GenomeNet

Database: UniProt
Entry: W5NBH2_LEPOC
LinkDB: W5NBH2_LEPOC
Original site: W5NBH2_LEPOC 
ID   W5NBH2_LEPOC            Unreviewed;       512 AA.
AC   W5NBH2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   28-JAN-2026, entry version 62.
DE   SubName: Full=Suppressor of cytokine signaling 9 {ECO:0000313|Ensembl:ENSLOCP00000017981.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017981.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000017981.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSLOCP00000017981.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AHAT01023721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NBH2; -.
DR   STRING; 7918.ENSLOCP00000017981; -.
DR   Ensembl; ENSLOCT00000018013.1; ENSLOCP00000017981.1; ENSLOCG00000014611.1.
DR   eggNOG; KOG4566; Eukaryota.
DR   GeneTree; ENSGT00940000164285; -.
DR   HOGENOM; CLU_035609_0_0_1; -.
DR   InParanoid; W5NBH2; -.
DR   OMA; SYRIHTQ; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000018468; Linkage group LG2.
DR   Bgee; ENSLOCG00000014611; Expressed in zone of skin and 13 other cell types or tissues.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.30.505.10:FF:000028; Suppressor of cytokine signaling 5; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR022252; SOCS4/SOCS5_dom.
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:SF18; SUPPRESSOR OF CYTOKINE SIGNALING 9 ISOFORM X1; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12610; SOCS; 1.
DR   Pfam; PF07525; SOCS_box; 1.
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.
PE   4: Predicted;
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          360..455
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          450..499
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          1..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..46
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..161
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  57056 MW;  E2578B09B3C8BB41 CRC64;
     MSQSPEAEER GKEKERGARP KVRQSRSEER REGNGRKSGR GKKKGRPPQN PLPERPVSDG
     FEYGELQGGR DPGDTGLPFQ ERCRWQDLTS AGTALQELGV DRPVAGTEEG EGEGGSAKLP
     SSRSLRQKIQ DAVGQCFPIK SSSTPSPSLS PSSSTSSCAS SSSRRKIHLS ELMLDKCPFP
     AGSDLAQKWY LIKQHTVPIS QPALLDTLNG NTLDSPITAV VEDEDDRLRE RRRISIEQGV
     EPPPNAHIHT FEVTAQINPL YKLGPKLAHG MNELAGDDRA THFLLQNCLD TLDDVVASSA
     SSAASSSNLS SSAAAAVRPL SSAVLQSDRL KARESYRVHT QIDYIHCLVP DLLQITNLPC
     YWGVMDRYEA EALLEGKPEG TFLLRDSAQE DYLFSVSFRR YGRSLHARIE QWNHNFSFDV
     HDPSVFYAST VTGLLEHYKD PNSCMFFEPL LSNPIHRVHP FSLQHICRAV IASCTTYDGI
     DVLPIPSALK EHLKEYHYKQ KVRVRRLDTW WE
//
DBGET integrated database retrieval system