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Q96JH7

- VCIP1_HUMAN

UniProt

Q96JH7 - VCIP1_HUMAN

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Protein

Deubiquitinating protein VCIP135

Gene

VCPIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei216 – 2161By similarity
Active sitei219 – 2191NucleophileBy similarity
Active sitei354 – 3541By similarity

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. endoplasmic reticulum membrane fusion Source: Ensembl
  2. Golgi reassembly Source: Ensembl
  3. mitotic nuclear division Source: Ensembl
  4. protein K11-linked deubiquitination Source: UniProtKB
  5. protein K48-linked deubiquitination Source: UniProtKB
  6. protein ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC64.006.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:VCPIP1
Synonyms:KIAA1850, VCIP135
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:30897. VCPIP1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. endoplasmic reticulum Source: UniProtKB-KW
  3. Golgi apparatus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670629.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12221222Deubiquitinating protein VCIP135PRO_0000065769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei408 – 4081N6-acetyllysine1 Publication
Modified residuei747 – 7471Phosphoserine1 Publication
Modified residuei763 – 7631Phosphothreonine1 Publication
Cross-linki870 – 870Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei994 – 9941Phosphoserine1 Publication
Modified residuei1198 – 11981Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96JH7.
PaxDbiQ96JH7.
PeptideAtlasiQ96JH7.
PRIDEiQ96JH7.

PTM databases

PhosphoSiteiQ96JH7.

Expressioni

Gene expression databases

BgeeiQ96JH7.
CleanExiHS_VCPIP1.
GenevestigatoriQ96JH7.

Organism-specific databases

HPAiHPA023932.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi123125. 30 interactions.
IntActiQ96JH7. 23 interactions.
MINTiMINT-1197027.
STRINGi9606.ENSP00000309031.

Structurei

3D structure databases

ProteinModelPortaliQ96JH7.
SMRiQ96JH7. Positions 191-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini208 – 361154OTUPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 2421Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 OTU domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG262027.
GeneTreeiENSGT00390000002854.
HOGENOMiHOG000154813.
HOVERGENiHBG059748.
InParanoidiQ96JH7.
KOiK11861.
OMAiQTAKKNP.
OrthoDBiEOG7FV3PG.
PhylomeDBiQ96JH7.
TreeFamiTF329469.

Family and domain databases

InterProiIPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96JH7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQPPPPPPP LPPPPPPPEA PQTPSSLASA AASGGLLKRR DRRILSGSCP
60 70 80 90 100
DPKCQARLFF PASGSVSIEC TECGQRHEQQ QLLGVEEVTD PDVVLHNLLR
110 120 130 140 150
NALLGVTGAP KKNTELVKVM GLSNYHCKLL SPILARYGMD KQTGRAKLLR
160 170 180 190 200
DMNQGELFDC ALLGDRAFLI EPEHVNTVGY GKDRSGSLLY LHDTLEDIKR
210 220 230 240 250
ANKSQECLIP VHVDGDGHCL VHAVSRALVG RELFWHALRE NLKQHFQQHL
260 270 280 290 300
ARYQALFHDF IDAAEWEDII NECDPLFVPP EGVPLGLRNI HIFGLANVLH
310 320 330 340 350
RPIILLDSLS GMRSSGDYSA TFLPGLIPAE KCTGKDGHLN KPICIAWSSS
360 370 380 390 400
GRNHYIPLVG IKGAALPKLP MNLLPKAWGV PQDLIKKYIK LEEDGGCVIG
410 420 430 440 450
GDRSLQDKYL LRLVAAMEEV FMDKHGIHPS LVADVHQYFY RRTGVIGVQP
460 470 480 490 500
EEVTAAAKKA VMDNRLHKCL LCGALSELHV PPEWLAPGGK LYNLAKSTHG
510 520 530 540 550
QLRTDKNYSF PLNNLVCSYD SVKDVLVPDY GMSNLTACNW CHGTSVRKVR
560 570 580 590 600
GDGSIVYLDG DRTNSRSTGG KCGCGFKHFW DGKEYDNLPE AFPITLEWGG
610 620 630 640 650
RVVRETVYWF QYESDSSLNS NVYDVAMKLV TKHFPGEFGS EILVQKVVHT
660 670 680 690 700
ILHQTAKKNP DDYTPVNIDG AHAQRVGDVQ GQESESQLPT KIILTGQKTK
710 720 730 740 750
TLHKEELNMS KTERTIQQNI TEQASVMQKR KTEKLKQEQK GQPRTVSPST
760 770 780 790 800
IRDGPSSAPA TPTKAPYSPT TSKEKKIRIT TNDGRQSMVT LKSSTTFFEL
810 820 830 840 850
QESIAREFNI PPYLQCIRYG FPPKELMPPQ AGMEKEPVPL QHGDRITIEI
860 870 880 890 900
LKSKAEGGQS AAAHSAHTVK QEDIAVTGKL SSKELQEQAE KEMYSLCLLA
910 920 930 940 950
TLMGEDVWSY AKGLPHMFQQ GGVFYSIMKK TMGMADGKHC TFPHLPGKTF
960 970 980 990 1000
VYNASEDRLE LCVDAAGHFP IGPDVEDLVK EAVSQVRAEA TTRSRESSPS
1010 1020 1030 1040 1050
HGLLKLGSGG VVKKKSEQLH NVTAFQGKGH SLGTASGNPH LDPRARETSV
1060 1070 1080 1090 1100
VRKHNTGTDF SNSSTKTEPS VFTASSSNSE LIRIAPGVVT MRDGRQLDPD
1110 1120 1130 1140 1150
LVEAQRKKLQ EMVSSIQASM DRHLRDQSTE QSPSDLPQRK TEVVSSSAKS
1160 1170 1180 1190 1200
GSLQTGLPES FPLTGGTENL NTETTDGCVA DALGAAFATR SKAQRGNSVE
1210 1220
ELEEMDSQDA EMTNTTEPMD HS
Length:1,222
Mass (Da):134,321
Last modified:February 16, 2004 - v2
Checksum:i5CE99D723386782D
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691L → P in CAD89944. (PubMed:17974005)Curated
Sequence conflicti437 – 4371Q → R in CAD89944. (PubMed:17974005)Curated
Sequence conflicti811 – 8111P → F in AAH49379. (PubMed:15489334)Curated
Sequence conflicti927 – 9271Missing(PubMed:15489334)Curated
Sequence conflicti988 – 9881A → S in AAH49379. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6192.1.
RefSeqiNP_079330.2. NM_025054.4.
UniGeneiHs.632066.

