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GID4_HUMAN
ID   GID4_HUMAN              Reviewed;         300 AA.
AC   Q8IVV7; Q8TEB5; Q9BW50;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Glucose-induced degradation protein 4 homolog;
DE   AltName: Full=Vacuolar import and degradation protein 24 homolog;
GN   Name=GID4; Synonyms=C17orf39, VID24;
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].
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=Eye, and Testis;
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   FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=29911972; DOI=10.7554/elife.35528;
RA   Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA   Picotti P., Stoffel M., Peter M.;
RT   "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT   the transcription factor Hbp1 for degradation.";
RL   Elife 7:0-0(2018).
RN   [5] {ECO:0007744|PDB:6CCR, ECO:0007744|PDB:6CCT, ECO:0007744|PDB:6CCU, ECO:0007744|PDB:6CD8, ECO:0007744|PDB:6CD9, ECO:0007744|PDB:6CDC, ECO:0007744|PDB:6CDG}
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 124-289 IN COMPLEXES WITH PEPTIDE
RP   SUBSTRATES, FUNCTION, DOMAIN, AND MUTAGENESIS OF.
RX   PubMed=29632410; DOI=10.1038/s41589-018-0036-1;
RA   Dong C., Zhang H., Li L., Tempel W., Loppnau P., Min J.;
RT   "Molecular basis of GID4-mediated recognition of degrons for the Pro/N-end
RT   rule pathway.";
RL   Nat. Chem. Biol. 14:466-473(2018).
CC   -!- FUNCTION: Substrate-recognition subunit of the CTLH E3 ubiquitin-
CC       protein ligase complex that selectively accepts ubiquitin from UBE2H
CC       and mediates ubiquitination and subsequent proteasomal degradation of
CC       the transcription factor HBP1 (Probable) (PubMed:29911972). Binds
CC       proteins and peptides with a Pro/N-degron consisting of an unmodified
CC       N-terminal Pro followed by a small residue, and has the highest
CC       affinity for the peptide Pro-Gly-Leu-Trp (PubMed:29632410). Binds
CC       peptides with an N-terminal sequence of the type Pro-[Ala,Gly]-
CC       [Leu,Met,Gln,Ser,Tyr]-[Glu,Gly,His,Ser,Val,Trp,Tyr]. Does not bind
CC       peptides with an acetylated N-terminal Pro residue (PubMed:29632410).
CC       {ECO:0000269|PubMed:29632410, ECO:0000269|PubMed:29911972,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC       and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC       RMND5B), GID8, ARMC8, WDR26 and YPEL5 (PubMed:29911972). Within this
CC       complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8,
CC       WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4,
CC       MKLN1, ARMC8 and YPEL5 have ancillary roles (PubMed:29911972).
CC       {ECO:0000269|PubMed:29911972}.
CC   -!- DOMAIN: The first four residues of target peptides with a free N-
CC       terminal Pro (a Pro/N-degron) are bound inside a deep and narrow beta-
CC       barrel structure. {ECO:0000269|PubMed:29632410}.
CC   -!- SIMILARITY: Belongs to the GID4/VID24 family. {ECO:0000305}.
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DR   EMBL; AK074284; BAB85036.1; -; mRNA.
DR   EMBL; AC087164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000636; AAH00636.2; -; mRNA.
DR   EMBL; BC041829; AAH41829.1; -; mRNA.
DR   CCDS; CCDS11190.1; -.
DR   RefSeq; NP_076957.3; NM_024052.4.
DR   PDB; 6CCR; X-ray; 1.60 A; A=116-300.
DR   PDB; 6CCT; X-ray; 2.40 A; A=124-289.
DR   PDB; 6CCU; X-ray; 1.75 A; A=116-300.
DR   PDB; 6CD8; X-ray; 1.60 A; A/B=124-289.
DR   PDB; 6CD9; X-ray; 1.55 A; A=124-289.
DR   PDB; 6CDC; X-ray; 1.75 A; A=124-289.
DR   PDB; 6CDG; X-ray; 1.60 A; A=124-289.
DR   PDB; 6WZX; X-ray; 1.75 A; A/B=124-289.
DR   PDB; 6WZZ; X-ray; 1.60 A; A=124-289.
DR   PDB; 7NSC; EM; 3.30 A; D=1-300.
DR   PDB; 7Q4Y; X-ray; 3.08 A; A/B=100-300.
DR   PDB; 7Q50; X-ray; 3.16 A; A=121-290.
DR   PDB; 7S12; X-ray; 2.15 A; A=124-289.
DR   PDB; 7SLZ; X-ray; 1.97 A; A=124-289.
DR   PDBsum; 6CCR; -.
DR   PDBsum; 6CCT; -.
DR   PDBsum; 6CCU; -.
DR   PDBsum; 6CD8; -.
DR   PDBsum; 6CD9; -.
DR   PDBsum; 6CDC; -.
DR   PDBsum; 6CDG; -.
DR   PDBsum; 6WZX; -.
DR   PDBsum; 6WZZ; -.
DR   PDBsum; 7NSC; -.
DR   PDBsum; 7Q4Y; -.
DR   PDBsum; 7Q50; -.
DR   PDBsum; 7S12; -.
DR   PDBsum; 7SLZ; -.
DR   AlphaFoldDB; Q8IVV7; -.
DR   SMR; Q8IVV7; -.
DR   BioGRID; 122487; 127.
DR   IntAct; Q8IVV7; 29.
DR   STRING; 9606.ENSP00000268719; -.
DR   GlyGen; Q8IVV7; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q8IVV7; -.
DR   PhosphoSitePlus; Q8IVV7; -.
DR   BioMuta; GID4; -.
