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Q8WVY7 (UBCP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Ubiquitin-like domain-containing CTD phosphatase 1

EC=3.1.3.16
Alternative name(s):
Nuclear proteasome inhibitor UBLCP1
Gene names
Name:UBLCP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome. Ref.1 Ref.8

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.1

Cofactor

Magnesium. Ref.1

Subcellular location

Nucleus. Note: Colocalizes with nuclear proteasomes. Ref.1 Ref.8

Tissue specificity

Broadly expressed, with highest levels in placenta, lung, testis and ovary. Up-regulated in tumor tissues. Ref.1

Domain

The Ubiquitin-like domain mediates interaction with proteasomes.

Sequence similarities

Contains 1 FCP1 homology domain.

Contains 1 ubiquitin-like domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0. Ref.1

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionphosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 318317Ubiquitin-like domain-containing CTD phosphatase 1
PRO_0000242640

Regions

Domain3 – 8179Ubiquitin-like
Domain133 – 294162FCP1 homology
Region133 – 294162Phosphatase

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.9
Modified residue1171N6-acetyllysine Ref.6

Experimental info

Mutagenesis441K → A: No binding to proteasome. Ref.8
Sequence conflict831E → G in BAB71628. Ref.2

Secondary structure

.................... 318
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WVY7 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 21CB4DB22C3B0E0F

FASTA31836,805
        10         20         30         40         50         60 
MALPIIVKWG GQEYSVTTLS EDDTVLDLKQ FLKTLTGVLP ERQKLLGLKV KGKPAENDVK 

        70         80         90        100        110        120 
LGALKLKPNT KIMMMGTREE SLEDVLGPPP DNDDVVNDFD IEDEVVEVEN REENLLKISR 

       130        140        150        160        170        180 
RVKEYKVEIL NPPREGKKLL VLDVDYTLFD HRSCAETGVE LMRPYLHEFL TSAYEDYDIV 

       190        200        210        220        230        240 
IWSATNMKWI EAKMKELGVS TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS 

       250        260        270        280        290        300 
EFYSKKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELLKLTQY LKEIAKLDDF 

       310 
LDLNHKYWER YLSKKQGQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase."
Zheng H., Ji C., Gu S., Shi B., Wang J., Xie Y., Mao Y.
Biochem. Biophys. Res. Commun. 331:1401-1407(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PRELIMINARY FUNCTION.
Tissue: Fetal brain.
[2]"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].
Tissue: Gastric mucosa.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Lung.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[6]"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-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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].
[8]"UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity."
Guo X., Engel J.L., Xiao J., Tagliabracci V.S., Wang X., Huang L., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 108:18649-18654(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ABSENCE OF INFLUENCE ON POLR2A CTD PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-44.
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY444562 mRNA. Translation: AAS68538.1.
AK057996 mRNA. Translation: BAB71628.1.
CH471062 Genomic DNA. Translation: EAW61577.1.
CH471062 Genomic DNA. Translation: EAW61578.1.
BC013425 mRNA. Translation: AAH13425.2.
CCDSCCDS4345.1.
RefSeqNP_659486.2. NM_145049.3.
UniGeneHs.591733.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KX3NMR-A1-81[»]
2LGDNMR-A1-81[»]
2M17NMR-A1-81[»]
ProteinModelPortalQ8WVY7.
SMRQ8WVY7. Positions 1-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126404. 7 interactions.
IntActQ8WVY7. 2 interactions.
MINTMINT-1445291.
STRING9606.ENSP00000296786.

PTM databases

PhosphoSiteQ8WVY7.

Polymorphism databases

DMDM74751564.

Proteomic databases

MaxQBQ8WVY7.
PaxDbQ8WVY7.
PeptideAtlasQ8WVY7.
PRIDEQ8WVY7.

Protocols and materials databases

DNASU134510.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296786; ENSP00000296786; ENSG00000164332.
GeneID134510.
KEGGhsa:134510.
UCSCuc003lxq.2. human.

Organism-specific databases

CTD134510.
GeneCardsGC05P158690.
HGNCHGNC:28110. UBLCP1.
HPAHPA039615.
MIM609867. gene.
neXtProtNX_Q8WVY7.
PharmGKBPA142670646.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310886.
HOGENOMHOG000231279.
HOVERGENHBG080207.
InParanoidQ8WVY7.
KOK17618.
OMAELNPPRE.
OrthoDBEOG74TX01.
PhylomeDBQ8WVY7.
TreeFamTF323786.

Gene expression databases

BgeeQ8WVY7.
CleanExHS_UBLCP1.
GenevestigatorQ8WVY7.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR011943. HAD-SF_hydro_IIID.
IPR004274. NIF.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF03031. NIF. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00577. CPDc. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02245. HAD_IIID1. 1 hit.
PROSITEPS50969. FCP1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi134510.
NextBio83393.
PROQ8WVY7.
SOURCESearch...

Entry information

Entry nameUBCP1_HUMAN
AccessionPrimary (citable) accession number: Q8WVY7
Secondary accession number(s): D3DQJ7, Q96DK5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 103 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM