ASB3_HUMAN
ID ASB3_HUMAN Reviewed; 518 AA.
AC Q9Y575; B3KPA3; D6W5B4; D6W5B5; G8JLA9; Q2TAI4; Q53TN0; Q53TN8; Q9NVZ2;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Ankyrin repeat and SOCS box protein 3;
DE Short=ASB-3;
GN Name=ASB3;
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).
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Teratocarcinoma;
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=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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Kidney, and Lung;
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 [6]
RP FUNCTION, AND INTERACTION WITH ELOB AND TNFRSF1B.
RX PubMed=15899873; DOI=10.1128/mcb.25.11.4716-4726.2005;
RA Chung A.S., Guan Y.J., Yuan Z.L., Albina J.E., Chin Y.E.;
RT "Ankyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and
RT degradation of tumor necrosis factor receptor II.";
RL Mol. Cell. Biol. 25:4716-4726(2005).
CC -!- FUNCTION: Probable 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. Recognizes TNFRSF1B.
CC {ECO:0000269|PubMed:15899873}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with ELOB and TNFRSF1B.
CC {ECO:0000269|PubMed:15899873}.
CC -!- INTERACTION:
CC Q9Y575; Q9NP31: SH2D2A; NbExp=3; IntAct=EBI-2875625, EBI-490630;
CC Q9Y575-3; P54253: ATXN1; NbExp=6; IntAct=EBI-14199987, EBI-930964;
CC Q9Y575-3; P54252: ATXN3; NbExp=3; IntAct=EBI-14199987, EBI-946046;
CC Q9Y575-3; P46379-2: BAG6; NbExp=3; IntAct=EBI-14199987, EBI-10988864;
CC Q9Y575-3; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-14199987, EBI-739773;
CC Q9Y575-3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-14199987, EBI-10976677;
CC Q9Y575-3; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-14199987, EBI-744099;
CC Q9Y575-3; P14136: GFAP; NbExp=3; IntAct=EBI-14199987, EBI-744302;
CC Q9Y575-3; Q53GS7: GLE1; NbExp=3; IntAct=EBI-14199987, EBI-1955541;
CC Q9Y575-3; P28799: GRN; NbExp=3; IntAct=EBI-14199987, EBI-747754;
CC Q9Y575-3; P07686: HEXB; NbExp=3; IntAct=EBI-14199987, EBI-7133736;
CC Q9Y575-3; P04792: HSPB1; NbExp=3; IntAct=EBI-14199987, EBI-352682;
CC Q9Y575-3; O43464: HTRA2; NbExp=3; IntAct=EBI-14199987, EBI-517086;
CC Q9Y575-3; P42858: HTT; NbExp=6; IntAct=EBI-14199987, EBI-466029;
CC Q9Y575-3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-14199987, EBI-1055254;
CC Q9Y575-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-14199987, EBI-10975473;
CC Q9Y575-3; O14901: KLF11; NbExp=3; IntAct=EBI-14199987, EBI-948266;
CC Q9Y575-3; P51608: MECP2; NbExp=3; IntAct=EBI-14199987, EBI-1189067;
CC Q9Y575-3; P19404: NDUFV2; NbExp=3; IntAct=EBI-14199987, EBI-713665;
CC Q9Y575-3; P07196: NEFL; NbExp=3; IntAct=EBI-14199987, EBI-475646;
CC Q9Y575-3; P29474: NOS3; NbExp=3; IntAct=EBI-14199987, EBI-1391623;
CC Q9Y575-3; P50897: PPT1; NbExp=3; IntAct=EBI-14199987, EBI-1237011;
CC Q9Y575-3; O60260-5: PRKN; NbExp=3; IntAct=EBI-14199987, EBI-21251460;
CC Q9Y575-3; P60891: PRPS1; NbExp=3; IntAct=EBI-14199987, EBI-749195;
CC Q9Y575-3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-14199987, EBI-396669;
CC Q9Y575-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-14199987, EBI-5235340;
CC Q9Y575-3; Q13148: TARDBP; NbExp=3; IntAct=EBI-14199987, EBI-372899;
CC Q9Y575-3; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-14199987, EBI-11139477;
CC Q9Y575-3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-14199987, EBI-11741437;
CC Q9Y575-3; P02766: TTR; NbExp=3; IntAct=EBI-14199987, EBI-711909;
CC Q9Y575-3; P40337-2: VHL; NbExp=3; IntAct=EBI-14199987, EBI-12157263;
CC Q9Y575-3; O76024: WFS1; NbExp=3; IntAct=EBI-14199987, EBI-720609;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y575-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y575-2; Sequence=VSP_036392;
CC Name=3;
CC IsoId=Q9Y575-3; Sequence=VSP_044606;
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 -!- SEQUENCE CAUTION:
CC Sequence=AAI10916.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF156778; AAD41895.1; -; mRNA.
