ASB11_HUMAN
ID ASB11_HUMAN Reviewed; 323 AA.
AC Q8WXH4; E9PEN1; Q3SYC4; Q7Z667;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ankyrin repeat and SOCS box protein 11;
DE Short=ASB-11;
GN Name=ASB11;
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 Kile B.T., Hilton D.J., Nicola N.A.;
RT "SOCS box proteins.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP VARIANT LEU-165.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex
CC which mediates the ubiquitination and subsequent proteasomal
CC degradation of target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WXH4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXH4-2; Sequence=VSP_043087;
CC Name=3;
CC IsoId=Q8WXH4-3; Sequence=VSP_047127;
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin-protein ligase
CC complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC {ECO:0000305}.
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; AF425642; AAL60519.1; -; mRNA.
DR EMBL; BX537857; CAD97864.1; -; mRNA.
DR EMBL; AC095351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069340; AAH69340.1; -; mRNA.
DR EMBL; BC103874; AAI03875.1; -; mRNA.
DR EMBL; BC103875; AAI03876.1; -; mRNA.
DR CCDS; CCDS14164.1; -. [Q8WXH4-1]
DR CCDS; CCDS35209.1; -. [Q8WXH4-3]
DR CCDS; CCDS56596.1; -. [Q8WXH4-2]
DR RefSeq; NP_001012428.1; NM_001012428.2. [Q8WXH4-3]
DR RefSeq; NP_001188512.1; NM_001201583.1. [Q8WXH4-2]
DR RefSeq; NP_543149.1; NM_080873.2. [Q8WXH4-1]
DR PDB; 4UUC; X-ray; 1.80 A; A=64-287.
DR PDBsum; 4UUC; -.
DR AlphaFoldDB; Q8WXH4; -.
DR SMR; Q8WXH4; -.
DR BioGRID; 126610; 20.
DR STRING; 9606.ENSP00000417914; -.
DR iPTMnet; Q8WXH4; -.
DR PhosphoSitePlus; Q8WXH4; -.
DR BioMuta; ASB11; -.
DR DMDM; 20531990; -.
DR MassIVE; Q8WXH4; -.
DR PaxDb; Q8WXH4; -.
DR PeptideAtlas; Q8WXH4; -.
DR PRIDE; Q8WXH4; -.
DR ProteomicsDB; 19927; -.
DR ProteomicsDB; 75055; -. [Q8WXH4-1]
DR ProteomicsDB; 75056; -. [Q8WXH4-2]
DR Antibodypedia; 353; 114 antibodies from 20 providers.
DR DNASU; 140456; -.
DR Ensembl; ENST00000344384.8; ENSP00000343408.4; ENSG00000165192.14. [Q8WXH4-3]
DR Ensembl; ENST00000380470.7; ENSP00000369837.3; ENSG00000165192.14. [Q8WXH4-2]
DR Ensembl; ENST00000480796.6; ENSP00000417914.1; ENSG00000165192.14. [Q8WXH4-1]
DR GeneID; 140456; -.
DR KEGG; hsa:140456; -.
DR MANE-Select; ENST00000480796.6; ENSP00000417914.1; NM_080873.3; NP_543149.1.
DR UCSC; uc004cwo.3; human. [Q8WXH4-1]
DR CTD; 140456; -.
DR DisGeNET; 140456; -.
DR GeneCards; ASB11; -.
DR HGNC; HGNC:17186; ASB11.
DR HPA; ENSG00000165192; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 300626; gene.
DR neXtProt; NX_Q8WXH4; -.
DR OpenTargets; ENSG00000165192; -.
DR PharmGKB; PA25029; -.
DR VEuPathDB; HostDB:ENSG00000165192; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000160592; -.
DR HOGENOM; CLU_000134_4_1_1; -.
DR InParanoid; Q8WXH4; -.
DR OMA; RPGLWKE; -.
DR OrthoDB; 1546307at2759; -.
DR PhylomeDB; Q8WXH4; -.
DR TreeFam; TF331945; -.
DR PathwayCommons; Q8WXH4; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140456; 8 hits in 734 CRISPR screens.
DR GenomeRNAi; 140456; -.
DR Pharos; Q8WXH4; Tdark.
DR PRO; PR:Q8WXH4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8WXH4; protein.
DR Bgee; ENSG00000165192; Expressed in hindlimb stylopod muscle and 43 other tissues.
DR ExpressionAtlas; Q8WXH4; baseline and differential.
DR Genevisible; Q8WXH4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd03728; SOCS_ASB_9_11; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037333; ASB9/11_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..323
FT /note="Ankyrin repeat and SOCS box protein 11"
FT /id="PRO_0000066944"
FT REPEAT 64..93
FT /note="ANK 1"
FT REPEAT 97..126
FT /note="ANK 2"
FT REPEAT 130..159
FT /note="ANK 3"
FT REPEAT 162..191
FT /note="ANK 4"
FT REPEAT 195..224
FT /note="ANK 5"
FT REPEAT 227..256
FT /note="ANK 6"
FT DOMAIN 273..323
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT VAR_SEQ 1..60
FT /note="MEDGPVFYGFKNIFITMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIA
FT EEIYGGIS -> MLQLTGENEKNCEVSERIRRSGPWKEISFGDYICHTFQG (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047127"
FT VAR_SEQ 88..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_043087"
FT VARIANT 165
FT /note="S -> L (in dbSNP:rs144572145)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069428"
FT VARIANT 249
FT /note="D -> N (in dbSNP:rs34025595)"
FT /id="VAR_048286"
FT VARIANT 263
FT /note="S -> G (in dbSNP:rs35859007)"
FT /id="VAR_048287"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:4UUC"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:4UUC"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:4UUC"
SQ SEQUENCE 323 AA; 35367 MW; F95A40184C5BBF4E CRC64;
MEDGPVFYGF KNIFITMFAT FFFFKLLIKV FLALLTHFYI VKGNRKEAAR IAEEIYGGIS
DCWADRSPLH EAAAQGRLLA LKTLIAQGVN VNLVTINRVS SLHEACLGGH VACAKALLEN
GAHVNGVTVH GATPLFNACC SGSAACVNVL LEFGAKAQLE VHLASPIHEA VKRGHRECME
ILLANNVNID HEVPQLGTPL YVACTYQRVD CVKKLLELGA SVDHGQWLDT PLHAAARQSN
VEVIHLLTDY GANLKRRNAQ GKSALDLAAP KSSVEQALLL REGPPALSQL CRLCVRKCLG
RACHQAIHKL HLPEPLERFL LYQ
