SPSB2_HUMAN
ID SPSB2_HUMAN Reviewed; 263 AA.
AC Q99619; B7Z4W1; D3DUT0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=SPRY domain-containing SOCS box protein 2;
DE Short=SSB-2;
DE AltName: Full=Gene-rich cluster protein C9;
GN Name=SPSB2; Synonyms=GRCC9, SSB2;
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] (ISOFORM 1).
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] (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=9074930; DOI=10.1101/gr.7.3.268;
RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT "Large-scale sequencing in human chromosome 12p13: experimental and
RT computational gene structure determination.";
RL Genome Res. 7:268-280(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Spleen;
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, AND INTERACTION WITH CUL5; RNF7; ELOB AND ELOC.
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.
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 PAWR, AND MUTAGENESIS OF 116-GLN--GLY-119.
RX PubMed=16498413; DOI=10.1038/sj.emboj.7600994;
RA Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.;
RT "Structural and functional insights into the B30.2/SPRY domain.";
RL EMBO J. 25:1353-1363(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 HCV ENVELOPE GLYCOPROTEIN E1 (MICROBIAL INFECTION), AND
RP INTERACTION WITH HCV NON-STRUCTURAL PROTEIN 5A (MICROBIAL INFECTION).
RX PubMed=31344133; DOI=10.1371/journal.pone.0219989;
RA Wang M., Wang Y., Liu Y., Wang H., Xin X., Li J., Hao Y., Han L., Yu F.,
RA Zheng C., Shen C.;
RT "SPSB2 inhibits hepatitis C virus replication by targeting NS5A for
RT ubiquitination and degradation.";
RL PLoS ONE 14:e0219989-e0219989(2019).
RN [12] {ECO:0007744|PDB:3EMW}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-219 IN COMPLEX WITH DROSOPHILA
RP VAS, AND INTERACTION WITH PAWR.
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(SPSB2) E3 ubiquitin-protein
CC ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and
CC SPSB2 (PubMed:15601820). Interacts with CUL5, RNF7, ELOB and ELOC
CC (PubMed:15601820). Interacts with MET (PubMed:15713673). Interacts (via
CC B30.2/SPRY domain) with PAWR; this interaction occurs in association
CC with the Elongin BC complex (PubMed:16498413, PubMed:20561531).
CC Interacts with NOS2 (PubMed:21199876). {ECO:0000269|PubMed:15601820,
CC ECO:0000269|PubMed:15713673, ECO:0000269|PubMed:16498413,
CC ECO:0000269|PubMed:20561531, ECO:0000269|PubMed:21199876}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with HCV
CC envelope glycoprotein E1. Interacts (via C-terminus) with HCV non-
CC structural protein 5A; this interaction targets NS5A for ubiquitination
CC and degradation. {ECO:0000269|PubMed:31344133}.
CC -!- INTERACTION:
CC Q99619; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2323209, EBI-10976677;
CC Q99619; Q15369: ELOC; NbExp=3; IntAct=EBI-2323209, EBI-301231;
CC Q99619; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-2323209, EBI-10242151;
CC Q99619; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2323209, EBI-10975473;
CC Q99619; Q16656-4: NRF1; NbExp=3; IntAct=EBI-2323209, EBI-11742836;
CC Q99619; P16284: PECAM1; NbExp=3; IntAct=EBI-2323209, EBI-716404;
CC Q99619; Q92569: PIK3R3; NbExp=3; IntAct=EBI-2323209, EBI-79893;
CC Q99619; O60260-5: PRKN; NbExp=3; IntAct=EBI-2323209, EBI-21251460;
CC Q99619; Q99873: PRMT1; NbExp=2; IntAct=EBI-2323209, EBI-78738;
CC Q99619; Q6P9E2: RECK; NbExp=3; IntAct=EBI-2323209, EBI-10253121;
CC Q99619; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2323209, EBI-396669;
CC Q99619; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2323209, EBI-358489;
CC Q99619; P61086: UBE2K; NbExp=3; IntAct=EBI-2323209, EBI-473850;
CC Q99619; P08670: VIM; NbExp=3; IntAct=EBI-2323209, EBI-353844;
CC Q99619; P09052: vas; Xeno; NbExp=2; IntAct=EBI-2323209, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99619-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99619-2; Sequence=VSP_057167;
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 -!- SIMILARITY: Belongs to the SPSB family. {ECO:0000305}.
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DR EMBL; AF403027; AAL57346.1; -; mRNA.
DR EMBL; AK297963; BAH12697.1; -; mRNA.
DR EMBL; U47924; AAB51328.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88719.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88720.1; -; Genomic_DNA.
DR EMBL; BC002983; AAH02983.1; -; mRNA.
DR EMBL; BC071933; AAH71933.1; -; mRNA.
DR CCDS; CCDS8567.1; -. [Q99619-1]
DR RefSeq; NP_001139788.1; NM_001146316.1. [Q99619-1]
DR RefSeq; NP_001306599.1; NM_001319670.1. [Q99619-1]
DR RefSeq; NP_116030.1; NM_032641.3. [Q99619-1]
DR PDB; 3EMW; X-ray; 1.80 A; A=26-219.
DR PDB; 5XN3; X-ray; 1.34 A; A=22-220.
DR PDB; 6DN5; X-ray; 2.40 A; A=26-219.
DR PDB; 6DN6; X-ray; 1.59 A; A=26-219.
DR PDB; 6JKJ; X-ray; 1.90 A; A/B=22-220.
DR PDB; 6JWM; X-ray; 1.23 A; A=22-220.
DR PDB; 6JWN; X-ray; 1.61 A; A/C=22-220.
DR PDB; 6KEY; X-ray; 1.24 A; A=22-220.
DR PDBsum; 3EMW; -.
DR PDBsum; 5XN3; -.
DR PDBsum; 6DN5; -.
DR PDBsum; 6DN6; -.
DR PDBsum; 6JKJ; -.
DR PDBsum; 6JWM; -.
DR PDBsum; 6JWN; -.
DR PDBsum; 6KEY; -.
DR AlphaFoldDB; Q99619; -.
DR SMR; Q99619; -.
DR BioGRID; 124227; 58.
DR ELM; Q99619; -.
DR IntAct; Q99619; 25.
DR MINT; Q99619; -.
DR STRING; 9606.ENSP00000428338; -.
DR BindingDB; Q99619; -.
DR ChEMBL; CHEMBL3325308; -.
DR iPTMnet; Q99619; -.
DR PhosphoSitePlus; Q99619; -.
DR BioMuta; SPSB2; -.
DR DMDM; 74732788; -.
DR MassIVE; Q99619; -.
DR PaxDb; Q99619; -.
DR PeptideAtlas; Q99619; -.
DR PRIDE; Q99619; -.
DR ProteomicsDB; 6639; -.
DR ProteomicsDB; 78362; -. [Q99619-1]
DR Antibodypedia; 11257; 92 antibodies from 21 providers.
DR DNASU; 84727; -.
DR Ensembl; ENST00000519357.1; ENSP00000431037.1; ENSG00000111671.10. [Q99619-2]
DR Ensembl; ENST00000523102.5; ENSP00000430872.1; ENSG00000111671.10. [Q99619-1]
DR Ensembl; ENST00000524270.6; ENSP00000428338.1; ENSG00000111671.10. [Q99619-1]
DR GeneID; 84727; -.
DR KEGG; hsa:84727; -.
DR MANE-Select; ENST00000524270.6; ENSP00000428338.1; NM_032641.4; NP_116030.1.
DR UCSC; uc001qrl.4; human. [Q99619-1]
DR CTD; 84727; -.
DR DisGeNET; 84727; -.
DR GeneCards; SPSB2; -.
DR HGNC; HGNC:29522; SPSB2.
DR HPA; ENSG00000111671; Low tissue specificity.
DR MIM; 611658; gene.
DR neXtProt; NX_Q99619; -.
DR OpenTargets; ENSG00000111671; -.
DR PharmGKB; PA142670872; -.
DR VEuPathDB; HostDB:ENSG00000111671; -.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_046756_0_0_1; -.
DR InParanoid; Q99619; -.
DR OMA; HAWEIGW; -.
DR OrthoDB; 938259at2759; -.
DR PhylomeDB; Q99619; -.
DR TreeFam; TF312822; -.
DR PathwayCommons; Q99619; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q99619; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 84727; 13 hits in 1074 CRISPR screens.
DR ChiTaRS; SPSB2; human.
DR EvolutionaryTrace; Q99619; -.
DR GenomeRNAi; 84727; -.
DR Pharos; Q99619; Tbio.
DR PRO; PR:Q99619; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q99619; protein.
DR Bgee; ENSG00000111671; Expressed in right uterine tube and 129 other tissues.
DR ExpressionAtlas; Q99619; baseline and differential.
DR Genevisible; Q99619; 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:0035556; P:intracellular signal transduction; IEA:InterPro.
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 CDD; cd03719; SOCS_SSB2; 1.
DR Gene3D; 2.60.120.920; -; 1.
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; IPR036036; SOCS_box-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR037340; SSB2_SOCS.
DR Pfam; PF07525; SOCS_box; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF158235; SSF158235; 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; Alternative splicing; Cytoplasm; Host-virus interaction;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..263
FT /note="SPRY domain-containing SOCS box protein 2"
FT /id="PRO_0000238474"
FT DOMAIN 26..221
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 222..263
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 222..263
FT /note="AEPHSLLHLSRLCVRHNLGDTRLGQVSALPLPPAMKRYLLYQ -> GEAWGR
FT RGENFLSLVAVVWDGNSSDKSRGDGPSSSLPQPLFSAGKG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057167"
FT MUTAGEN 116..119
FT /note="QTDH->HSVG: Enhances interaction with PAWR."
FT /evidence="ECO:0000269|PubMed:16498413"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6KEY"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:6JWM"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6JWM"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6KEY"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6JWM"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6JWM"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6JWM"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:6JWM"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6JWM"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:6JWM"
SQ SEQUENCE 263 AA; 28630 MW; 0729EDDD0B598665 CRC64;
MGQTALAGGS SSTPTPQALY PDLSCPEGLE ELLSAPPPDL GAQRRHGWNP KDCSENIEVK
EGGLYFERRP VAQSTDGARG KRGYSRGLHA WEISWPLEQR GTHAVVGVAT ALAPLQTDHY
AALLGSNSES WGWDIGRGKL YHQSKGPGAP QYPAGTQGEQ LEVPERLLVV LDMEEGTLGY
AIGGTYLGPA FRGLKGRTLY PAVSAVWGQC QVRIRYLGER RAEPHSLLHL SRLCVRHNLG
DTRLGQVSAL PLPPAMKRYL LYQ
