct=EBI-747035, EBI-1050964;
CC Q9H788; Q6NUQ1: RINT1; NbExp=6; IntAct=EBI-747035, EBI-726876;
CC Q9H788; Q6FGM0: SH3GL1; NbExp=3; IntAct=EBI-747035, EBI-10173690;
CC Q9H788; Q99961: SH3GL1; NbExp=6; IntAct=EBI-747035, EBI-697911;
CC Q9H788; Q86WV1: SKAP1; NbExp=3; IntAct=EBI-747035, EBI-2477305;
CC Q9H788; O60504: SORBS3; NbExp=6; IntAct=EBI-747035, EBI-741237;
CC Q9H788; Q96R06: SPAG5; NbExp=3; IntAct=EBI-747035, EBI-413317;
CC Q9H788; O75886: STAM2; NbExp=3; IntAct=EBI-747035, EBI-373258;
CC Q9H788; O75558: STX11; NbExp=3; IntAct=EBI-747035, EBI-714135;
CC Q9H788; O75410: TACC1; NbExp=4; IntAct=EBI-747035, EBI-624237;
CC Q9H788; O75410-7: TACC1; NbExp=3; IntAct=EBI-747035, EBI-12007872;
CC Q9H788; Q9UBB9: TFIP11; NbExp=8; IntAct=EBI-747035, EBI-1105213;
CC Q9H788; Q12933: TRAF2; NbExp=3; IntAct=EBI-747035, EBI-355744;
CC Q9H788; P36406: TRIM23; NbExp=3; IntAct=EBI-747035, EBI-740098;
CC Q9H788; P14373: TRIM27; NbExp=3; IntAct=EBI-747035, EBI-719493;
CC Q9H788; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-747035, EBI-11059915;
CC Q9H788; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-747035, EBI-948354;
CC Q9H788; Q5T124: UBXN11; NbExp=3; IntAct=EBI-747035, EBI-746004;
CC Q9H788; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-747035, EBI-2799833;
CC Q9H788; Q9NZC7-5: WWOX; NbExp=5; IntAct=EBI-747035, EBI-12040603;
CC Q9H788; Q96QA6: YPEL2; NbExp=3; IntAct=EBI-747035, EBI-6658719;
CC Q9H788; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-747035, EBI-12030590;
CC Q9H788; Q8N720: ZNF655; NbExp=3; IntAct=EBI-747035, EBI-625509;
CC Q9H788; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-747035, EBI-10251462;
CC Q9H788-2; Q01850: CDR2; NbExp=3; IntAct=EBI-10308083, EBI-1181367;
CC Q9H788-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10308083, EBI-739624;
CC Q9H788-2; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-10308083, EBI-751783;
CC Q9H788-2; A1L4K1: FSD2; NbExp=3; IntAct=EBI-10308083, EBI-5661036;
CC Q9H788-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10308083, EBI-618309;
CC Q9H788-2; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10308083, EBI-742948;
CC Q9H788-2; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-10308083, EBI-10172876;
CC Q9H788-2; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-10308083, EBI-1105124;
CC Q9H788-2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10308083, EBI-726876;
CC Q9H788-2; Q6FGM0: SH3GL1; NbExp=3; IntAct=EBI-10308083, EBI-10173690;
CC Q9H788-2; Q86WV1: SKAP1; NbExp=3; IntAct=EBI-10308083, EBI-2477305;
CC Q9H788-2; O94875: SORBS2; NbExp=3; IntAct=EBI-10308083, EBI-311323;
CC Q9H788-2; O60504: SORBS3; NbExp=3; IntAct=EBI-10308083, EBI-741237;
CC Q9H788-2; O75886: STAM2; NbExp=3; IntAct=EBI-10308083, EBI-373258;
CC Q9H788-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-10308083, EBI-1105213;
CC Q9H788-2; P36406: TRIM23; NbExp=3; IntAct=EBI-10308083, EBI-740098;
CC Q9H788-2; P14373: TRIM27; NbExp=3; IntAct=EBI-10308083, EBI-719493;
CC Q9H788-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10308083, EBI-739895;
CC Q9H788-2; Q05516: ZBTB16; NbExp=3; IntAct=EBI-10308083, EBI-711925;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18641339}.
CC Note=Located at podocyte foot processes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H788-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H788-2; Sequence=VSP_042784;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Aberrantly expressed in
CC some cancers. {ECO:0000269|PubMed:12476414}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH67117.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO41715.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO41715.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14935.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK024620; BAB14935.1; ALT_INIT; mRNA.
DR EMBL; AK024799; BAB15010.1; -; mRNA.
DR EMBL; AK293301; BAG56822.1; -; mRNA.
DR EMBL; AC068880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014525; AAH14525.2; -; mRNA.
DR EMBL; BC067117; AAH67117.1; ALT_FRAME; mRNA.
DR EMBL; BC082982; AAH82982.1; -; mRNA.
DR EMBL; AY190323; AAO41715.1; ALT_SEQ; mRNA.
DR CCDS; CCDS55206.1; -. [Q9H788-2]
DR CCDS; CCDS6009.1; -. [Q9H788-1]
DR RefSeq; NP_001167630.1; NM_001174159.1. [Q9H788-1]
DR RefSeq; NP_001167631.1; NM_001174160.1. [Q9H788-2]
DR RefSeq; NP_071354.2; NM_022071.3. [Q9H788-1]
DR AlphaFoldDB; Q9H788; -.
DR BioGRID; 121977; 117.
