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DPH7_HUMAN
ID   DPH7_HUMAN              Reviewed;         452 AA.
AC   Q9BTV6; Q96AB7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Diphthine methyltransferase;
DE            EC=3.1.1.97;
DE   AltName: Full=Diphthamide biosynthesis protein 7;
DE   AltName: Full=WD repeat-containing protein 85;
GN   Name=DPH7; Synonyms=C9orf112, WDR85;
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=Placenta;
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 MRNA].
RC   TISSUE=Brain, and Skin;
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.
RX   PubMed=19965467; DOI=10.1126/science.1178955;
RA   Carette J.E., Guimaraes C.P., Varadarajan M., Park A.S., Wuethrich I.,
RA   Godarova A., Kotecki M., Cochran B.H., Spooner E., Ploegh H.L.,
RA   Brummelkamp T.R.;
RT   "Haploid genetic screens in human cells identify host factors used by
RT   pathogens.";
RL   Science 326:1231-1235(2009).
RN   [5]
RP   FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS.
RX   PubMed=23486472; DOI=10.1074/jbc.m113.461343;
RA   Wei H., Bera T.K., Wayne A.S., Xiang L., Colantonio S., Chertov O.,
RA   Pastan I.;
RT   "A modified form of diphthamide causes immunotoxin resistance in a lymphoma
RT   cell line with a deletion of the WDR85 gene.";
RL   J. Biol. Chem. 288:12305-12312(2013).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [7]
RP   INTERACTION WITH INCA1.
RX   PubMed=21750715; DOI=10.1371/journal.pone.0021505;
RA   Zhang F., Baeumer N., Rode M., Ji P., Zhang T., Berdel W.E.,
RA   Mueller-Tidow C.;
RT   "The inhibitor of growth protein 5 (ING5) depends on INCA1 as a co-factor
RT   for its antiproliferative effects.";
RL   PLoS ONE 6:E21505-E21505(2011).
CC   -!- FUNCTION: Catalyzes the demethylation of diphthine methyl ester to form
CC       diphthine, an intermediate diphthamide biosynthesis, a post-
CC       translational modification of histidine which occurs in translation
CC       elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria
CC       toxin and by Pseudomonas exotoxin A (Eta).
CC       {ECO:0000250|UniProtKB:P38332, ECO:0000269|PubMed:19965467,
CC       ECO:0000269|PubMed:23486472}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphthine methyl ester-[translation elongation factor 2] + H2O
CC         = diphthine-[translation elongation factor 2] + H(+) + methanol;
CC         Xref=Rhea:RHEA:42656, Rhea:RHEA-COMP:10172, Rhea:RHEA-COMP:10173,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC         ChEBI:CHEBI:79005, ChEBI:CHEBI:82696; EC=3.1.1.97;
CC         Evidence={ECO:0000250|UniProtKB:P38332};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC   -!- SUBUNIT: Interacts with INCA1. {ECO:0000269|PubMed:21750715}.
CC   -!- INTERACTION:
CC       Q9BTV6; Q0VD86: INCA1; NbExp=2; IntAct=EBI-11059920, EBI-6509505;
CC   -!- SIMILARITY: Belongs to the DPH7 family. {ECO:0000305}.
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DR   EMBL; AK075115; BAC11411.1; -; mRNA.
DR   EMBL; AL365502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003123; AAH03123.2; -; mRNA.
DR   EMBL; BC017335; AAH17335.1; -; mRNA.
DR   CCDS; CCDS7047.1; -.
DR   RefSeq; NP_620133.1; NM_138778.4.
DR   AlphaFoldDB; Q9BTV6; -.
DR   SMR; Q9BTV6; -.
DR   BioGRID; 124971; 18.
DR   IntAct; Q9BTV6; 11.
DR   STRING; 9606.ENSP00000277540; -.
DR   GlyGen; Q9BTV6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BTV6; -.
DR   PhosphoSitePlus; Q9BTV6; -.
DR   BioMuta; DPH7; -.
DR   DMDM; 68565266; -.
DR   EPD; Q9BTV6; -.
DR   jPOST; Q9BTV6; -.
DR   MassIVE; Q9BTV6; -.
DR   MaxQB; Q9BTV6; -.
DR   PaxDb; Q9BTV6; -.
