ID   SOCS2_HUMAN             Reviewed;         198 AA.
AC   O14508; A8K3D1; O14542; O95102; Q9UKS5;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Suppressor of cytokine signaling 2;
DE            Short=SOCS-2;
DE   AltName: Full=Cytokine-inducible SH2 protein 2;
DE            Short=CIS-2;
DE   AltName: Full=STAT-induced STAT inhibitor 2;
DE            Short=SSI-2;
GN   Name=SOCS2; Synonyms=CIS2, SSI2, STATI2;
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 [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=T-cell lymphoma;
RX   PubMed=9266833; DOI=10.1006/bbrc.1997.7080;
RA   Minamoto S., Ikegame K., Ueno K., Narazaki M., Naka T., Yamamoto H.,
RA   Matsumoto T., Saito H., Hosoe S., Kishimoto T.;
RT   "Cloning and functional analysis of new members of STAT induced STAT
RT   inhibitor (SSI) family: SSI-2 and SSI-3.";
RL   Biochem. Biophys. Res. Commun. 237:79-83(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9344848; DOI=10.1006/bbrc.1997.7484;
RA   Masuhara M., Sakamoto H., Matsumoto A., Suzuki R., Yasukawa H., Mitsui K.,
RA   Wakioka T., Tanimura S., Sasaki A., Misawa H., Yokouchi M., Ohtsubo M.,
RA   Yoshimura A.;
RT   "Cloning and characterization of novel CIS family genes.";
RL   Biochem. Biophys. Res. Commun. 239:439-446(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tu Q., Yu L., Zhang Q.;
RT   "Cloning of a novel human gene coding human suppressor of cytokine
RT   signaling-2 (HsSOCS-2).";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH IGF1R.
RC   TISSUE=Fetal brain;
RX   PubMed=9727029; DOI=10.1074/jbc.273.37.24095;
RA   Dey B.R., Spence S.L., Nissley P., Furlanetto R.W.;
RT   "Interaction of human suppressor of cytokine signaling (SOCS)-2 with the
RT   insulin-like growth factor-I receptor.";
RL   J. Biol. Chem. 273:24095-24101(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Lung;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-198.
RX   PubMed=10512686; DOI=10.1006/geno.1999.5937;
RA   Yandava C.N., Pillari A., Drazen J.M.;
RT   "Radiation hybrid and cytogenetic mapping of SOCS1 and SOCS2 to chromosomes
RT   16p13 and 12q, respectively.";
RL   Genomics 61:108-111(1999).
RN   [9]
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   [10]
RP   INTERACTION WITH DCUN1D1.
RX   PubMed=23401859; DOI=10.1128/mcb.01342-12;
RA   Heir P., Sufan R.I., Greer S.N., Poon B.P., Lee J.E., Ohh M.;
RT   "DCNL1 functions as a substrate sensor and activator of cullin 2-RING
RT   ligase.";
RL   Mol. Cell. Biol. 33:1621-1631(2013).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
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   [12]
RP   PHOSPHORYLATION AT SER-52, UBIQUITINATION AT LYS-173, PROTEASOMAL
RP   DEGRADATION, MUTAGENESIS OF LYS-173, INTERACTION WITH AREL1, AND
RP   CHARACTERIZATION OF VARIANT ASN-52.
RX   PubMed=31578312; DOI=10.1172/jci.insight.129110;
RA   Lear T.B., McKelvey A.C., Evankovich J.W., Rajbhandari S., Coon T.A.,
RA   Dunn S.R., Londino J.D., McVerry B.J., Zhang Y., Valenzi E., Burton C.L.,
RA   Gordon R., Gingras S., Lockwood K.C., Jurczak M.J., Lafyatis R.,
RA   Shlomchik M.J., Liu Y., Chen B.B.;
RT   "KIAA0317 regulates pulmonary inflammation through SOCS2 degradation.";
RL   JCI Insight 4:0-0(2019).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE ELONGIN BC
RP   COMPLEX.
RX   PubMed=16675548; DOI=10.1073/pnas.0601638103;
RA   Bullock A.N., Debreczeni J.E., Edwards A.M., Sundstrom M., Knapp S.;
RT   "Crystal structure of the SOCS2-elongin C-elongin B complex defines a
RT   prototypical SOCS box ubiquitin ligase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7637-7642(2006).