DR   DMDM; 73620594; -.
DR   EPD; Q8IVV7; -.
DR   jPOST; Q8IVV7; -.
DR   MassIVE; Q8IVV7; -.
DR   MaxQB; Q8IVV7; -.
DR   PaxDb; Q8IVV7; -.
DR   PeptideAtlas; Q8IVV7; -.
DR   PRIDE; Q8IVV7; -.
DR   ProteomicsDB; 70778; -.
DR   Antibodypedia; 25602; 88 antibodies from 18 providers.
DR   DNASU; 79018; -.
DR   Ensembl; ENST00000268719.9; ENSP00000268719.4; ENSG00000141034.10.
DR   GeneID; 79018; -.
DR   KEGG; hsa:79018; -.
DR   MANE-Select; ENST00000268719.9; ENSP00000268719.4; NM_024052.5; NP_076957.3.
DR   UCSC; uc002gsg.2; human.
DR   CTD; 79018; -.
DR   DisGeNET; 79018; -.
DR   GeneCards; GID4; -.
DR   HGNC; HGNC:28453; GID4.
DR   HPA; ENSG00000141034; Tissue enhanced (testis).
DR   MIM; 617699; gene.
DR   neXtProt; NX_Q8IVV7; -.
DR   OpenTargets; ENSG00000141034; -.
DR   PharmGKB; PA134994398; -.
DR   VEuPathDB; HostDB:ENSG00000141034; -.
DR   eggNOG; KOG4635; Eukaryota.
DR   GeneTree; ENSGT00500000044930; -.
DR   HOGENOM; CLU_081159_0_0_1; -.
DR   InParanoid; Q8IVV7; -.
DR   OMA; KHWGQFL; -.
DR   PhylomeDB; Q8IVV7; -.
DR   TreeFam; TF323749; -.
DR   PathwayCommons; Q8IVV7; -.
DR   SignaLink; Q8IVV7; -.
DR   BioGRID-ORCS; 79018; 16 hits in 1073 CRISPR screens.
DR   ChiTaRS; GID4; human.
DR   GenomeRNAi; 79018; -.
DR   Pharos; Q8IVV7; Tbio.
DR   PRO; PR:Q8IVV7; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q8IVV7; protein.
DR   Bgee; ENSG00000141034; Expressed in left testis and 190 other tissues.
DR   ExpressionAtlas; Q8IVV7; baseline and differential.
DR   Genevisible; Q8IVV7; HS.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR018618; Vacuolar_import/degrad_Vid24.
DR   Pfam; PF09783; Vac_ImportDeg; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Glucose-induced degradation protein 4 homolog"
FT                   /id="PRO_0000079302"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            132
FT                   /note="Interaction with the N-terminal Pro (Pro/N-degron)
FT                   of proteins that are targeted for degradation"
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   SITE            237
FT                   /note="Interaction with the N-terminal Pro (Pro/N-degron)
FT                   of proteins that are targeted for degradation"
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   SITE            258
FT                   /note="Interaction with the N-terminal Pro (Pro/N-degron)
FT                   of proteins that are targeted for degradation"
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   MUTAGEN         132
FT                   /note="Q->A: Loss of interaction with peptides with a
FT                   Pro/N-degron."
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   MUTAGEN         237
FT                   /note="E->A: Loss of interaction with peptides with a
FT                   Pro/N-degron."
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   MUTAGEN         253
FT                   /note="S->D: Strongly decreased affinity for peptides with
FT                   a Pro/N-degron."
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   MUTAGEN         258
FT                   /note="Y->A: Loss of interaction with peptides with a
FT                   Pro/N-degron."
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   MUTAGEN         273
FT                   /note="Y->A: Loss of interaction with peptides with a
FT                   Pro/N-degron."
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   MUTAGEN         282
FT                   /note="Q->A: Loss of interaction with peptides with a
FT                   Pro/N-degron."
FT                   /evidence="ECO:0000269|PubMed:29632410"
FT   CONFLICT        146
FT                   /note="Q -> R (in Ref. 1; BAB85036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="Y -> H (in Ref. 1; BAB85036)"
FT                   /evidence="ECO:0000305"
FT   STRAND          127..133
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   STRAND          138..149
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   TURN            150..153
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   STRAND          154..167
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   STRAND          169..179
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   HELIX           195..202
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   TURN            211..216
FT                   /evidence="ECO:0007829|PDB:6CCR"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:6CDC"
FT   HELIX           222..227
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   STRAND          228..242
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   HELIX           251..254
FT                   /evidence="ECO:0007829|PDB:6CCR"
FT   STRAND          256..263
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   TURN            264..267
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   STRAND          268..274
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   STRAND          283..289
FT                   /evidence="ECO:0007829|PDB:6CD9"
FT   HELIX           290..292
FT                   /evidence="ECO:0007829|PDB:6CCR"
SQ   SEQUENCE   300 AA;  33514 MW;  9FE12824E9C46CD4 CRC64;
     MCARGQVGRG TQLRTGRPCS QVPGSRWRPE RLLRRQRAGG RPSRPHPARA RPGLSLPATL
     LGSRAAAAVP LPLPPALAPG DPAMPVRTEC PPPAGASAAS AASLIPPPPI NTQQPGVATS
     LLYSGSKFRG HQKSKGNSYD VEVVLQHVDT GNSYLCGYLK IKGLTEEYPT LTTFFEGEII
     SKKHPFLTRK WDADEDVDRK HWGKFLAFYQ YAKSFNSDDF DYEELKNGDY VFMRWKEQFL
     VPDHTIKDIS GASFAGFYYI CFQKSAASIE GYYYHRSSEW YQSLNLTHVP EHSAPIYEFR
 
 
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