ASB16_HUMAN
ID ASB16_HUMAN Reviewed; 453 AA.
AC Q96NS5; B2RBC0; Q8WXK0;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ankyrin repeat and SOCS box protein 16;
DE Short=ASB-16;
GN Name=ASB16;
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 [LARGE SCALE MRNA].
RC TISSUE=Cerebellum, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [MRNA] OF 102-354.
RA Kile B.T., Nicola N.A.;
RT "SOCS box proteins.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP VARIANT PRO-173.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
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 -!- INTERACTION:
CC Q96NS5; P16333: NCK1; NbExp=2; IntAct=EBI-1751918, EBI-389883;
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; AK054727; BAB70800.1; -; mRNA.
DR EMBL; AK314595; BAG37167.1; -; mRNA.
DR EMBL; AC004596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC075088; AAH75088.1; -; mRNA.
DR EMBL; AF403034; AAL57353.1; -; mRNA.
DR CCDS; CCDS11478.1; -.
DR RefSeq; NP_543139.4; NM_080863.4.
DR AlphaFoldDB; Q96NS5; -.
DR SMR; Q96NS5; -.
DR BioGRID; 124958; 35.
DR IntAct; Q96NS5; 7.
DR STRING; 9606.ENSP00000293414; -.
DR iPTMnet; Q96NS5; -.
DR PhosphoSitePlus; Q96NS5; -.
DR BioMuta; ASB16; -.
DR DMDM; 296434399; -.
DR PaxDb; Q96NS5; -.
DR PeptideAtlas; Q96NS5; -.
DR PRIDE; Q96NS5; -.
DR Antibodypedia; 77181; 6 antibodies from 4 providers.
DR DNASU; 92591; -.
DR Ensembl; ENST00000293414.6; ENSP00000293414.1; ENSG00000161664.7.
DR GeneID; 92591; -.
DR KEGG; hsa:92591; -.
DR MANE-Select; ENST00000293414.6; ENSP00000293414.1; NM_080863.5; NP_543139.4.
DR UCSC; uc002ifl.1; human.
DR CTD; 92591; -.
DR DisGeNET; 92591; -.
DR GeneCards; ASB16; -.
DR HGNC; HGNC:19768; ASB16.
DR HPA; ENSG00000161664; Tissue enriched (skeletal).
DR MIM; 615056; gene.
DR neXtProt; NX_Q96NS5; -.
DR OpenTargets; ENSG00000161664; -.
DR PharmGKB; PA134879678; -.
DR VEuPathDB; HostDB:ENSG00000161664; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000160773; -.
DR HOGENOM; CLU_035721_2_0_1; -.
DR InParanoid; Q96NS5; -.
DR OMA; GSCRRHQ; -.
DR OrthoDB; 540084at2759; -.
DR PhylomeDB; Q96NS5; -.
DR TreeFam; TF333494; -.
DR PathwayCommons; Q96NS5; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96NS5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 92591; 23 hits in 1120 CRISPR screens.
DR GenomeRNAi; 92591; -.
DR Pharos; Q96NS5; Tdark.
DR PRO; PR:Q96NS5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96NS5; protein.
DR Bgee; ENSG00000161664; Expressed in hindlimb stylopod muscle and 106 other tissues.
DR ExpressionAtlas; Q96NS5; baseline and differential.
DR Genevisible; Q96NS5; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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 SMART; SM00248; ANK; 7.
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 1: Evidence at protein level;
KW ANK repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..453
FT /note="Ankyrin repeat and SOCS box protein 16"
FT /id="PRO_0000066956"
FT REPEAT 56..85
FT /note="ANK 1"
FT REPEAT 110..139
FT /note="ANK 2"
FT REPEAT 142..171
FT /note="ANK 3"
FT REPEAT 175..204
FT /note="ANK 4"
FT REPEAT 209..238
FT /note="ANK 5"
FT REPEAT 242..279
FT /note="ANK 6"
FT REPEAT 283..312
FT /note="ANK 7"
FT DOMAIN 398..450
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT VARIANT 173
FT /note="T -> P (found in a clear cell renal carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064697"
FT VARIANT 240
FT /note="T -> I (in dbSNP:rs7224330)"
FT /id="VAR_059127"
FT CONFLICT 63
FT /note="Q -> H (in Ref. 1; BAB70800/BAG37167 and 3;
FT AAH75088)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="T -> A (in Ref. 1; BAB70800/BAG37167, 3; AAH75088
FT and 4; AAL57353)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="N -> S (in Ref. 1; BAB70800/BAG37167, 3; AAH75088
FT and 4; AAL57353)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="S -> A (in Ref. 1; BAB70800/BAG37167, 3; AAH75088
FT and 4; AAL57353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 49637 MW; CAF7A454F76F3A32 CRC64;
MARETFPFTS SMLRSLRLQQ EWLEWEDRRR AAAQQCRSRR CPSSPRARLT RPHRSCRDPA
VHQALFSGNL QQVQALFQDE EAANMIVETV SNQLAWSAEQ GFWVLTPKTK QTAPLAIATA
RGYTDCARHL IRQGAELDAR VGGRAALHEA CARAQFDCVR LLLTFGAKAN VLTEEGTTPL
HLCTIPESLQ CAKLLLEAGA TVNLAAGESQ ETPLHVAAAR GLEQHVALYL EHGADVGLRT
SQGETALNTA CAGAEGPGSC RRHQAAARRL LEAGADARAA GRKRHTPLHN ACANGCGGLA
ELLLRYGARA EVPNGAGHTP MDCALQAVQD SPNWEPEVLF AALLDYGAQP VRPEMLKHCA
NFPRALEVLL NAYPCVPSCE TWVEAVLPEL WKEHEAFYSS ALCMVNQPRQ LQHLARLAVR
ARLGSRCRQG ATRLPLPPLL RDYLLLRVEG CIQ