Genome annotation databases

EnsembliENST00000310421; ENSP00000309031; ENSG00000175073.
GeneIDi80124.
KEGGihsa:80124.
UCSCiuc003xwn.3. human.

Polymorphism databases

DMDMi42560002.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS6192.1.
RefSeqi NP_079330.2. NM_025054.4.
UniGenei Hs.632066.

3D structure databases

ProteinModelPortali Q96JH7.
SMRi Q96JH7. Positions 191-371.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123125. 30 interactions.
IntActi Q96JH7. 23 interactions.
MINTi MINT-1197027.
STRINGi 9606.ENSP00000309031.

Protein family/group databases

MEROPSi C64.006.

PTM databases

PhosphoSitei Q96JH7.

Polymorphism databases

DMDMi 42560002.

Proteomic databases

MaxQBi Q96JH7.
PaxDbi Q96JH7.
PeptideAtlasi Q96JH7.
PRIDEi Q96JH7.

Protocols and materials databases

DNASUi 80124.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310421 ; ENSP00000309031 ; ENSG00000175073 .
GeneIDi 80124.
KEGGi hsa:80124.
UCSCi uc003xwn.3. human.

Organism-specific databases

CTDi 80124.
GeneCardsi GC08M067540.
HGNCi HGNC:30897. VCPIP1.
HPAi HPA023932.
MIMi 611745. gene.
neXtProti NX_Q96JH7.
PharmGKBi PA142670629.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262027.
GeneTreei ENSGT00390000002854.
HOGENOMi HOG000154813.
HOVERGENi HBG059748.
InParanoidi Q96JH7.
KOi K11861.
OMAi QTAKKNP.
OrthoDBi EOG7FV3PG.
PhylomeDBi Q96JH7.
TreeFami TF329469.

Miscellaneous databases

GeneWikii VCPIP1.
GenomeRNAii 80124.
NextBioi 70360.
PROi Q96JH7.
SOURCEi Search...

Gene expression databases

Bgeei Q96JH7.
CleanExi HS_VCPIP1.
Genevestigatori Q96JH7.

Family and domain databases

InterProi IPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF02338. OTU. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS50802. OTU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiVCIP1_HUMAN
AccessioniPrimary (citable) accession number: Q96JH7
Secondary accession number(s): Q504T4
, Q86T93, Q86W01, Q8N3A9, Q9H5R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3