SPSB1_HUMAN
ID SPSB1_HUMAN Reviewed; 273 AA.
AC Q96BD6; A2A275; Q59FA1; Q5TIH9; Q9BRY9; Q9H6C5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=SPRY domain-containing SOCS box protein 1;
DE Short=SSB-1;
GN Name=SPSB1; Synonyms=SSB1;
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].
RA Friedel E.J., Nicholson S.E., Nicola N.A., Kile B.T., Hilton D.J.;
RT "SOCS box proteins.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
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 [7]
RP FUNCTION IN AN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, INTERACTION WITH CUL5; RNF7; ELOB AND ELOC, AND MUTAGENESIS
RP OF 260-LEU--PRO-263.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C.,
RA Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1
RT and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
RN [8]
RP INTERACTION WITH MET AND RASA1, PHOSPHORYLATION AT TYR-31, MUTAGENESIS OF
RP TYR-31, AND DOMAIN.
RX PubMed=15713673; DOI=10.1074/jbc.m413897200;
RA Wang D., Li Z., Messing E.M., Wu G.;
RT "The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET
RT and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response
RT element pathway.";
RL J. Biol. Chem. 280:16393-16401(2005).
RN [9]
RP INTERACTION WITH ELONGIN BC COMPLEX AND PAWR.
RX PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
RA Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
RT "Structural basis for protein recognition by B30.2/SPRY domains.";
RL Mol. Cell 24:967-976(2006).
RN [10]
RP FUNCTION, INTERACTION WITH NOS2, SUBCELLULAR LOCATION, AND DOMAIN SOCS BOX.
RX PubMed=21199876; DOI=10.1074/jbc.m110.190678;
RA Nishiya T., Matsumoto K., Maekawa S., Kajita E., Horinouchi T.,
RA Fujimuro M., Ogasawara K., Uehara T., Miwa S.;
RT "Regulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS
RT box-containing proteins.";
RL J. Biol. Chem. 286:9009-9019(2011).
RN [11]
RP INTERACTION WITH EPHB2.
RX PubMed=28931592; DOI=10.1091/mbc.e17-07-0450;
RA Okumura F., Joo-Okumura A., Obara K., Petersen A., Nishikimi A., Fukui Y.,
RA Nakatsukasa K., Kamura T.;
RT "Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by
RT EphB2.";
RL Mol. Biol. Cell 28:3532-3541(2017).
RN [12] {ECO:0007744|PDB:2JK9, ECO:0007744|PDB:3F2O}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 30-233 IN COMPLEX WITH PAWR AND
RP DROSOPHILA VAS, INTERACTION WITH PAWR, AND DOMAIN.
RX PubMed=20561531; DOI=10.1016/j.jmb.2010.06.017;
RA Filippakopoulos P., Low A., Sharpe T.D., Uppenberg J., Yao S., Kuang Z.,
RA Savitsky P., Lewis R.S., Nicholson S.E., Norton R.S., Bullock A.N.;
RT "Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-
RT containing proteins SPSB1, SPSB2, and SPSB4.";
RL J. Mol. Biol. 401:389-402(2010).
CC -!- FUNCTION: Substrate recognition component of a SCF-like ECS (Elongin
CC BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation of
CC target proteins (PubMed:15601820, PubMed:21199876). Negatively
CC regulates nitric oxide (NO) production and limits cellular toxicity in
CC activated macrophages by mediating the ubiquitination and proteasomal
CC degradation of NOS2 (PubMed:21199876). Acts as a bridge which links
CC NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5
CC (PubMed:21199876). {ECO:0000269|PubMed:15601820,
CC ECO:0000269|PubMed:21199876}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the probable ECS(SPSB1) E3 ubiquitin-protein
CC ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and
CC SPSB1 (PubMed:15601820). Interacts with CUL5, RNF7, ELOB and ELOC
CC (PubMed:15601820). Directly interacts with MET tyrosine kinase domain
CC in the presence and in the absence of HGF, however HGF treatment has a
CC positive effect on this interaction (PubMed:15713673). When
CC phosphorylated, interacts with RASA1 without affecting its stability
CC (PubMed:15713673). Interacts (via B30.2/SPRY domain) with PAWR; this
CC interaction is direct and occurs in association with the Elongin BC
CC complex (PubMed:17189197, PubMed:20561531). Interacts with NOS2
CC (PubMed:21199876). Interacts with EPHB2 (PubMed:28931592).
