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   24-JAN-2024, entry version 168.
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; 9606-ENSP00000296525; -.
DR   PeptideAtlas; Q8WWX0; -.
DR   ProteomicsDB; 72279; -.
DR   ProteomicsDB; 74949; -. [Q8WWX0-1]
DR   Antibodypedia; 28653; 113 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   AGR; HGNC:17180; -.
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; LASREEC; -.
DR   OrthoDB; 50291at2759; -.
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 1184 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 121 other cell types or tissues.
DR   ExpressionAtlas; Q8WWX0; baseline and differential.
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; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.750.20; SOCS box; 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   PANTHER; PTHR24136:SF18; ANKYRIN REPEAT AND SOCS BOX PROTEIN 5; 1.
DR   PANTHER; PTHR24136; SOWAH (DROSOPHILA) HOMOLOG; 1.
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; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF158235; SOCS box-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50225; SOCS; 1.
DR   Genevisible; Q8WWX0; HS.
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
//