DR   PeptideAtlas; Q9BTV6; -.
DR   PRIDE; Q9BTV6; -.
DR   ProteomicsDB; 79014; -.
DR   Antibodypedia; 19075; 107 antibodies from 18 providers.
DR   DNASU; 92715; -.
DR   Ensembl; ENST00000277540.7; ENSP00000277540.2; ENSG00000148399.13.
DR   GeneID; 92715; -.
DR   KEGG; hsa:92715; -.
DR   MANE-Select; ENST00000277540.7; ENSP00000277540.2; NM_138778.5; NP_620133.1.
DR   UCSC; uc004cnk.1; human.
DR   CTD; 92715; -.
DR   DisGeNET; 92715; -.
DR   GeneCards; DPH7; -.
DR   HGNC; HGNC:25199; DPH7.
DR   HPA; ENSG00000148399; Low tissue specificity.
DR   MIM; 613210; gene.
DR   neXtProt; NX_Q9BTV6; -.
DR   OpenTargets; ENSG00000148399; -.
DR   PharmGKB; PA134942088; -.
DR   VEuPathDB; HostDB:ENSG00000148399; -.
DR   eggNOG; KOG0280; Eukaryota.
DR   GeneTree; ENSGT00390000018644; -.
DR   HOGENOM; CLU_036100_2_1_1; -.
DR   InParanoid; Q9BTV6; -.
DR   OMA; LDMKWLP; -.
DR   OrthoDB; 960224at2759; -.
DR   PhylomeDB; Q9BTV6; -.
DR   TreeFam; TF324407; -.
DR   BRENDA; 3.1.1.97; 2681.
DR   PathwayCommons; Q9BTV6; -.
DR   Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2.
DR   SignaLink; Q9BTV6; -.
DR   UniPathway; UPA00559; -.
DR   BioGRID-ORCS; 92715; 15 hits in 1070 CRISPR screens.
DR   ChiTaRS; DPH7; human.
DR   GenomeRNAi; 92715; -.
DR   Pharos; Q9BTV6; Tbio.
DR   PRO; PR:Q9BTV6; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9BTV6; protein.
DR   Bgee; ENSG00000148399; Expressed in right uterine tube and 141 other tissues.
DR   Genevisible; Q9BTV6; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0061685; F:diphthine methylesterase activity; IBA:GO_Central.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IMP:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..452
FT                   /note="Diphthine methyltransferase"
FT                   /id="PRO_0000050906"
FT   REPEAT          79..130
FT                   /note="WD 1"
FT   REPEAT          131..185
FT                   /note="WD 2"
FT   REPEAT          186..229
FT                   /note="WD 3"
FT   REPEAT          230..273
FT                   /note="WD 4"
FT   REPEAT          274..313
FT                   /note="WD 5"
FT   REPEAT          314..403
FT                   /note="WD 6"
FT   REPEAT          404..448
FT                   /note="WD 7"
FT   REGION          371..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         158
FT                   /note="G -> R (in dbSNP:rs821314)"
FT                   /id="VAR_053437"
SQ   SEQUENCE   452 AA;  50575 MW;  B79D25EE38096733 CRC64;
     MMGCFALQTV DTELTADSVE WCPLQGCRHL LACGTYQLRR PEDRPAGPQN KGGMEVKEPQ
     VRLGRLFLYS FNDNNSIHPL VEVQRKDTSA ILDMKWCHIP VAGHALLGLA DASGSIQLLR
     LVESEKSHVL EPLSSLALEE QCLALSLDWS TGKTGRAGDQ PLKIISSDST GQLHLLMVNE
     TRPRLQKVAS WQAHQFEAWI AAFNYWHPEI VYSGGDDGLL RGWDTRVPGK FLFTSKRHTM
     GVCSIQSSPH REHILATGSY DEHILLWDTR NMKQPLADTP VQGGVWRIKW HPFHHHLLLA
     ACMHSGFKIL NCQKAMEERQ EATVLTSHTL PDSLVYGADW SWLLFRSLQR APSWSFPSNL
     GTKTADLKGA SELPTPCHEC REDNDGEGHA RPQSGMKPLT EGMRKNGTWL QATAATTRDC
     GVNPEEADSA FSLLATCSFY DHALHLWEWE GN
 
 
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