ID   ASB1_HUMAN              Reviewed;         335 AA.
AC   Q9Y576; A6NL50; Q4ZG29; Q9ULS4;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Ankyrin repeat and SOCS box protein 1;
DE            Short=ASB-1;
GN   Name=ASB1; Synonyms=KIAA1146;
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].
RX   PubMed=11111040; DOI=10.1016/s0378-1119(00)00402-9;
RA   Kile B.T., Viney E.M., Willson T.A., Brodnicki T.C., Cancilla M.R.,
RA   Herlihy A.S., Croker B.A., Baca M., Nicola N.A., Hilton D.J.,
RA   Alexander W.S.;
RT   "Cloning and characterization of the genes encoding the ankyrin repeat and
RT   SOCS box-containing proteins Asb-1, Asb-2, Asb-3 and Asb-4.";
RL   Gene 258:31-41(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-335.
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [5]
RP   FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL5 AND
RP   RNF7.
RX   PubMed=16325183; DOI=10.1016/j.febslet.2005.11.016;
RA   Kohroki J., Nishiyama T., Nakamura T., Masuho Y.;
RT   "ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin ligase
RT   complexes.";
RL   FEBS Lett. 579:6796-6802(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=21119685; DOI=10.1038/cr.2010.165;
RA   Nie L., Zhao Y., Wu W., Yang Y.Z., Wang H.C., Sun X.H.;
RT   "Notch-induced Asb2 expression promotes protein ubiquitination by forming
RT   non-canonical E3 ligase complexes.";
RL   Cell Res. 21:754-769(2011).
CC   -!- FUNCTION: Probable substrate-recognition component of a SCF-like ECS
CC       (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins (PubMed:16325183). Mediates Notch-induced ubiquitination and
CC       degradation of TCF3/E2A and JAK2 (PubMed:21119685). May play a role in
CC       testis development (By similarity). {ECO:0000250|UniProtKB:Q9WV74,
CC       ECO:0000269|PubMed:16325183, ECO:0000269|PubMed:21119685}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with CUL5 and RNF7. {ECO:0000269|PubMed:16325183}.
CC   -!- INTERACTION:
CC       Q9Y576; Q93034: CUL5; NbExp=6; IntAct=EBI-2323092, EBI-1057139;
CC       Q9Y576; Q92993: KAT5; NbExp=3; IntAct=EBI-2323092, EBI-399080;
CC       Q9Y576; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2323092, EBI-11742507;
CC       Q9Y576; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2323092, EBI-9090795;
CC       Q9Y576; P61981: YWHAG; NbExp=3; IntAct=EBI-2323092, EBI-359832;
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}.
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DR   EMBL; AF156777; AAD41894.1; -; mRNA.
DR   EMBL; AC016999; AAX88934.1; -; Genomic_DNA.
DR   EMBL; BC014528; AAH14528.1; -; mRNA.
DR   EMBL; AB032972; BAA86460.1; -; mRNA.
DR   CCDS; CCDS33416.1; -.
DR   RefSeq; NP_001035535.1; NM_001040445.2.
DR   AlphaFoldDB; Q9Y576; -.
DR   SMR; Q9Y576; -.
DR   BioGRID; 119668; 24.
DR   CORUM; Q9Y576; -.
DR   IntAct; Q9Y576; 9.
DR   MINT; Q9Y576; -.
DR   STRING; 9606.ENSP00000264607; -.
DR   iPTMnet; Q9Y576; -.
DR   PhosphoSitePlus; Q9Y576; -.
DR   BioMuta; ASB1; -.
DR   DMDM; 20532005; -.
DR   EPD; Q9Y576; -.
DR   MassIVE; Q9Y576; -.
DR   MaxQB; Q9Y576; -.
DR   PaxDb; Q9Y576; -.
DR   PeptideAtlas; Q9Y576; -.
DR   PRIDE; Q9Y576; -.
DR   ProteomicsDB; 86308; -.
DR   Antibodypedia; 1137; 31 antibodies from 12 providers.
DR   DNASU; 51665; -.
DR   Ensembl; ENST00000264607.9; ENSP00000264607.4; ENSG00000065802.12.
DR   GeneID; 51665; -.
DR   KEGG; hsa:51665; -.
DR   MANE-Select; ENST00000264607.9; ENSP00000264607.4; NM_001040445.3; NP_001035535.1.
DR   UCSC; uc002vyg.4; human.
DR   CTD; 51665; -.
DR   DisGeNET; 51665; -.
DR   GeneCards; ASB1; -.
DR   HGNC; HGNC:16011; ASB1.
DR   HPA; ENSG00000065802; Low tissue specificity.
DR   MIM; 605758; gene.
DR   neXtProt; NX_Q9Y576; -.
DR   OpenTargets; ENSG00000065802; -.
DR   PharmGKB; PA25027; -.
DR   VEuPathDB; HostDB:ENSG00000065802; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000153969; -.
DR   HOGENOM; CLU_053981_0_0_1; -.
DR   InParanoid; Q9Y576; -.
DR   OMA; TGPVCQE; -.
DR   OrthoDB; 1048859at2759; -.
DR   PhylomeDB; Q9Y576; -.
DR   TreeFam; TF331945; -.
DR   PathwayCommons; Q9Y576; -.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q9Y576; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 51665; 14 hits in 1116 CRISPR screens.
DR   ChiTaRS; ASB1; human.
DR   GeneWiki; ASB1; -.
DR   GenomeRNAi; 51665; -.
DR   Pharos; Q9Y576; Tdark.
DR   PRO; PR:Q9Y576; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9Y576; protein.
DR   Bgee; ENSG00000065802; Expressed in apex of heart and 184 other tissues.
DR   ExpressionAtlas; Q9Y576; baseline and differential.
DR   Genevisible; Q9Y576; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
DR   GO; GO:0001818; P:negative regulation of cytokine production; NAS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   CDD; cd03720; SOCS_ASB1; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037331; ASB1_SOCS.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF07525; SOCS_box; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
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; 3.
DR   PROSITE; PS50225; SOCS; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Developmental protein; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..335
FT                   /note="Ankyrin repeat and SOCS box protein 1"
FT                   /id="PRO_0000066923"
FT   REPEAT          36..68
FT                   /note="ANK 1"
FT   REPEAT          77..106
FT                   /note="ANK 2"
FT   REPEAT          110..139
FT                   /note="ANK 3"
FT   REPEAT          143..172
FT                   /note="ANK 4"
FT   REPEAT          191..220
FT                   /note="ANK 5"
FT   REPEAT          235..265
FT                   /note="ANK 6"
FT   DOMAIN          286..335
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
SQ   SEQUENCE   335 AA;  37014 MW;  0843C96AD1AF60D9 CRC64;
     MAEGGSPDGR AGPGSAGRNL KEWLREQFCD HPLEHCEDTR LHDAAYVGDL QTLRSLLQEE
     SYRSRINEKS VWCCGWLPCT PLRIAATAGH GSCVDFLIRK GAEVDLVDVK GQTALYVAVV
     NGHLESTQIL LEAGADPNGS RHHRSTPVYH ASRVGRADIL KALIRYGADV DVNHHLTPDV
     QPRFSRRLTS LVVCPLYISA AYHNLQCFRL LLLAGANPDF NCNGPVNTQG FYRGSPGCVM
     DAVLRHGCEA AFVSLLVEFG ANLNLVKWES LGPESRGRRK VDPEALQVFK EARSVPRTLL
     CLCRVAVRRA LGKHRLHLIP SLPLPDPIKK FLLHE