CC   -!- FUNCTION: SOCS family proteins form part of a classical negative
CC       feedback system that regulates cytokine signal transduction. SOCS2
CC       appears to be a negative regulator in the growth hormone/IGF1 signaling
CC       pathway. Probable substrate recognition component of a SCF-like ECS
CC       (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase
CC       complex which mediates the ubiquitination and subsequent proteasomal
CC       degradation of target proteins.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with IGF1R (PubMed:9727029). Associates with the
CC       Elongin BC complex (PubMed:16675548). Interacts with AREL1
CC       (PubMed:31578312). Interacts with PRKCA (By similarity). Interacts with
CC       DCUN1D1 (PubMed:23401859). {ECO:0000250|UniProtKB:O35717,
CC       ECO:0000269|PubMed:16675548, ECO:0000269|PubMed:23401859,
CC       ECO:0000269|PubMed:31578312, ECO:0000269|PubMed:9727029}.
CC   -!- INTERACTION:
CC       O14508; Q93034: CUL5; NbExp=9; IntAct=EBI-617737, EBI-1057139;
CC       O14508; Q15369: ELOC; NbExp=2; IntAct=EBI-617737, EBI-301231;
CC       O14508; P19235: EPOR; NbExp=3; IntAct=EBI-617737, EBI-617321;
CC       O14508; P10721: KIT; NbExp=4; IntAct=EBI-617737, EBI-1379503;
CC       O14508; O75716: STK16; NbExp=3; IntAct=EBI-617737, EBI-749295;
CC       O14508; P40337-2: VHL; NbExp=3; IntAct=EBI-617737, EBI-12157263;
CC       O14508; P07947: YES1; NbExp=3; IntAct=EBI-617737, EBI-515331;
CC   -!- TISSUE SPECIFICITY: High expression in heart, placenta, lung, kidney
CC       and prostate. Predominantly expressed in pulmonary epithelia cells,
CC       specifically type II pneumocytes. {ECO:0000269|PubMed:31578312,
CC       ECO:0000269|PubMed:9266833}.
CC   -!- INDUCTION: By a subset of cytokines, including EPO/erythropoietin and
CC       CSF2/GM-CSF.
CC   -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC       BC complex, an adapter module in different E3 ubiquitin ligase
CC       complexes.
CC   -!- PTM: Ubiquitinated; mediated by AREL1 and leading to its subsequent
CC       proteasomal degradation (PubMed:31578312). Ubiquitination is dependent
CC       on its phosphorylation at Ser-52, by PKC (PubMed:31578312).
CC       Ubiquitination is stimulated by LPS (By similarity).
CC       {ECO:0000250|UniProtKB:O35717, ECO:0000269|PubMed:31578312}.
CC   -!- PTM: Phosphorylation at Ser-52 by PKC facilitates its ubiquitination
CC       and proteasomal degradation. {ECO:0000269|PubMed:31578312}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44123/SOCS2";
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DR   EMBL; AB004903; BAA22429.1; -; mRNA.
DR   EMBL; AB006966; BAA22536.1; -; mRNA.
DR   EMBL; AF020590; AAC98896.1; -; mRNA.
DR   EMBL; AF037989; AAC34745.1; -; mRNA.
DR   EMBL; AK290546; BAF83235.1; -; mRNA.
DR   EMBL; AK313165; BAG35983.1; -; mRNA.
DR   EMBL; CH471054; EAW97492.1; -; Genomic_DNA.
DR   EMBL; BC010399; AAH10399.1; -; mRNA.
DR   EMBL; AF132441; AAD27710.1; -; Genomic_DNA.
DR   CCDS; CCDS9047.1; -.
DR   PIR; JC5626; JC5626.
DR   PIR; JC5760; JC5760.
DR   RefSeq; NP_001257396.1; NM_001270467.1.
DR   RefSeq; NP_001257397.1; NM_001270468.1.
DR   RefSeq; NP_001257398.1; NM_001270469.1.
DR   RefSeq; NP_001257399.1; NM_001270470.1.
DR   RefSeq; NP_001257400.1; NM_001270471.1.
DR   RefSeq; NP_003868.1; NM_003877.4.
DR   RefSeq; XP_016875645.1; XM_017020156.1.
DR   PDB; 2C9W; X-ray; 1.90 A; A=32-198.
