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Protein

Ubiquitin-like domain-containing CTD phosphatase 1

Gene

UBLCP1

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

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like domain-containing CTD phosphatase 1 (EC:3.1.3.16)
Alternative name(s):
Nuclear proteasome inhibitor UBLCP1
Gene namesi
Name:UBLCP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:28110. UBLCP1.

Subcellular locationi

Nucleus 2 Publications
Note: Colocalizes with nuclear proteasomes.

GO - Cellular componenti

  1. nucleolus Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441K → A: No binding to proteasome. 1 Publication

Organism-specific databases

PharmGKBiPA142670646.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 318317Ubiquitin-like domain-containing CTD phosphatase 1PRO_0000242640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei117 – 1171N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8WVY7.
PaxDbiQ8WVY7.
PeptideAtlasiQ8WVY7.
PRIDEiQ8WVY7.

PTM databases

DEPODiQ8WVY7.
PhosphoSiteiQ8WVY7.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8WVY7.
CleanExiHS_UBLCP1.
GenevestigatoriQ8WVY7.

Organism-specific databases

HPAiHPA039615.

Interactioni

Protein-protein interaction databases

BioGridi126404. 10 interactions.
IntActiQ8WVY7. 2 interactions.
MINTiMINT-1445291.
STRINGi9606.ENSP00000296786.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi12 – 165Combined sources
Turni21 – 233Combined sources
Helixi25 – 3612Combined sources
Turni40 – 423Combined sources
Beta strandi44 – 474Combined sources
Beta strandi57 – 593Combined sources
Helixi61 – 644Combined sources
Beta strandi68 – 769Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KX3NMR-A1-81[»]
2LGDNMR-A1-81[»]
2M17NMR-A1-81[»]
ProteinModelPortaliQ8WVY7.
SMRiQ8WVY7. Positions 1-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8179Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini133 – 294162FCP1 homologyPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 294162PhosphataseAdd
BLAST

Domaini

The Ubiquitin-like domain mediates interaction with proteasomes.

Sequence similaritiesi

Contains 1 FCP1 homology domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG310886.
GeneTreeiENSGT00390000010107.
HOGENOMiHOG000231279.
HOVERGENiHBG080207.
InParanoidiQ8WVY7.
KOiK17618.
OMAiARRVKDY.
OrthoDBiEOG74TX01.
PhylomeDBiQ8WVY7.
TreeFamiTF323786.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR011943. HAD-SF_hydro_IIID.
IPR004274. NIF.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF03031. NIF. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00577. CPDc. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02245. HAD_IIID1. 1 hit.
PROSITEiPS50969. FCP1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8WVY7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALPIIVKWG GQEYSVTTLS EDDTVLDLKQ FLKTLTGVLP ERQKLLGLKV
60 70 80 90 100
KGKPAENDVK LGALKLKPNT KIMMMGTREE SLEDVLGPPP DNDDVVNDFD
110 120 130 140 150
IEDEVVEVEN REENLLKISR RVKEYKVEIL NPPREGKKLL VLDVDYTLFD
160 170 180 190 200
HRSCAETGVE LMRPYLHEFL TSAYEDYDIV IWSATNMKWI EAKMKELGVS
210 220 230 240 250
TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS EFYSKKNTIM
260 270 280 290 300
FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELLKLTQY LKEIAKLDDF
310
LDLNHKYWER YLSKKQGQ
Length:318
Mass (Da):36,805
Last modified:October 1, 2002 - v2
Checksum:i21CB4DB22C3B0E0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831E → G in BAB71628. (PubMed:14702039)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4345.1.
RefSeqiNP_659486.2. NM_145049.3.
UniGeneiHs.591733.

Genome annotation databases

EnsembliENST00000296786; ENSP00000296786; ENSG00000164332.
GeneIDi134510.
KEGGihsa:134510.
UCSCiuc003lxq.2. human.

Polymorphism databases

DMDMi74751564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4345.1.
RefSeqiNP_659486.2. NM_145049.3.
UniGeneiHs.591733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KX3NMR-A1-81[»]
2LGDNMR-A1-81[»]
2M17NMR-A1-81[»]
ProteinModelPortaliQ8WVY7.
SMRiQ8WVY7. Positions 1-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126404. 10 interactions.
IntActiQ8WVY7. 2 interactions.
MINTiMINT-1445291.
STRINGi9606.ENSP00000296786.

PTM databases

DEPODiQ8WVY7.
PhosphoSiteiQ8WVY7.

Polymorphism databases

DMDMi74751564.

Proteomic databases

MaxQBiQ8WVY7.
PaxDbiQ8WVY7.
PeptideAtlasiQ8WVY7.
PRIDEiQ8WVY7.

Protocols and materials databases

DNASUi134510.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296786; ENSP00000296786; ENSG00000164332.
GeneIDi134510.
KEGGihsa:134510.
UCSCiuc003lxq.2. human.

Organism-specific databases

CTDi134510.
GeneCardsiGC05P158690.
HGNCiHGNC:28110. UBLCP1.
HPAiHPA039615.
MIMi609867. gene.
neXtProtiNX_Q8WVY7.
PharmGKBiPA142670646.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310886.
GeneTreeiENSGT00390000010107.
HOGENOMiHOG000231279.
HOVERGENiHBG080207.
InParanoidiQ8WVY7.
KOiK17618.
OMAiARRVKDY.
OrthoDBiEOG74TX01.
PhylomeDBiQ8WVY7.
TreeFamiTF323786.

Miscellaneous databases

ChiTaRSiUBLCP1. human.
GenomeRNAii134510.
NextBioi83393.
PROiQ8WVY7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WVY7.
CleanExiHS_UBLCP1.
GenevestigatoriQ8WVY7.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR011943. HAD-SF_hydro_IIID.
IPR004274. NIF.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF03031. NIF. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00577. CPDc. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02245. HAD_IIID1. 1 hit.
PROSITEiPS50969. FCP1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiUBCP1_HUMAN
AccessioniPrimary (citable) accession number: Q8WVY7
Secondary accession number(s): D3DQJ7, Q96DK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2002
Last modified: February 4, 2015
This is version 108 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.