DR ELM; Q9H788; -.
DR IntAct; Q9H788; 85.
DR MINT; Q9H788; -.
DR STRING; 9606.ENSP00000265807; -.
DR iPTMnet; Q9H788; -.
DR MetOSite; Q9H788; -.
DR PhosphoSitePlus; Q9H788; -.
DR BioMuta; SH2D4A; -.
DR DMDM; 74725117; -.
DR CPTAC; CPTAC-1003; -.
DR EPD; Q9H788; -.
DR jPOST; Q9H788; -.
DR MassIVE; Q9H788; -.
DR MaxQB; Q9H788; -.
DR PaxDb; Q9H788; -.
DR PeptideAtlas; Q9H788; -.
DR PRIDE; Q9H788; -.
DR ProteomicsDB; 81087; -. [Q9H788-1]
DR ProteomicsDB; 81088; -. [Q9H788-2]
DR Antibodypedia; 968; 226 antibodies from 33 providers.
DR DNASU; 63898; -.
DR Ensembl; ENST00000265807.8; ENSP00000265807.3; ENSG00000104611.12. [Q9H788-1]
DR Ensembl; ENST00000518040.5; ENSP00000429482.1; ENSG00000104611.12. [Q9H788-2]
DR Ensembl; ENST00000519207.5; ENSP00000428684.1; ENSG00000104611.12. [Q9H788-1]
DR GeneID; 63898; -.
DR KEGG; hsa:63898; -.
DR MANE-Select; ENST00000265807.8; ENSP00000265807.3; NM_022071.4; NP_071354.2.
DR UCSC; uc003wzb.4; human. [Q9H788-1]
DR CTD; 63898; -.
DR DisGeNET; 63898; -.
DR GeneCards; SH2D4A; -.
DR HGNC; HGNC:26102; SH2D4A.
DR HPA; ENSG00000104611; Low tissue specificity.
DR MIM; 614968; gene.
DR neXtProt; NX_Q9H788; -.
DR OpenTargets; ENSG00000104611; -.
DR PharmGKB; PA134891945; -.
DR VEuPathDB; HostDB:ENSG00000104611; -.
DR eggNOG; ENOG502QVV5; Eukaryota.
DR GeneTree; ENSGT00940000157357; -.
DR HOGENOM; CLU_029296_1_0_1; -.
DR InParanoid; Q9H788; -.
DR OMA; YPCGQQG; -.
DR OrthoDB; 782492at2759; -.
DR PhylomeDB; Q9H788; -.
DR TreeFam; TF336893; -.
DR PathwayCommons; Q9H788; -.
DR SignaLink; Q9H788; -.
DR BioGRID-ORCS; 63898; 14 hits in 1068 CRISPR screens.
DR GeneWiki; SH2D4A; -.
DR GenomeRNAi; 63898; -.
DR Pharos; Q9H788; Tbio.
DR PRO; PR:Q9H788; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H788; protein.
DR Bgee; ENSG00000104611; Expressed in secondary oocyte and 173 other tissues.
DR ExpressionAtlas; Q9H788; baseline and differential.
DR Genevisible; Q9H788; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW SH2 domain.
FT CHAIN 1..454
FT /note="SH2 domain-containing protein 4A"
FT /id="PRO_0000233133"
FT DOMAIN 347..440
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D7V1"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..60
FT /note="MLKQILSEMYIDPDLLAELSEEQKQILFFKMREEQIRRWKEREAAMERKESL
FT PVKPRPKK -> MWRVIEPPCPGAPST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042784"
FT VARIANT 209
FT /note="E -> G (in dbSNP:rs35647122)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_051350"
FT VARIANT 216
FT /note="E -> G (in dbSNP:rs4921637)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_026055"
FT VARIANT 263
FT /note="G -> A (in dbSNP:rs877386)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_026056"
FT VARIANT 275
FT /note="S -> N (in dbSNP:rs34608771)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051351"
FT CONFLICT 95
FT /note="N -> T (in Ref. 1; BAB14935)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="N -> T (in Ref. 4; AAO41715)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="K -> R (in Ref. 4; AAO41715)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="A -> V (in Ref. 4; AAO41715)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="K -> E (in Ref. 1; BAB14935)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="P -> S (in Ref. 4; AAO41715)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="C -> R (in Ref. 1; BAB14935)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 52727 MW; 2FC21D4E07FDA922 CRC64;
MLKQILSEMY IDPDLLAELS EEQKQILFFK MREEQIRRWK EREAAMERKE SLPVKPRPKK
ENGKSVHWKL GADKEVWVWV MGEHHLDKPY DVLCNEIIAE RARLKAEQEA EEPRKTHSEE
FTNSLKTKSQ YHDLQAPDNQ QTKDIWKKVA EKEELEQGSR PAPTLEEEKI RSLSSSSRNI
QQMLADSINR MKAYAFHQKK ESMKKKQDEE INQIEEERTK QICKSWKEDS EWQASLRKSK
AADEKRRSLA KQAREDYKRL SLGAQKGRGG ERLQSPLRVP QKPERPPLPP KPQFLNSGAY
PQKPLRNQGV VRTLSSSAQE DIIRWFKEEQ LPLRAGYQKT SDTIAPWFHG ILTLKKANEL
LLSTGMPGSF LIRVSERIKG YALSYLSEDG CKHFLIDASA DAYSFLGVDQ LQHATLADLV
EYHKEEPITS LGKELLLYPC GQQDQLPDYL ELFE
