ID ASB7_HUMAN Reviewed; 318 AA.
AC Q9H672; A8K1E5; Q6GSJ6; Q7Z4S3;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=Ankyrin repeat and SOCS box protein 7;
DE Short=ASB-7;
GN Name=ASB7;
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).
RC TISSUE=Testis;
RA Guo J.H., Zan Q., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Small intestine;
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].
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] (ISOFORM 2).
RC TISSUE=Bone;
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:0000250,
CC ECO:0000269|PubMed:16325183}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CUL5 and RNF7. {ECO:0000269|PubMed:16325183}.
CC -!- INTERACTION:
CC Q9H672; Q96JN2-2: CCDC136; NbExp=4; IntAct=EBI-3916346, EBI-10171416;
CC Q9H672; Q93034: CUL5; NbExp=3; IntAct=EBI-3916346, EBI-1057139;
CC Q9H672; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-3916346, EBI-2549423;
CC Q9H672-2; Q9NWT6: HIF1AN; NbExp=3; IntAct=EBI-12104328, EBI-745632;
CC Q9H672-2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-12104328, EBI-2549423;
CC Q9H672-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-12104328, EBI-21251460;
CC Q9H672-2; Q8WV99: ZFAND2B; NbExp=3; IntAct=EBI-12104328, EBI-747823;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H672-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H672-2; Sequence=VSP_008919, VSP_008920;
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; AF451994; AAP97683.1; -; mRNA.
DR EMBL; AK026204; BAB15392.1; -; mRNA.
DR EMBL; AK289860; BAF82549.1; -; mRNA.
DR EMBL; CH471101; EAX02274.1; -; Genomic_DNA.
DR EMBL; CH471101; EAX02276.1; -; Genomic_DNA.
DR EMBL; BC063581; AAH63581.1; -; mRNA.
DR CCDS; CCDS10387.1; -. [Q9H672-1]
DR CCDS; CCDS10388.1; -. [Q9H672-2]
DR RefSeq; NP_078984.2; NM_024708.3. [Q9H672-2]
DR RefSeq; NP_937886.1; NM_198243.2. [Q9H672-1]
DR AlphaFoldDB; Q9H672; -.
DR SMR; Q9H672; -.
DR BioGRID; 126613; 55.
DR CORUM; Q9H672; -.
DR DIP; DIP-43701N; -.
DR IntAct; Q9H672; 36.
DR MINT; Q9H672; -.
DR STRING; 9606.ENSP00000328327; -.
DR iPTMnet; Q9H672; -.
DR PhosphoSitePlus; Q9H672; -.
DR BioMuta; ASB7; -.
DR DMDM; 38372887; -.
DR EPD; Q9H672; -.
DR MassIVE; Q9H672; -.
DR MaxQB; Q9H672; -.
DR PaxDb; 9606-ENSP00000328327; -.
DR PeptideAtlas; Q9H672; -.
DR ProteomicsDB; 80962; -. [Q9H672-1]
DR ProteomicsDB; 80963; -. [Q9H672-2]
DR Pumba; Q9H672; -.
DR Antibodypedia; 1147; 164 antibodies from 20 providers.
DR DNASU; 140460; -.
DR Ensembl; ENST00000332783.12; ENSP00000328327.8; ENSG00000183475.13. [Q9H672-1]
DR Ensembl; ENST00000343276.4; ENSP00000339819.4; ENSG00000183475.13. [Q9H672-2]
DR GeneID; 140460; -.
DR KEGG; hsa:140460; -.
DR MANE-Select; ENST00000332783.12; ENSP00000328327.8; NM_198243.3; NP_937886.1.
DR UCSC; uc002bwj.4; human. [Q9H672-1]
DR AGR; HGNC:17182; -.
DR CTD; 140460; -.
DR GeneCards; ASB7; -.
DR HGNC; HGNC:17182; ASB7.
DR HPA; ENSG00000183475; Low tissue specificity.
DR MIM; 615052; gene.
DR neXtProt; NX_Q9H672; -.
DR OpenTargets; ENSG00000183475; -.
DR PharmGKB; PA25035; -.
DR VEuPathDB; HostDB:ENSG00000183475; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000158068; -.
DR HOGENOM; CLU_084795_0_0_1; -.
DR InParanoid; Q9H672; -.
DR OMA; CNGWTLL; -.
DR OrthoDB; 5387069at2759; -.
DR PhylomeDB; Q9H672; -.
DR TreeFam; TF331695; -.
DR PathwayCommons; Q9H672; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9H672; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140460; 14 hits in 1204 CRISPR screens.
DR ChiTaRS; ASB7; human.
DR GenomeRNAi; 140460; -.
DR Pharos; Q9H672; Tbio.
DR PRO; PR:Q9H672; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H672; Protein.
DR Bgee; ENSG00000183475; Expressed in buccal mucosa cell and 159 other cell types or tissues.
DR ExpressionAtlas; Q9H672; baseline and differential.
DR Genevisible; Q9H672; 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 CDD; cd03726; SOCS_ASB7; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.750.20; SOCS box; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037326; ASB7_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR24193:SF121; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00253; SOCS; 1.
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; 5.
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..318
FT /note="Ankyrin repeat and SOCS box protein 7"
FT /id="PRO_0000066935"
FT REPEAT 13..42
FT /note="ANK 1"
FT REPEAT 46..75
FT /note="ANK 2"
FT REPEAT 80..109
FT /note="ANK 3"
FT REPEAT 116..145
FT /note="ANK 4"
FT REPEAT 149..178
FT /note="ANK 5"
FT REPEAT 180..208
FT /note="ANK 6"
FT REPEAT 213..242
FT /note="ANK 7"
FT DOMAIN 265..318
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT VAR_SEQ 273..274
FT /note="RQ -> SM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008919"
FT VAR_SEQ 275..318
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008920"
FT CONFLICT 162
FT /note="R -> K (in Ref. 2; BAB15392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36011 MW; F6FE48D0970DF83E CRC64;
MLHHHCRRNP ELQEELQIQA AVAAGDVHTV RKMLEQGYSP NGRDANGWTL LHFSAARGKE
RCVRVFLEHG ADPTVKDLIG GFTALHYAAM HGRARIARLM LESEYRSDII NAKSNDGWTP
LHVAAHYGRD SFVRLLLEFK AEVDPLSDKG TTPLQLAIIR ERSSCVKILL DHNANIDIQN
GFLLRYAVIK SNHSYCRMFL QRGADTNLGR LEDGQTPLHL SALRDDVLCA RMLYNYGADT
NTRNYEGQTP LAVSISISGS SRPCLDFLQE VTRQPRNLQD LCRIKIRQCI GLQNLKLLDE
LPIAKVMKDY LKHKFDDI
//
