Full text data of VCPIP1
VCPIP1
(KIAA1850, VCIP135)
[Confidence: low (only semi-automatic identification from reviews)]
Deubiquitinating protein VCIP135; 3.4.19.12 (Valosin-containing protein p97/p47 complex-interacting protein 1; Valosin-containing protein p97/p47 complex-interacting protein p135; VCP/p47 complex-interacting 135-kDa protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Deubiquitinating protein VCIP135; 3.4.19.12 (Valosin-containing protein p97/p47 complex-interacting protein 1; Valosin-containing protein p97/p47 complex-interacting protein p135; VCP/p47 complex-interacting 135-kDa protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96JH7
ID VCIP1_HUMAN Reviewed; 1222 AA.
AC Q96JH7; Q504T4; Q86T93; Q86W01; Q8N3A9; Q9H5R8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-FEB-2004, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Deubiquitinating protein VCIP135;
DE EC=3.4.19.12;
DE AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein 1;
DE AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein p135;
DE Short=VCP/p47 complex-interacting 135-kDa protein;
GN Name=VCPIP1; Synonyms=KIAA1850, VCIP135;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1184.
RC TISSUE=Lung;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-870, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747; THR-763; SER-994
RP AND SER-1198, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-408, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
CC -!- FUNCTION: Acts as a deubiquitinating enzyme. Necessary for VCP-
CC mediated reassembly of Golgi stacks after mitosis. May play a role
CC in VCP-mediated formation of transitional endoplasmic reticulum
CC (tER). Mediates dissociation of the ternary complex containing
CC STX5A, NSFL1C and VCP (By similarity). Hydrolyzes 'Lys-11'- and
CC 'Lys-48'-linked polyubiquitin chains.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Binds VCP and the ternary complex containing STX5A,
CC NSFL1C and VCP (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). Golgi
CC apparatus, Golgi stack (By similarity). Note=Associated with Golgi
CC stacks and endoplasmic reticulum (By similarity).
CC -!- SIMILARITY: Contains 1 OTU domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15552.1; Type=Frameshift; Positions=1065, 1110;
CC Sequence=BAB47479.1; Type=Erroneous initiation;
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DR EMBL; AB058753; BAB47479.1; ALT_INIT; mRNA.
DR EMBL; AL834476; CAD39135.1; -; mRNA.
DR EMBL; AL832606; CAD89944.1; -; mRNA.
DR EMBL; BC049379; AAH49379.1; -; mRNA.
DR EMBL; BC094799; AAH94799.1; -; mRNA.
DR EMBL; AK026785; BAB15552.1; ALT_FRAME; mRNA.
DR RefSeq; NP_079330.2; NM_025054.4.
DR UniGene; Hs.632066; -.
DR ProteinModelPortal; Q96JH7; -.
DR SMR; Q96JH7; 191-371.
DR IntAct; Q96JH7; 23.
DR MINT; MINT-1197027; -.
DR STRING; 9606.ENSP00000309031; -.
DR MEROPS; C64.006; -.
DR PhosphoSite; Q96JH7; -.
DR DMDM; 42560002; -.
DR PaxDb; Q96JH7; -.
DR PeptideAtlas; Q96JH7; -.
DR PRIDE; Q96JH7; -.
DR DNASU; 80124; -.
DR Ensembl; ENST00000310421; ENSP00000309031; ENSG00000175073.
DR GeneID; 80124; -.
DR KEGG; hsa:80124; -.
DR UCSC; uc003xwn.3; human.
DR CTD; 80124; -.
DR GeneCards; GC08M067540; -.
DR HGNC; HGNC:30897; VCPIP1.
DR HPA; HPA023932; -.
DR MIM; 611745; gene.
DR neXtProt; NX_Q96JH7; -.
DR PharmGKB; PA142670629; -.
DR eggNOG; NOG262027; -.
DR HOGENOM; HOG000154813; -.
DR HOVERGEN; HBG059748; -.
DR InParanoid; Q96JH7; -.
DR KO; K11861; -.
DR OMA; QTAKKNP; -.
DR OrthoDB; EOG7FV3PG; -.
DR PhylomeDB; Q96JH7; -.
DR GeneWiki; VCPIP1; -.
DR GenomeRNAi; 80124; -.
DR NextBio; 70360; -.
DR PRO; PR:Q96JH7; -.
DR Bgee; Q96JH7; -.
DR CleanEx; HS_VCPIP1; -.
DR Genevestigator; Q96JH7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:Ensembl.
DR GO; GO:0090168; P:Golgi reassembly; IEA:Ensembl.
DR GO; GO:0007067; P:mitosis; IEA:Ensembl.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR003323; OTU.
DR Pfam; PF02338; OTU; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum;
KW Golgi apparatus; Hydrolase; Isopeptide bond; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1 1222 Deubiquitinating protein VCIP135.
FT /FTId=PRO_0000065769.
FT DOMAIN 208 361 OTU.
FT COMPBIAS 4 24 Pro-rich.
FT ACT_SITE 216 216 By similarity.
FT ACT_SITE 219 219 Nucleophile (By similarity).
FT ACT_SITE 354 354 By similarity.
FT MOD_RES 408 408 N6-acetyllysine.
FT MOD_RES 747 747 Phosphoserine.
FT MOD_RES 763 763 Phosphothreonine.
FT MOD_RES 994 994 Phosphoserine.
FT MOD_RES 1198 1198 Phosphoserine.
FT CROSSLNK 870 870 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 169 169 L -> P (in Ref. 2; CAD89944).
FT CONFLICT 437 437 Q -> R (in Ref. 2; CAD89944).
FT CONFLICT 811 811 P -> F (in Ref. 3; AAH49379).
FT CONFLICT 927 927 Missing (in Ref. 3).
FT CONFLICT 988 988 A -> S (in Ref. 3; AAH49379).
SQ SEQUENCE 1222 AA; 134321 MW; 5CE99D723386782D CRC64;
MSQPPPPPPP LPPPPPPPEA PQTPSSLASA AASGGLLKRR DRRILSGSCP DPKCQARLFF
PASGSVSIEC TECGQRHEQQ QLLGVEEVTD PDVVLHNLLR NALLGVTGAP KKNTELVKVM
GLSNYHCKLL SPILARYGMD KQTGRAKLLR DMNQGELFDC ALLGDRAFLI EPEHVNTVGY
GKDRSGSLLY LHDTLEDIKR ANKSQECLIP VHVDGDGHCL VHAVSRALVG RELFWHALRE
NLKQHFQQHL ARYQALFHDF IDAAEWEDII NECDPLFVPP EGVPLGLRNI HIFGLANVLH
RPIILLDSLS GMRSSGDYSA TFLPGLIPAE KCTGKDGHLN KPICIAWSSS GRNHYIPLVG
IKGAALPKLP MNLLPKAWGV PQDLIKKYIK LEEDGGCVIG GDRSLQDKYL LRLVAAMEEV
FMDKHGIHPS LVADVHQYFY RRTGVIGVQP EEVTAAAKKA VMDNRLHKCL LCGALSELHV
PPEWLAPGGK LYNLAKSTHG QLRTDKNYSF PLNNLVCSYD SVKDVLVPDY GMSNLTACNW
CHGTSVRKVR GDGSIVYLDG DRTNSRSTGG KCGCGFKHFW DGKEYDNLPE AFPITLEWGG
RVVRETVYWF QYESDSSLNS NVYDVAMKLV TKHFPGEFGS EILVQKVVHT ILHQTAKKNP
DDYTPVNIDG AHAQRVGDVQ GQESESQLPT KIILTGQKTK TLHKEELNMS KTERTIQQNI
TEQASVMQKR KTEKLKQEQK GQPRTVSPST IRDGPSSAPA TPTKAPYSPT TSKEKKIRIT
TNDGRQSMVT LKSSTTFFEL QESIAREFNI PPYLQCIRYG FPPKELMPPQ AGMEKEPVPL
QHGDRITIEI LKSKAEGGQS AAAHSAHTVK QEDIAVTGKL SSKELQEQAE KEMYSLCLLA
TLMGEDVWSY AKGLPHMFQQ GGVFYSIMKK TMGMADGKHC TFPHLPGKTF VYNASEDRLE
LCVDAAGHFP IGPDVEDLVK EAVSQVRAEA TTRSRESSPS HGLLKLGSGG VVKKKSEQLH
NVTAFQGKGH SLGTASGNPH LDPRARETSV VRKHNTGTDF SNSSTKTEPS VFTASSSNSE
LIRIAPGVVT MRDGRQLDPD LVEAQRKKLQ EMVSSIQASM DRHLRDQSTE QSPSDLPQRK
TEVVSSSAKS GSLQTGLPES FPLTGGTENL NTETTDGCVA DALGAAFATR SKAQRGNSVE
ELEEMDSQDA EMTNTTEPMD HS
//
ID VCIP1_HUMAN Reviewed; 1222 AA.
AC Q96JH7; Q504T4; Q86T93; Q86W01; Q8N3A9; Q9H5R8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-FEB-2004, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Deubiquitinating protein VCIP135;
DE EC=3.4.19.12;
DE AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein 1;
DE AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein p135;
DE Short=VCP/p47 complex-interacting 135-kDa protein;
GN Name=VCPIP1; Synonyms=KIAA1850, VCIP135;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1184.
RC TISSUE=Lung;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-870, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747; THR-763; SER-994
RP AND SER-1198, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-408, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
CC -!- FUNCTION: Acts as a deubiquitinating enzyme. Necessary for VCP-
CC mediated reassembly of Golgi stacks after mitosis. May play a role
CC in VCP-mediated formation of transitional endoplasmic reticulum
CC (tER). Mediates dissociation of the ternary complex containing
CC STX5A, NSFL1C and VCP (By similarity). Hydrolyzes 'Lys-11'- and
CC 'Lys-48'-linked polyubiquitin chains.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Binds VCP and the ternary complex containing STX5A,
CC NSFL1C and VCP (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). Golgi
CC apparatus, Golgi stack (By similarity). Note=Associated with Golgi
CC stacks and endoplasmic reticulum (By similarity).
CC -!- SIMILARITY: Contains 1 OTU domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15552.1; Type=Frameshift; Positions=1065, 1110;
CC Sequence=BAB47479.1; Type=Erroneous initiation;
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DR EMBL; AB058753; BAB47479.1; ALT_INIT; mRNA.
DR EMBL; AL834476; CAD39135.1; -; mRNA.
DR EMBL; AL832606; CAD89944.1; -; mRNA.
DR EMBL; BC049379; AAH49379.1; -; mRNA.
DR EMBL; BC094799; AAH94799.1; -; mRNA.
DR EMBL; AK026785; BAB15552.1; ALT_FRAME; mRNA.
DR RefSeq; NP_079330.2; NM_025054.4.
DR UniGene; Hs.632066; -.
DR ProteinModelPortal; Q96JH7; -.
DR SMR; Q96JH7; 191-371.
DR IntAct; Q96JH7; 23.
DR MINT; MINT-1197027; -.
DR STRING; 9606.ENSP00000309031; -.
DR MEROPS; C64.006; -.
DR PhosphoSite; Q96JH7; -.
DR DMDM; 42560002; -.
DR PaxDb; Q96JH7; -.
DR PeptideAtlas; Q96JH7; -.
DR PRIDE; Q96JH7; -.
DR DNASU; 80124; -.
DR Ensembl; ENST00000310421; ENSP00000309031; ENSG00000175073.
DR GeneID; 80124; -.
DR KEGG; hsa:80124; -.
DR UCSC; uc003xwn.3; human.
DR CTD; 80124; -.
DR GeneCards; GC08M067540; -.
DR HGNC; HGNC:30897; VCPIP1.
DR HPA; HPA023932; -.
DR MIM; 611745; gene.
DR neXtProt; NX_Q96JH7; -.
DR PharmGKB; PA142670629; -.
DR eggNOG; NOG262027; -.
DR HOGENOM; HOG000154813; -.
DR HOVERGEN; HBG059748; -.
DR InParanoid; Q96JH7; -.
DR KO; K11861; -.
DR OMA; QTAKKNP; -.
DR OrthoDB; EOG7FV3PG; -.
DR PhylomeDB; Q96JH7; -.
DR GeneWiki; VCPIP1; -.
DR GenomeRNAi; 80124; -.
DR NextBio; 70360; -.
DR PRO; PR:Q96JH7; -.
DR Bgee; Q96JH7; -.
DR CleanEx; HS_VCPIP1; -.
DR Genevestigator; Q96JH7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:Ensembl.
DR GO; GO:0090168; P:Golgi reassembly; IEA:Ensembl.
DR GO; GO:0007067; P:mitosis; IEA:Ensembl.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR003323; OTU.
DR Pfam; PF02338; OTU; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum;
KW Golgi apparatus; Hydrolase; Isopeptide bond; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1 1222 Deubiquitinating protein VCIP135.
FT /FTId=PRO_0000065769.
FT DOMAIN 208 361 OTU.
FT COMPBIAS 4 24 Pro-rich.
FT ACT_SITE 216 216 By similarity.
FT ACT_SITE 219 219 Nucleophile (By similarity).
FT ACT_SITE 354 354 By similarity.
FT MOD_RES 408 408 N6-acetyllysine.
FT MOD_RES 747 747 Phosphoserine.
FT MOD_RES 763 763 Phosphothreonine.
FT MOD_RES 994 994 Phosphoserine.
FT MOD_RES 1198 1198 Phosphoserine.
FT CROSSLNK 870 870 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 169 169 L -> P (in Ref. 2; CAD89944).
FT CONFLICT 437 437 Q -> R (in Ref. 2; CAD89944).
FT CONFLICT 811 811 P -> F (in Ref. 3; AAH49379).
FT CONFLICT 927 927 Missing (in Ref. 3).
FT CONFLICT 988 988 A -> S (in Ref. 3; AAH49379).
SQ SEQUENCE 1222 AA; 134321 MW; 5CE99D723386782D CRC64;
MSQPPPPPPP LPPPPPPPEA PQTPSSLASA AASGGLLKRR DRRILSGSCP DPKCQARLFF
PASGSVSIEC TECGQRHEQQ QLLGVEEVTD PDVVLHNLLR NALLGVTGAP KKNTELVKVM
GLSNYHCKLL SPILARYGMD KQTGRAKLLR DMNQGELFDC ALLGDRAFLI EPEHVNTVGY
GKDRSGSLLY LHDTLEDIKR ANKSQECLIP VHVDGDGHCL VHAVSRALVG RELFWHALRE
NLKQHFQQHL ARYQALFHDF IDAAEWEDII NECDPLFVPP EGVPLGLRNI HIFGLANVLH
RPIILLDSLS GMRSSGDYSA TFLPGLIPAE KCTGKDGHLN KPICIAWSSS GRNHYIPLVG
IKGAALPKLP MNLLPKAWGV PQDLIKKYIK LEEDGGCVIG GDRSLQDKYL LRLVAAMEEV
FMDKHGIHPS LVADVHQYFY RRTGVIGVQP EEVTAAAKKA VMDNRLHKCL LCGALSELHV
PPEWLAPGGK LYNLAKSTHG QLRTDKNYSF PLNNLVCSYD SVKDVLVPDY GMSNLTACNW
CHGTSVRKVR GDGSIVYLDG DRTNSRSTGG KCGCGFKHFW DGKEYDNLPE AFPITLEWGG
RVVRETVYWF QYESDSSLNS NVYDVAMKLV TKHFPGEFGS EILVQKVVHT ILHQTAKKNP
DDYTPVNIDG AHAQRVGDVQ GQESESQLPT KIILTGQKTK TLHKEELNMS KTERTIQQNI
TEQASVMQKR KTEKLKQEQK GQPRTVSPST IRDGPSSAPA TPTKAPYSPT TSKEKKIRIT
TNDGRQSMVT LKSSTTFFEL QESIAREFNI PPYLQCIRYG FPPKELMPPQ AGMEKEPVPL
QHGDRITIEI LKSKAEGGQS AAAHSAHTVK QEDIAVTGKL SSKELQEQAE KEMYSLCLLA
TLMGEDVWSY AKGLPHMFQQ GGVFYSIMKK TMGMADGKHC TFPHLPGKTF VYNASEDRLE
LCVDAAGHFP IGPDVEDLVK EAVSQVRAEA TTRSRESSPS HGLLKLGSGG VVKKKSEQLH
NVTAFQGKGH SLGTASGNPH LDPRARETSV VRKHNTGTDF SNSSTKTEPS VFTASSSNSE
LIRIAPGVVT MRDGRQLDPD LVEAQRKKLQ EMVSSIQASM DRHLRDQSTE QSPSDLPQRK
TEVVSSSAKS GSLQTGLPES FPLTGGTENL NTETTDGCVA DALGAAFATR SKAQRGNSVE
ELEEMDSQDA EMTNTTEPMD HS
//
MIM
611745
*RECORD*
*FIELD* NO
611745
*FIELD* TI
*611745 VCP/p47 COMPLEX-INTERACTING PROTEIN 1; VCPIP1
;;VCP/p47 COMPLEX-INTERACTING PROTEIN, 135-KD; VCIP135;;
read moreKIAA1850
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult hippocampus
cDNA library, Nagase et al. (2001) cloned VCPIP1, which they designated
KIAA1850. The deduced protein contains 1,236 amino acids. RT-PCR ELISA
detected moderate VCPIP1 expression in all adult and fetal tissues
examined.
GENE FUNCTION
Reassembly of the Golgi apparatus from membrane fragments after cell
division requires the ATPases NSF (601633) and p97 (VCP; 601023), as
well as the cofactor p47 (NSFL1C; 606610) and the receptor syntaxin-5
(STX5A; 603189). Uchiyama et al. (2002) showed that rat Vcip135 was
essential for p97/p47-mediated membrane fusion and that Vcip135 bound to
the p97/p47/Stx5a complex and dissociated it via p97-catalyzed ATP
hydrolysis. Microinjection of antibodies against Vcip135 and p47 in rat
kidney cells showed that Vcip135 and p47 were required for Golgi and
endoplasmic reticulum assembly.
Wang et al. (2004) found that p97/p47-mediated reassembly of Golgi
cisternae required ubiquitin. They identified rat Vcip135 as a
deubiquitinating enzyme and found that it reversed the ubiquitination
event that occurred during mitotic disassembly. Wang et al. (2004)
concluded that a cycle of ubiquitination and VCIP135-mediated
deubiquitination regulates Golgi membrane dynamics during mitosis.
MAPPING
By radiation hybrid analysis, Nagase et al. (2001) mapped the VCPIP1
gene to chromosome 8.
*FIELD* RF
1. Nagase, T.; Nakayama, M.; Nakajima, D.; Kikuno, R.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 8: 85-95, 2001.
2. Uchiyama, K.; Jokitalo, E.; Kano, F.; Murata, M.; Zhang, X.; Canas,
B.; Newman, R.; Rabouille, C.; Pappin, D.; Freemont, P.; Kondo, H.
: VCIP135, a novel essential factor for p97/p47-mediated membrane
fusion, is required for Golgi and ER assembly in vivo. J. Cell Biol. 159:
855-866, 2002.
3. Wang, Y.; Satoh, A.; Warren, G.; Meyer, H. H.: VCIP135 acts as
a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic
Golgi fragments. J. Cell Biol. 164: 973-978, 2004. Note: Erratum:
J. Cell Biol. 166: 433 only, 2004.
*FIELD* CD
Patricia A. Hartz: 1/22/2008
*FIELD* ED
terry: 09/25/2012
mgross: 1/22/2008
*RECORD*
*FIELD* NO
611745
*FIELD* TI
*611745 VCP/p47 COMPLEX-INTERACTING PROTEIN 1; VCPIP1
;;VCP/p47 COMPLEX-INTERACTING PROTEIN, 135-KD; VCIP135;;
read moreKIAA1850
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult hippocampus
cDNA library, Nagase et al. (2001) cloned VCPIP1, which they designated
KIAA1850. The deduced protein contains 1,236 amino acids. RT-PCR ELISA
detected moderate VCPIP1 expression in all adult and fetal tissues
examined.
GENE FUNCTION
Reassembly of the Golgi apparatus from membrane fragments after cell
division requires the ATPases NSF (601633) and p97 (VCP; 601023), as
well as the cofactor p47 (NSFL1C; 606610) and the receptor syntaxin-5
(STX5A; 603189). Uchiyama et al. (2002) showed that rat Vcip135 was
essential for p97/p47-mediated membrane fusion and that Vcip135 bound to
the p97/p47/Stx5a complex and dissociated it via p97-catalyzed ATP
hydrolysis. Microinjection of antibodies against Vcip135 and p47 in rat
kidney cells showed that Vcip135 and p47 were required for Golgi and
endoplasmic reticulum assembly.
Wang et al. (2004) found that p97/p47-mediated reassembly of Golgi
cisternae required ubiquitin. They identified rat Vcip135 as a
deubiquitinating enzyme and found that it reversed the ubiquitination
event that occurred during mitotic disassembly. Wang et al. (2004)
concluded that a cycle of ubiquitination and VCIP135-mediated
deubiquitination regulates Golgi membrane dynamics during mitosis.
MAPPING
By radiation hybrid analysis, Nagase et al. (2001) mapped the VCPIP1
gene to chromosome 8.
*FIELD* RF
1. Nagase, T.; Nakayama, M.; Nakajima, D.; Kikuno, R.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 8: 85-95, 2001.
2. Uchiyama, K.; Jokitalo, E.; Kano, F.; Murata, M.; Zhang, X.; Canas,
B.; Newman, R.; Rabouille, C.; Pappin, D.; Freemont, P.; Kondo, H.
: VCIP135, a novel essential factor for p97/p47-mediated membrane
fusion, is required for Golgi and ER assembly in vivo. J. Cell Biol. 159:
855-866, 2002.
3. Wang, Y.; Satoh, A.; Warren, G.; Meyer, H. H.: VCIP135 acts as
a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic
Golgi fragments. J. Cell Biol. 164: 973-978, 2004. Note: Erratum:
J. Cell Biol. 166: 433 only, 2004.
*FIELD* CD
Patricia A. Hartz: 1/22/2008
*FIELD* ED
terry: 09/25/2012
mgross: 1/22/2008