ASB5_HUMAN
ID ASB5_HUMAN Reviewed; 329 AA.
AC Q8WWX0; Q8N7B5;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ankyrin repeat and SOCS box protein 5;
DE Short=ASB-5;
GN Name=ASB5;
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.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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).
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. May play a role in the initiation of
CC arteriogenesis (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WWX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WWX0-2; Sequence=VSP_054425;
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; AY057053; AAL18248.1; -; mRNA.
DR EMBL; AK098693; BAC05382.1; -; mRNA.
DR EMBL; AC019163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065710; AAH65710.1; -; mRNA.
DR CCDS; CCDS3827.1; -. [Q8WWX0-1]
DR RefSeq; NP_543150.1; NM_080874.3. [Q8WWX0-1]
DR RefSeq; XP_005262816.1; XM_005262759.1. [Q8WWX0-1]
DR RefSeq; XP_011529919.1; XM_011531617.2. [Q8WWX0-2]
DR AlphaFoldDB; Q8WWX0; -.
DR SMR; Q8WWX0; -.
DR BioGRID; 126611; 23.
DR STRING; 9606.ENSP00000296525; -.
DR BioMuta; ASB5; -.
DR DMDM; 20531989; -.
DR MassIVE; Q8WWX0; -.
DR PaxDb; Q8WWX0; -.
DR PeptideAtlas; Q8WWX0; -.
DR PRIDE; Q8WWX0; -.
DR ProteomicsDB; 72279; -.
DR ProteomicsDB; 74949; -. [Q8WWX0-1]
DR Antibodypedia; 28653; 97 antibodies from 22 providers.
DR DNASU; 140458; -.
DR Ensembl; ENST00000296525.7; ENSP00000296525.3; ENSG00000164122.9. [Q8WWX0-1]
DR Ensembl; ENST00000512254.1; ENSP00000422877.1; ENSG00000164122.9. [Q8WWX0-2]
DR GeneID; 140458; -.
DR KEGG; hsa:140458; -.
DR MANE-Select; ENST00000296525.7; ENSP00000296525.3; NM_080874.4; NP_543150.1.
DR UCSC; uc003iup.3; human. [Q8WWX0-1]
DR CTD; 140458; -.
DR GeneCards; ASB5; -.
DR HGNC; HGNC:17180; ASB5.
DR HPA; ENSG00000164122; Group enriched (skeletal muscle, tongue).
DR MIM; 615050; gene.
DR neXtProt; NX_Q8WWX0; -.
DR OpenTargets; ENSG00000164122; -.
DR PharmGKB; PA25033; -.
DR VEuPathDB; HostDB:ENSG00000164122; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000159851; -.
DR HOGENOM; CLU_000134_4_1_1; -.
DR InParanoid; Q8WWX0; -.
DR OMA; HHECLAI; -.
DR PhylomeDB; Q8WWX0; -.
DR TreeFam; TF331945; -.
DR PathwayCommons; Q8WWX0; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140458; 8 hits in 1106 CRISPR screens.
DR ChiTaRS; ASB5; human.
DR GenomeRNAi; 140458; -.
DR Pharos; Q8WWX0; Tdark.
DR PRO; PR:Q8WWX0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8WWX0; protein.
DR Bgee; ENSG00000164122; Expressed in skeletal muscle tissue of rectus abdominis and 119 other tissues.
DR ExpressionAtlas; Q8WWX0; baseline and differential.
DR Genevisible; Q8WWX0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; cd03724; SOCS_ASB5; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037328; ASB5_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR01415; ANKYRIN.
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; 4.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="Ankyrin repeat and SOCS box protein 5"
FT /id="PRO_0000066930"
FT REPEAT 69..98
FT /note="ANK 1"
FT REPEAT 102..131
FT /note="ANK 2"
FT REPEAT 135..164
FT /note="ANK 3"
FT REPEAT 167..196
FT /note="ANK 4"
FT REPEAT 200..229
FT /note="ANK 5"
FT REPEAT 232..261
FT /note="ANK 6"
FT DOMAIN 278..329
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT VAR_SEQ 1..65
FT /note="MSVLEENRPFAQQLSNVYFTILSLFCFKLFVKISLAILSHFYIVKGNRKEAA
FT RIAAEFYGVTQGQ -> MPLCNGGNLAVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054425"
SQ SEQUENCE 329 AA; 36341 MW; 966B823CED8A8B71 CRC64;
MSVLEENRPF AQQLSNVYFT ILSLFCFKLF VKISLAILSH FYIVKGNRKE AARIAAEFYG
VTQGQGSWAD RSPLHEAASQ GRLLALRTLL SQGYNVNAVT LDHVTPLHEA CLGDHVACAR
TLLEAGANVN AITIDGVTPL FNACSQGSPS CAELLLEYGA KAQLESCLPS PTHEAASKGH
HECLDILISW GIDVDQEIPH LGTPLYVACM SQQFHCIWKL LYAGADVQKG KYWDTPLHAA
AQQSSTEIVN LLLEFGADIN AKNTELLRPI DVATSSSMVE RILLQHEATP SSLYQLCRLC
IRSYIGKPRL HLIPQLQLPT LLKNFLQYR