DR   PDB; 4JGH; X-ray; 3.00 A; A=32-198.
DR   PDB; 5BO4; X-ray; 2.90 A; A/D/G/J/M/P=32-198.
DR   PDB; 6I4X; X-ray; 2.69 A; A=30-198.
DR   PDB; 6I5J; X-ray; 2.80 A; A/D=30-198.
DR   PDB; 6I5N; X-ray; 1.98 A; A/D=30-198.
DR   PDB; 7M6T; X-ray; 3.19 A; A=32-198.
DR   PDB; 7ZLM; X-ray; 1.79 A; A/D/G/J=32-198.
DR   PDB; 7ZLN; X-ray; 2.60 A; A=32-198.
DR   PDB; 7ZLO; X-ray; 2.22 A; A=32-198.
DR   PDB; 7ZLP; X-ray; 1.94 A; A=32-198.
DR   PDB; 7ZLR; X-ray; 2.01 A; A=32-198.
DR   PDB; 7ZLS; X-ray; 1.92 A; A/D/G/J=32-198.
DR   PDBsum; 2C9W; -.
DR   PDBsum; 4JGH; -.
DR   PDBsum; 5BO4; -.
DR   PDBsum; 6I4X; -.
DR   PDBsum; 6I5J; -.
DR   PDBsum; 6I5N; -.
DR   PDBsum; 7M6T; -.
DR   PDBsum; 7ZLM; -.
DR   PDBsum; 7ZLN; -.
DR   PDBsum; 7ZLO; -.
DR   PDBsum; 7ZLP; -.
DR   PDBsum; 7ZLR; -.
DR   PDBsum; 7ZLS; -.
DR   AlphaFoldDB; O14508; -.
DR   SMR; O14508; -.
DR   BioGRID; 114362; 97.
DR   DIP; DIP-29569N; -.
DR   IntAct; O14508; 14.
DR   MINT; O14508; -.
DR   STRING; 9606.ENSP00000481249; -.
DR   iPTMnet; O14508; -.
DR   PhosphoSitePlus; O14508; -.
DR   BioMuta; SOCS2; -.
DR   EPD; O14508; -.
DR   MassIVE; O14508; -.
DR   MaxQB; O14508; -.
DR   PaxDb; 9606-ENSP00000481249; -.
DR   PeptideAtlas; O14508; -.
DR   ProteomicsDB; 48046; -.
DR   Pumba; O14508; -.
DR   Antibodypedia; 4158; 343 antibodies from 37 providers.
DR   DNASU; 8835; -.
DR   Ensembl; ENST00000340600.6; ENSP00000339428.2; ENSG00000120833.14.
DR   Ensembl; ENST00000536696.6; ENSP00000442898.2; ENSG00000120833.14.
DR   Ensembl; ENST00000549122.5; ENSP00000447161.1; ENSG00000120833.14.
DR   Ensembl; ENST00000549206.5; ENSP00000448815.1; ENSG00000120833.14.
DR   Ensembl; ENST00000551556.2; ENSP00000449227.1; ENSG00000120833.14.
DR   Ensembl; ENST00000622746.4; ENSP00000481249.1; ENSG00000120833.14.
DR   GeneID; 8835; -.
DR   KEGG; hsa:8835; -.
DR   MANE-Select; ENST00000551556.2; ENSP00000449227.1; NM_001270471.2; NP_001257400.1.
DR   UCSC; uc001tcw.3; human.
DR   AGR; HGNC:19382; -.
DR   CTD; 8835; -.
DR   DisGeNET; 8835; -.
DR   GeneCards; SOCS2; -.
DR   HGNC; HGNC:19382; SOCS2.
DR   HPA; ENSG00000120833; Low tissue specificity.
DR   MIM; 605117; gene.
DR   neXtProt; NX_O14508; -.
DR   OpenTargets; ENSG00000120833; -.
DR   PharmGKB; PA128394542; -.
DR   VEuPathDB; HostDB:ENSG00000120833; -.
DR   eggNOG; KOG4566; Eukaryota.
DR   GeneTree; ENSGT00940000157983; -.
DR   InParanoid; O14508; -.
DR   OMA; LRKTGWY; -.
DR   OrthoDB; 5362214at2759; -.
DR   PhylomeDB; O14508; -.
DR   TreeFam; TF321368; -.
DR   PathwayCommons; O14508; -.
DR   Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-9706369; Negative regulation of FLT3.
DR   Reactome; R-HSA-982772; Growth hormone receptor signaling.
DR   SignaLink; O14508; -.
DR   SIGNOR; O14508; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 8835; 20 hits in 1200 CRISPR screens.
DR   ChiTaRS; SOCS2; human.
DR   EvolutionaryTrace; O14508; -.
DR   GeneWiki; SOCS2; -.
DR   GenomeRNAi; 8835; -.
DR   Pharos; O14508; Tbio.
DR   PRO; PR:O14508; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; O14508; Protein.
DR   Bgee; ENSG00000120833; Expressed in secondary oocyte and 185 other cell types or tissues.
DR   ExpressionAtlas; O14508; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0005131; F:growth hormone receptor binding; NAS:UniProtKB.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:UniProtKB.
DR   GO; GO:0008269; F:JAK pathway signal transduction adaptor activity; TAS:ProtInc.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IDA:BHF-UCL.
DR   GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; TAS:ProtInc.
DR   GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB.
DR   GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
DR   GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
DR   CDD; cd10383; SH2_SOCS2; 1.
DR   CDD; cd03736; SOCS_SOCS2; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.750.20; SOCS box; 1.
DR   IDEAL; IID00523; -.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR035862; SOCS2_SH2.
DR   InterPro; IPR028410; SOCS2_SOCS_box.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10155:SF7; SUPPRESSOR OF CYTOKINE SIGNALING 2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF07525; SOCS_box; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00253; SOCS; 1.
DR   SMART; SM00969; SOCS_box; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF158235; SOCS box-like; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50225; SOCS; 1.
DR   Genevisible; O14508; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Growth regulation; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; SH2 domain; Signal transduction inhibitor;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..198
FT                   /note="Suppressor of cytokine signaling 2"
FT                   /id="PRO_0000181238"
FT   DOMAIN          48..156
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          151..197
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT   REGION          1..75
FT                   /note="Interaction with AREL1"
FT                   /evidence="ECO:0000269|PubMed:31578312"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         52
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:31578312"
FT   CROSSLNK        173
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:31578312"
FT   VARIANT         52
FT                   /note="S -> N (increased protein half-life; reduced
FT                   interaction with AREL1; dbSNP:rs3741676)"
FT                   /evidence="ECO:0000269|PubMed:31578312"
FT                   /id="VAR_052032"
FT   MUTAGEN         87
FT                   /note="K->R: No effect on protein half-life."
FT                   /evidence="ECO:0000269|PubMed:31578312"
FT   MUTAGEN         154
FT                   /note="K->R: No effect on protein half-life."
FT                   /evidence="ECO:0000269|PubMed:31578312"
FT   MUTAGEN         173
FT                   /note="K->R: Increased protein half-life."
FT                   /evidence="ECO:0000269|PubMed:31578312"
FT   CONFLICT        2
FT                   /note="T -> N (in Ref. 3; AAC98896)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        5
FT                   /note="C -> R (in Ref. 2; BAA22536)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31..39
FT                   /note="PQAARLAKA -> RRRRVWRR (in Ref. 3; AAC98896)"
FT                   /evidence="ECO:0000305"
FT   HELIX           33..46
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   HELIX           55..62
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:7ZLN"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:6I5J"
FT   STRAND          81..88
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   STRAND          91..100
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:7ZLO"
FT   HELIX           122..134
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:7ZLP"
FT   HELIX           163..174
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:7ZLM"
FT   HELIX           185..192
FT                   /evidence="ECO:0007829|PDB:7ZLM"
SQ   SEQUENCE   198 AA;  22172 MW;  DAFC4AD97F8182BF CRC64;
     MTLRCLEPSG NGGEGTRSQW GTAGSAEEPS PQAARLAKAL RELGQTGWYW GSMTVNEAKE
     KLKEAPEGTF LIRDSSHSDY LLTISVKTSA GPTNLRIEYQ DGKFRLDSII CVKSKLKQFD
     SVVHLIDYYV QMCKDKRTGP EAPRNGTVHL YLTKPLYTSA PSLQHLCRLT INKCTGAIWG
     LPLPTRLKDY LEEYKFQV
//