DR EMBL; AK000985; BAA91455.1; -; mRNA.
DR EMBL; AK001283; BAA91599.1; -; mRNA.
DR EMBL; AK056069; BAG51615.1; -; mRNA.
DR EMBL; AC007883; AAY24350.1; -; Genomic_DNA.
DR EMBL; AC008064; AAX93180.1; -; Genomic_DNA.
DR EMBL; AC008068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00167.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00168.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00169.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00170.1; -; Genomic_DNA.
DR EMBL; BC006488; AAH06488.1; -; mRNA.
DR EMBL; BC009569; AAH09569.1; -; mRNA.
DR EMBL; BC110915; AAI10916.1; ALT_INIT; mRNA.
DR CCDS; CCDS1846.1; -. [Q9Y575-1]
DR CCDS; CCDS1847.1; -. [Q9Y575-2]
DR RefSeq; NP_001157637.1; NM_001164165.1. [Q9Y575-3]
DR RefSeq; NP_001188894.1; NM_001201965.1. [Q9Y575-2]
DR RefSeq; NP_057199.1; NM_016115.4. [Q9Y575-1]
DR RefSeq; NP_665862.1; NM_145863.2. [Q9Y575-2]
DR AlphaFoldDB; Q9Y575; -.
DR SMR; Q9Y575; -.
DR BioGRID; 119317; 80.
DR BioGRID; 950460; 1.
DR IntAct; Q9Y575; 69.
DR MINT; Q9Y575; -.
DR STRING; 9606.ENSP00000263634; -.
DR iPTMnet; Q9Y575; -.
DR PhosphoSitePlus; Q9Y575; -.
DR SwissPalm; Q9Y575; -.
DR BioMuta; ASB3; -.
DR DMDM; 20532004; -.
DR EPD; Q9Y575; -.
DR jPOST; Q9Y575; -.
DR MassIVE; Q9Y575; -.
DR MaxQB; Q9Y575; -.
DR PaxDb; Q9Y575; -.
DR PeptideAtlas; Q9Y575; -.
DR PRIDE; Q9Y575; -.
DR ProteomicsDB; 34171; -.
DR ProteomicsDB; 86306; -. [Q9Y575-1]
DR ProteomicsDB; 86307; -. [Q9Y575-2]
DR Antibodypedia; 1141; 163 antibodies from 22 providers.
DR DNASU; 51130; -.
DR Ensembl; ENST00000263634.8; ENSP00000263634.2; ENSG00000115239.24. [Q9Y575-1]
DR Ensembl; ENST00000394717.3; ENSP00000378206.2; ENSG00000115239.24. [Q9Y575-2]
DR Ensembl; ENST00000406625.6; ENSP00000385085.4; ENSG00000115239.24. [Q9Y575-1]
DR Ensembl; ENST00000406687.5; ENSP00000384728.1; ENSG00000115239.24. [Q9Y575-2]
DR GeneID; 100302652; -.
DR GeneID; 51130; -.
DR KEGG; hsa:100302652; -.
DR KEGG; hsa:51130; -.
DR MANE-Select; ENST00000263634.8; ENSP00000263634.2; NM_016115.5; NP_057199.1.
DR UCSC; uc002rxg.3; human. [Q9Y575-1]
DR CTD; 100302652; -.
