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Q96JH7 (VCIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deubiquitinating protein VCIP135

EC=3.4.19.12
Alternative name(s):
Valosin-containing protein p97/p47 complex-interacting protein 1
Valosin-containing protein p97/p47 complex-interacting protein p135
Short name=VCP/p47 complex-interacting 135-kDa protein
Gene names
Name:VCPIP1
Synonyms:KIAA1850, VCIP135
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a deubiquitinating enzyme. Necessary for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP By similarity. Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. Ref.12

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Ref.12

Subunit structure

Binds VCP and the ternary complex containing STX5A, NSFL1C and VCP By similarity.

Subcellular location

Endoplasmic reticulum By similarity. Golgi apparatusGolgi stack By similarity. Note: Associated with Golgi stacks and endoplasmic reticulum By similarity.

Sequence similarities

Contains 1 OTU domain.

Sequence caution

The sequence BAB15552.1 differs from that shown. Reason: Frameshift at positions 1065 and 1110.

The sequence BAB47479.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12221222Deubiquitinating protein VCIP135
PRO_0000065769

Regions

Domain208 – 361154OTU
Compositional bias4 – 2421Pro-rich

Sites

Active site2161 By similarity
Active site2191Nucleophile By similarity
Active site3541 By similarity

Amino acid modifications

Modified residue4081N6-acetyllysine Ref.8
Modified residue7471Phosphoserine Ref.6
Modified residue7631Phosphothreonine Ref.6
Modified residue9941Phosphoserine Ref.6
Modified residue11981Phosphoserine Ref.6 Ref.7 Ref.9 Ref.11
Cross-link870Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Experimental info

Sequence conflict1691L → P in CAD89944. Ref.2
Sequence conflict4371Q → R in CAD89944. Ref.2
Sequence conflict8111P → F in AAH49379. Ref.3
Sequence conflict9271Missing Ref.3
Sequence conflict9881A → S in AAH49379. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q96JH7 [UniParc].

Last modified February 16, 2004. Version 2.
Checksum: 5CE99D723386782D

FASTA1,222134,321
        10         20         30         40         50         60 
MSQPPPPPPP LPPPPPPPEA PQTPSSLASA AASGGLLKRR DRRILSGSCP DPKCQARLFF 

        70         80         90        100        110        120 
PASGSVSIEC TECGQRHEQQ QLLGVEEVTD PDVVLHNLLR NALLGVTGAP KKNTELVKVM 

       130        140        150        160        170        180 
GLSNYHCKLL SPILARYGMD KQTGRAKLLR DMNQGELFDC ALLGDRAFLI EPEHVNTVGY 

       190        200        210        220        230        240 
GKDRSGSLLY LHDTLEDIKR ANKSQECLIP VHVDGDGHCL VHAVSRALVG RELFWHALRE 

       250        260        270        280        290        300 
NLKQHFQQHL ARYQALFHDF IDAAEWEDII NECDPLFVPP EGVPLGLRNI HIFGLANVLH 

       310        320        330        340        350        360 
RPIILLDSLS GMRSSGDYSA TFLPGLIPAE KCTGKDGHLN KPICIAWSSS GRNHYIPLVG 

       370        380        390        400        410        420 
IKGAALPKLP MNLLPKAWGV PQDLIKKYIK LEEDGGCVIG GDRSLQDKYL LRLVAAMEEV 

       430        440        450        460        470        480 
FMDKHGIHPS LVADVHQYFY RRTGVIGVQP EEVTAAAKKA VMDNRLHKCL LCGALSELHV 

       490        500        510        520        530        540 
PPEWLAPGGK LYNLAKSTHG QLRTDKNYSF PLNNLVCSYD SVKDVLVPDY GMSNLTACNW 

       550        560        570        580        590        600 
CHGTSVRKVR GDGSIVYLDG DRTNSRSTGG KCGCGFKHFW DGKEYDNLPE AFPITLEWGG 

       610        620        630        640        650        660 
RVVRETVYWF QYESDSSLNS NVYDVAMKLV TKHFPGEFGS EILVQKVVHT ILHQTAKKNP 

       670        680        690        700        710        720 
DDYTPVNIDG AHAQRVGDVQ GQESESQLPT KIILTGQKTK TLHKEELNMS KTERTIQQNI 

       730        740        750        760        770        780 
TEQASVMQKR KTEKLKQEQK GQPRTVSPST IRDGPSSAPA TPTKAPYSPT TSKEKKIRIT 

       790        800        810        820        830        840 
TNDGRQSMVT LKSSTTFFEL QESIAREFNI PPYLQCIRYG FPPKELMPPQ AGMEKEPVPL 

       850        860        870        880        890        900 
QHGDRITIEI LKSKAEGGQS AAAHSAHTVK QEDIAVTGKL SSKELQEQAE KEMYSLCLLA 

       910        920        930        940        950        960 
TLMGEDVWSY AKGLPHMFQQ GGVFYSIMKK TMGMADGKHC TFPHLPGKTF VYNASEDRLE 

       970        980        990       1000       1010       1020 
LCVDAAGHFP IGPDVEDLVK EAVSQVRAEA TTRSRESSPS HGLLKLGSGG VVKKKSEQLH 

      1030       1040       1050       1060       1070       1080 
NVTAFQGKGH SLGTASGNPH LDPRARETSV VRKHNTGTDF SNSSTKTEPS VFTASSSNSE 

      1090       1100       1110       1120       1130       1140 
LIRIAPGVVT MRDGRQLDPD LVEAQRKKLQ EMVSSIQASM DRHLRDQSTE QSPSDLPQRK 

      1150       1160       1170       1180       1190       1200 
TEVVSSSAKS GSLQTGLPES FPLTGGTENL NTETTDGCVA DALGAAFATR SKAQRGNSVE 

      1210       1220 
ELEEMDSQDA EMTNTTEPMD HS 

« Hide

References

« Hide 'large scale' references
[1]"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."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Melanoma.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis and Uterus.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1184.
Tissue: Lung.
[5]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-870.
Tissue: Mammary cancer.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747; THR-763; SER-994 AND SER-1198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB058753 mRNA. Translation: BAB47479.1. Different initiation.
AL834476 mRNA. Translation: CAD39135.1.
AL832606 mRNA. Translation: CAD89944.1.
BC049379 mRNA. Translation: AAH49379.1.
BC094799 mRNA. Translation: AAH94799.1.
AK026785 mRNA. Translation: BAB15552.1. Frameshift.
CCDSCCDS6192.1.
RefSeqNP_079330.2. NM_025054.4.
UniGeneHs.632066.

3D structure databases

ProteinModelPortalQ96JH7.
SMRQ96JH7. Positions 191-371, 777-849.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123125. 25 interactions.
IntActQ96JH7. 23 interactions.
MINTMINT-1197027.
STRING9606.ENSP00000309031.

Protein family/group databases

MEROPSC64.006.

PTM databases

PhosphoSiteQ96JH7.

Polymorphism databases

DMDM42560002.

Proteomic databases

MaxQBQ96JH7.
PaxDbQ96JH7.
PeptideAtlasQ96JH7.
PRIDEQ96JH7.

Protocols and materials databases

DNASU80124.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310421; ENSP00000309031; ENSG00000175073.
GeneID80124.
KEGGhsa:80124.
UCSCuc003xwn.3. human.

Organism-specific databases

CTD80124.
GeneCardsGC08M067540.
HGNCHGNC:30897. VCPIP1.
HPAHPA023932.
MIM611745. gene.
neXtProtNX_Q96JH7.
PharmGKBPA142670629.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262027.
HOGENOMHOG000154813.
HOVERGENHBG059748.
InParanoidQ96JH7.
KOK11861.
OMAQTAKKNP.
OrthoDBEOG7FV3PG.
PhylomeDBQ96JH7.
TreeFamTF329469.

Gene expression databases

BgeeQ96JH7.
CleanExHS_VCPIP1.
GenevestigatorQ96JH7.

Family and domain databases

InterProIPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF02338. OTU. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiVCPIP1.
GenomeRNAi80124.
NextBio70360.
PROQ96JH7.
SOURCESearch...

Entry information

Entry nameVCIP1_HUMAN
AccessionPrimary (citable) accession number: Q96JH7
Secondary accession number(s): Q504T4 expand/collapse secondary AC list , Q86T93, Q86W01, Q8N3A9, Q9H5R8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: July 9, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM