ASB6_HUMAN
ID ASB6_HUMAN Reviewed; 421 AA.
AC Q9NWX5; Q5SZB7; Q9BV15;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ankyrin repeat and SOCS box protein 6;
DE Short=ASB-6;
GN Name=ASB6;
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] (ISOFORM 1).
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, and 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 [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).
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. {ECO:0000269|PubMed:16325183}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Binds APS. Identified in a complex with ELOB and ELOC (By
CC similarity). Interacts with CUL5 and RNF7. {ECO:0000250,
CC ECO:0000269|PubMed:16325183}.
CC -!- INTERACTION:
CC Q9NWX5; P11230: CHRNB1; NbExp=3; IntAct=EBI-6425205, EBI-724218;
CC Q9NWX5; Q93034: CUL5; NbExp=9; IntAct=EBI-6425205, EBI-1057139;
CC Q9NWX5; Q9BVJ7: DUSP23; NbExp=3; IntAct=EBI-6425205, EBI-724940;
CC Q9NWX5; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-6425205, EBI-10175124;
CC Q9NWX5; P09067: HOXB5; NbExp=3; IntAct=EBI-6425205, EBI-3893317;
CC Q9NWX5; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-6425205, EBI-2686809;
CC Q9NWX5; P00540: MOS; NbExp=3; IntAct=EBI-6425205, EBI-1757866;
CC Q9NWX5; P24928: POLR2A; NbExp=4; IntAct=EBI-6425205, EBI-295301;
CC Q9NWX5; Q9H4P4: RNF41; NbExp=7; IntAct=EBI-6425205, EBI-2130266;
CC Q9NWX5; O14492-2: SH2B2; NbExp=6; IntAct=EBI-6425205, EBI-19952306;
CC Q9NWX5; Q9BW92: TARS2; NbExp=3; IntAct=EBI-6425205, EBI-1045099;
CC Q9NWX5; O15273: TCAP; NbExp=3; IntAct=EBI-6425205, EBI-954089;
CC Q9NWX5; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-6425205, EBI-12287587;
CC Q9NWX5; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-6425205, EBI-6427977;
CC Q9NWX5; Q8N720: ZNF655; NbExp=3; IntAct=EBI-6425205, EBI-625509;
CC Q9NWX5-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-25838672, EBI-10968534;
CC Q9NWX5-2; O14773: TPP1; NbExp=3; IntAct=EBI-25838672, EBI-2800203;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NWX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWX5-2; Sequence=VSP_042006;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK000555; BAA91250.1; -; mRNA.
DR EMBL; AK023004; BAB14355.1; -; mRNA.
DR EMBL; AL590369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87899.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87900.1; -; Genomic_DNA.
DR EMBL; BC001719; AAH01719.1; -; mRNA.
DR EMBL; BC065913; AAH65913.1; -; mRNA.
DR CCDS; CCDS6924.1; -. [Q9NWX5-1]
DR CCDS; CCDS6925.1; -. [Q9NWX5-2]
DR RefSeq; NP_001189332.1; NM_001202403.1.
DR RefSeq; NP_060343.1; NM_017873.3. [Q9NWX5-1]
DR RefSeq; NP_821066.1; NM_177999.2. [Q9NWX5-2]
DR AlphaFoldDB; Q9NWX5; -.
DR SMR; Q9NWX5; -.
DR BioGRID; 126612; 106.
DR CORUM; Q9NWX5; -.
DR IntAct; Q9NWX5; 46.
DR MINT; Q9NWX5; -.
DR STRING; 9606.ENSP00000277458; -.
DR iPTMnet; Q9NWX5; -.
DR PhosphoSitePlus; Q9NWX5; -.
DR BioMuta; ASB6; -.
DR DMDM; 41688801; -.
DR EPD; Q9NWX5; -.
DR jPOST; Q9NWX5; -.
DR MassIVE; Q9NWX5; -.
DR MaxQB; Q9NWX5; -.
DR PaxDb; Q9NWX5; -.
DR PeptideAtlas; Q9NWX5; -.
DR PRIDE; Q9NWX5; -.
DR ProteomicsDB; 82996; -. [Q9NWX5-1]
DR ProteomicsDB; 82997; -. [Q9NWX5-2]
DR Antibodypedia; 1154; 81 antibodies from 21 providers.
DR DNASU; 140459; -.
DR Ensembl; ENST00000277458.5; ENSP00000277458.4; ENSG00000148331.12. [Q9NWX5-1]
DR Ensembl; ENST00000277459.8; ENSP00000277459.4; ENSG00000148331.12. [Q9NWX5-2]
DR GeneID; 140459; -.
DR KEGG; hsa:140459; -.
DR MANE-Select; ENST00000277458.5; ENSP00000277458.4; NM_017873.4; NP_060343.1.
DR UCSC; uc004byf.3; human. [Q9NWX5-1]
DR CTD; 140459; -.
DR DisGeNET; 140459; -.
DR GeneCards; ASB6; -.
DR HGNC; HGNC:17181; ASB6.
DR HPA; ENSG00000148331; Low tissue specificity.
DR MIM; 615051; gene.
DR neXtProt; NX_Q9NWX5; -.
DR OpenTargets; ENSG00000148331; -.
DR PharmGKB; PA25034; -.
DR VEuPathDB; HostDB:ENSG00000148331; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00390000006784; -.
DR HOGENOM; CLU_1383762_0_0_1; -.
DR InParanoid; Q9NWX5; -.
DR OMA; HLQPWPV; -.
DR OrthoDB; 668449at2759; -.
DR PhylomeDB; Q9NWX5; -.
DR TreeFam; TF330837; -.
DR PathwayCommons; Q9NWX5; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9NWX5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140459; 40 hits in 1115 CRISPR screens.
DR ChiTaRS; ASB6; human.
DR GeneWiki; ASB6; -.
DR GenomeRNAi; 140459; -.
DR Pharos; Q9NWX5; Tdark.
DR PRO; PR:Q9NWX5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NWX5; protein.
DR Bgee; ENSG00000148331; Expressed in granulocyte and 165 other tissues.
DR ExpressionAtlas; Q9NWX5; baseline and differential.
DR Genevisible; Q9NWX5; HS.
DR GO; GO:0031436; C:BRCA1-BARD1 complex; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd03725; SOCS_ASB6; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037327; ASB6_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00253; SOCS; 1.
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; 2.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..421
FT /note="Ankyrin repeat and SOCS box protein 6"
FT /id="PRO_0000066933"
FT REPEAT 67..97
FT /note="ANK 1"
FT REPEAT 102..131
FT /note="ANK 2"
FT REPEAT 136..166
FT /note="ANK 3"
FT REPEAT 170..205
FT /note="ANK 4"
FT REPEAT 226..255
FT /note="ANK 5"
FT REPEAT 260..289
FT /note="ANK 6"
FT DOMAIN 360..415
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT VAR_SEQ 135..421
FT /note="IHESSPLDLASEEPERLPCLQRLLDLGADVNAADKHGKTALLHALASSDGVQ
FT IHNTENIRLLLEGGADVKATTKDGDTVFTCIIFLLGETVGGDKEEAQMINRFCFQVTRL
FT LLAHGADPSECPAHESLTHICLKSFKLHFPLLRFLLESGAAYNCSLHGASCWSGFHIIF
FT ERLCSHPGCTEDESHADLLRKAETVLDLMVTNSQKLQLPENFDIHPVGSLAEKIQALHF
FT SLRQLESYPPPLKHLCRVAIRLYLQPWPVDVKVKALPLPDRLKWYLLSEHSGSVEDDI
FT -> EKLLCSMLWPAATGCRSTILRTFVSYWKEGQTSRPPPKMGTQCSPASSSCLVRPWE
FT GTKRRPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042006"
SQ SEQUENCE 421 AA; 47136 MW; 2DBAF086B54FF1CB CRC64;
MPFLHGFRRI IFEYQPLVDA ILGSLGIQDP ERQESLDRPS YVASEESRIL VLTELLERKA
HSPFYQEGVS NALLKMAELG LTRAADVLLR HGANLNFEDP VTYYTALHIA VLRNQPDMVE
LLVHHGADVN RRDRIHESSP LDLASEEPER LPCLQRLLDL GADVNAADKH GKTALLHALA
SSDGVQIHNT ENIRLLLEGG ADVKATTKDG DTVFTCIIFL LGETVGGDKE EAQMINRFCF
QVTRLLLAHG ADPSECPAHE SLTHICLKSF KLHFPLLRFL LESGAAYNCS LHGASCWSGF
HIIFERLCSH PGCTEDESHA DLLRKAETVL DLMVTNSQKL QLPENFDIHP VGSLAEKIQA
LHFSLRQLES YPPPLKHLCR VAIRLYLQPW PVDVKVKALP LPDRLKWYLL SEHSGSVEDD
I