DR CTD; 51130; -.
DR DisGeNET; 100302652; -.
DR DisGeNET; 51130; -.
DR GeneCards; ASB3; -.
DR HGNC; HGNC:16013; ASB3.
DR HPA; ENSG00000115239; Low tissue specificity.
DR MIM; 605760; gene.
DR neXtProt; NX_Q9Y575; -.
DR OpenTargets; ENSG00000115239; -.
DR PharmGKB; PA25031; -.
DR VEuPathDB; HostDB:ENSG00000115239; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000159080; -.
DR HOGENOM; CLU_000134_3_0_1; -.
DR InParanoid; Q9Y575; -.
DR OMA; MCMVFQK; -.
DR PhylomeDB; Q9Y575; -.
DR TreeFam; TF315127; -.
DR PathwayCommons; Q9Y575; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9Y575; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 100302652; 8 hits in 965 CRISPR screens.
DR BioGRID-ORCS; 51130; 30 hits in 1043 CRISPR screens.
DR ChiTaRS; ASB3; human.
DR GeneWiki; ASB3; -.
DR Pharos; Q9Y575; Tbio.
DR PRO; PR:Q9Y575; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y575; protein.
DR Bgee; ENSG00000115239; Expressed in secondary oocyte and 182 other tissues.
DR ExpressionAtlas; Q9Y575; baseline and differential.
DR Genevisible; Q9Y575; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030315; C:T-tubule; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0036371; P:protein localization to T-tubule; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IBA:GO_Central.
DR CDD; cd03722; SOCS_ASB3; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037329; ASB3_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF48403; SSF48403; 2.
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 Alternative splicing; ANK repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..518
FT /note="Ankyrin repeat and SOCS box protein 3"
FT /id="PRO_0000066926"
FT REPEAT 9..38
FT /note="ANK 1"
FT REPEAT 42..71
FT /note="ANK 2"
FT REPEAT 78..107
FT /note="ANK 3"
FT REPEAT 111..140
FT /note="ANK 4"
FT REPEAT 145..174
FT /note="ANK 5"
FT REPEAT 178..207
FT /note="ANK 6"
FT REPEAT 211..240
FT /note="ANK 7"
FT REPEAT 246..275
FT /note="ANK 8"
FT REPEAT 279..308
FT /note="ANK 9"
FT REPEAT 315..346
FT /note="ANK 10"
FT REPEAT 348..373
FT /note="ANK 11"
FT DOMAIN 441..504
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036392"
FT VAR_SEQ 1
FT /note="M -> MAMMPLVLHHPERQAELGSGLRDGGGAALRPPGRLVKQM (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044606"
FT CONFLICT 118
FT /note="L -> S (in Ref. 2; BAA91599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57745 MW; E6FC2EF76DD814DF CRC64;
MDFTEAYADT CSTVGLAARE GNVKVLRKLL KKGRSVDVAD NRGWMPIHEA AYHNSVECLQ
MLINADSSEN YIKMKTFEGF CALHLAASQG HWKIVQILLE AGADPNATTL EETTPLFLAV
ENGQIDVLRL LLQHGANVNG SHSMCGWNSL HQASFQENAE IIKLLLRKGA NKECQDDFGI
TPLFVAAQYG KLESLSILIS SGANVNCQAL DKATPLFIAA QEGHTKCVEL LLSSGADPDL
YCNEDSWQLP IHAAAQMGHT KILDLLIPLT NRACDTGLNK VSPVYSAVFG GHEDCLEILL
RNGYSPDAQA CLVFGFSSPV CMAFQKDCEF FGIVNILLKY GAQINELHLA YCLKYEKFSI
FRYFLRKGCS LGPWNHIYEF VNHAIKAQAK YKEWLPHLLV AGFDPLILLC NSWIDSVSID
TLIFTLEFTN WKTLAPAVER MLSARASNAW ILQQHIATVP SLTHLCRLEI RSSLKSERLR
SDSYISQLPL PRSLHNYLLY EDVLRMYEVP ELAAIQDG
