SOCS2_HUMAN
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 03-AUG-2022, entry version 192.
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 proteosomal degradation. {ECO:0000269|PubMed:31578312}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SOCS2ID44123ch12q21.html";
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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 PDBsum; 2C9W; -.
DR PDBsum; 4JGH; -.
DR PDBsum; 5BO4; -.
DR PDBsum; 6I4X; -.
DR PDBsum; 6I5J; -.
DR PDBsum; 6I5N; -.
DR PDBsum; 7M6T; -.
DR AlphaFoldDB; O14508; -.
DR SMR; O14508; -.
DR BioGRID; 114362; 89.
DR DIP; DIP-29569N; -.
DR IntAct; O14508; 13.
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; O14508; -.
DR PeptideAtlas; O14508; -.
DR PRIDE; O14508; -.
DR ProteomicsDB; 48046; -.
DR Antibodypedia; 4158; 297 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 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; AGWYWGN; -.
DR OrthoDB; 1135696at2759; -.
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 1122 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 183 other tissues.
DR ExpressionAtlas; O14508; baseline and differential.
DR Genevisible; O14508; HS.
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 Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID00523; -.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028410; SOCS2.
DR InterPro; IPR035862; SOCS2_SH2.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR10155:SF7; PTHR10155:SF7; 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; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
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..45
FT /evidence="ECO:0007829|PDB:2C9W"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:2C9W"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6I4X"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2C9W"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6I5J"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2C9W"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:2C9W"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2C9W"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:2C9W"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2C9W"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:2C9W"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6I5J"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6I5J"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:2C9W"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2C9W"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2C9W"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:2C9W"
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