CC {ECO:0000269|PubMed:15601820, ECO:0000269|PubMed:15713673,
CC ECO:0000269|PubMed:17189197, ECO:0000269|PubMed:20561531,
CC ECO:0000269|PubMed:21199876, ECO:0000269|PubMed:28931592}.
CC -!- INTERACTION:
CC Q96BD6; P54922: ADPRH; NbExp=3; IntAct=EBI-2659201, EBI-6657604;
CC Q96BD6; P55212: CASP6; NbExp=3; IntAct=EBI-2659201, EBI-718729;
CC Q96BD6; P06307: CCK; NbExp=3; IntAct=EBI-2659201, EBI-6624398;
CC Q96BD6; P02489: CRYAA; NbExp=3; IntAct=EBI-2659201, EBI-6875961;
CC Q96BD6; Q6V0L0: CYP26C1; NbExp=2; IntAct=EBI-2659201, EBI-25602589;
CC Q96BD6; O00291: HIP1; NbExp=3; IntAct=EBI-2659201, EBI-473886;
CC Q96BD6; P30519: HMOX2; NbExp=3; IntAct=EBI-2659201, EBI-712096;
CC Q96BD6; O60341: KDM1A; NbExp=2; IntAct=EBI-2659201, EBI-710124;
CC Q96BD6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2659201, EBI-21591415;
CC Q96BD6; Q13153: PAK1; NbExp=3; IntAct=EBI-2659201, EBI-1307;
CC Q96BD6; Q96IZ0: PAWR; NbExp=2; IntAct=EBI-2659201, EBI-595869;
CC Q96BD6; P16284: PECAM1; NbExp=3; IntAct=EBI-2659201, EBI-716404;
CC Q96BD6; O60260-5: PRKN; NbExp=3; IntAct=EBI-2659201, EBI-21251460;
CC Q96BD6; Q99873: PRMT1; NbExp=2; IntAct=EBI-2659201, EBI-78738;
CC Q96BD6; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-2659201, EBI-912440;
CC Q96BD6; P62826: RAN; NbExp=3; IntAct=EBI-2659201, EBI-286642;
CC Q96BD6; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2659201, EBI-396669;
CC Q96BD6; O95863: SNAI1; NbExp=3; IntAct=EBI-2659201, EBI-1045459;
CC Q96BD6; O43463: SUV39H1; NbExp=2; IntAct=EBI-2659201, EBI-349968;
CC Q96BD6; Q13148: TARDBP; NbExp=3; IntAct=EBI-2659201, EBI-372899;
CC Q96BD6; P61086: UBE2K; NbExp=3; IntAct=EBI-2659201, EBI-473850;
CC Q96BD6; P08670: VIM; NbExp=3; IntAct=EBI-2659201, EBI-353844;
CC Q96BD6; O00534: VWA5A; NbExp=3; IntAct=EBI-2659201, EBI-12246480;
CC Q96BD6; P09052: vas; Xeno; NbExp=2; IntAct=EBI-2659201, EBI-134067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21199876}. Note=Exhibits a diffuse cytosolic
CC localization. {ECO:0000269|PubMed:21199876}.
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 (By similarity). Essential for its ability to link NOS2 and
CC the ECS E3 ubiquitin ligase complex components ELOC and CUL5.
CC {ECO:0000250, ECO:0000269|PubMed:21199876}.
CC -!- DOMAIN: The B30.2/SPRY domain is involved in MET and PAWR binding
CC (PubMed:15713673, PubMed:20561531). {ECO:0000269|PubMed:15713673,
CC ECO:0000269|PubMed:20561531}.
CC -!- SIMILARITY: Belongs to the SPSB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF403026; AAL57345.1; -; mRNA.
DR EMBL; AK026046; BAB15335.1; -; mRNA.
DR EMBL; AB209559; BAD92796.1; ALT_INIT; mRNA.
DR EMBL; AL358252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL008734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71617.1; -; Genomic_DNA.
DR EMBL; BC005852; AAH05852.2; -; mRNA.
DR EMBL; BC015711; AAH15711.1; -; mRNA.
DR CCDS; CCDS102.1; -.
DR RefSeq; NP_079382.2; NM_025106.3.
DR PDB; 2JK9; X-ray; 1.79 A; A=30-231.
DR PDB; 3F2O; X-ray; 2.05 A; A/B=31-233.
DR PDBsum; 2JK9; -.
DR PDBsum; 3F2O; -.
DR AlphaFoldDB; Q96BD6; -.
DR SMR; Q96BD6; -.
DR BioGRID; 123158; 36.
DR ELM; Q96BD6; -.
DR IntAct; Q96BD6; 42.
DR MINT; Q96BD6; -.
DR STRING; 9606.ENSP00000330221; -.
DR iPTMnet; Q96BD6; -.
DR PhosphoSitePlus; Q96BD6; -.
DR BioMuta; SPSB1; -.
DR DMDM; 74731225; -.
DR MassIVE; Q96BD6; -.
DR PaxDb; Q96BD6; -.
DR PeptideAtlas; Q96BD6; -.
DR PRIDE; Q96BD6; -.
DR ProteomicsDB; 76068; -.
DR Antibodypedia; 1144; 63 antibodies from 19 providers.
DR DNASU; 80176; -.
DR Ensembl; ENST00000328089.11; ENSP00000330221.6; ENSG00000171621.14.
DR Ensembl; ENST00000357898.3; ENSP00000350573.3; ENSG00000171621.14.
DR Ensembl; ENST00000377399.2; ENSP00000366616.2; ENSG00000171621.14.
DR GeneID; 80176; -.
DR KEGG; hsa:80176; -.
DR MANE-Select; ENST00000328089.11; ENSP00000330221.6; NM_025106.4; NP_079382.2.
DR UCSC; uc001apv.4; human.
DR CTD; 80176; -.
DR DisGeNET; 80176; -.
DR GeneCards; SPSB1; -.
DR HGNC; HGNC:30628; SPSB1.
DR HPA; ENSG00000171621; Low tissue specificity.
DR MIM; 611657; gene.
DR neXtProt; NX_Q96BD6; -.
DR OpenTargets; ENSG00000171621; -.
DR PharmGKB; PA142670871; -.
DR VEuPathDB; HostDB:ENSG00000171621; -.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_046756_0_1_1; -.
DR InParanoid; Q96BD6; -.
DR OMA; SESYGWD; -.
DR OrthoDB; 938259at2759; -.
DR PhylomeDB; Q96BD6; -.
DR TreeFam; TF312822; -.
DR PathwayCommons; Q96BD6; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96BD6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 80176; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; SPSB1; human.
DR EvolutionaryTrace; Q96BD6; -.
DR GeneWiki; SPSB1; -.
DR GenomeRNAi; 80176; -.
DR Pharos; Q96BD6; Tbio.
DR PRO; PR:Q96BD6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96BD6; protein.
DR Bgee; ENSG00000171621; Expressed in decidua and 172 other tissues.
DR ExpressionAtlas; Q96BD6; baseline and differential.
DR Genevisible; Q96BD6; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IPI:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.120.920; -; 1.
DR IDEAL; IID00343; -.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR003877; SPRY_dom.
DR Pfam; PF07525; SOCS_box; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..273
FT /note="SPRY domain-containing SOCS box protein 1"
FT /id="PRO_0000238472"
FT DOMAIN 33..231
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 232..273
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT MOD_RES 31
FT /note="Phosphotyrosine; by MET"
FT /evidence="ECO:0000269|PubMed:15713673"
FT MUTAGEN 31
FT /note="Y->F: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:15713673"
FT MUTAGEN 260..263
FT /note="LPLP->AAAA: Abolishes interaction with RNF7 and
FT CUL5."
FT /evidence="ECO:0000269|PubMed:15601820"
FT CONFLICT 14
FT /note="M -> L (in Ref. 3; BAD92796)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="L -> P (in Ref. 2; BAB15335)"
FT /evidence="ECO:0000305"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2JK9"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:2JK9"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2JK9"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:2JK9"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:2JK9"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:2JK9"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:2JK9"
SQ SEQUENCE 273 AA; 30942 MW; F93D5690A32403DF CRC64;
MGQKVTGGIK TVDMRDPTYR PLKQELQGLD YCKPTRLDLL LDMPPVSYDV QLLHSWNNND
RSLNVFVKED DKLIFHRHPV AQSTDAIRGK VGYTRGLHVW QITWAMRQRG THAVVGVATA
DAPLHSVGYT TLVGNNHESW GWDLGRNRLY HDGKNQPSKT YPAFLEPDET FIVPDSFLVA
LDMDDGTLSF IVDGQYMGVA FRGLKGKKLY PVVSAVWGHC EIRMRYLNGL DPEPLPLMDL
CRRSVRLALG RERLGEIHTL PLPASLKAYL LYQ
