Q8WVY7 (UBCP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-like domain-containing CTD phosphatase 1
EC=3.1.3.16

Alternative name(s):
Nuclear proteasome inhibitor UBLCP1

Gene names

Name:

UBLCP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. Ref.1
Cofactor	Magnesium. Ref.1
Subcellular location	Nucleus. Note: Colocalizes with nuclear proteasomes. Ref.1 Ref.7
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 component	Nucleus
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	nucleolus Inferred from direct assay. Source: HPA
Molecular_function	phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 318

318

Ubiquitin-like domain-containing CTD phosphatase 1

PRO_0000242640

Regions

Domain

3 – 81

79

Ubiquitin-like

Domain

133 – 294

162

FCP1 homology

Region

133 – 294

162

Phosphatase

Amino acid modifications

Modified residue

117

1

N6-acetyllysine Ref.5

Experimental info

Mutagenesis

44

1

K → A: No binding to proteasome. Ref.7

Sequence conflict

83

1

E → G in BAB71628. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

318

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Beta strand

12 – 16

5

Turn

21 – 23

3

Helix

25 – 35

11

Turn

39 – 41

3

Beta strand

46 – 49

4

Helix

61 – 64

4

Helix

68 – 70

3

Sequences

	Sequence		Length	Mass (Da)
	Q8WVY7 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: 21CB4DB22C3B0E0F	FASTA	318	36,805
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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, MASS SPECTROMETRY.
[6]	"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].
[7]	"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.
+	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.

IPI

IPI00291669.

RefSeq

NP_659486.2. NM_145049.3.

UniGene

Hs.591733.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KX3	NMR	-	A	1-81	[»]
2LGD	NMR	-	A	1-81	[»]

ProteinModelPortal

Q8WVY7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WVY7. 2 interactions.

MINT

MINT-1445291.

STRING

9606.ENSP00000296786.

PTM databases

PhosphoSite

Q8WVY7.

Polymorphism databases

DMDM

74751564.

Proteomic databases

PaxDb

Q8WVY7.

PeptideAtlas

Q8WVY7.

PRIDE

Q8WVY7.

Protocols and materials databases

DNASU

134510.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296786; ENSP00000296786; ENSG00000164332.

GeneID

134510.

KEGG

hsa:134510.

UCSC

uc003lxq.2. human.

Organism-specific databases

CTD

134510.

GeneCards

GC05P158690.

HGNC

HGNC:28110. UBLCP1.

HPA

HPA039615.

MIM

609867. gene.

neXtProt

NX_Q8WVY7.

PharmGKB

PA142670646.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG310886.

HOGENOM

HOG000231279.

HOVERGEN

HBG080207.

InParanoid

Q8WVY7.

KO

K01090.

OMA

KWIDAKM.

OrthoDB

EOG476K0P.

PhylomeDB

Q8WVY7.

Gene expression databases

Bgee

Q8WVY7.

CleanEx

HS_UBLCP1.

Genevestigator

Q8WVY7.

GermOnline

ENSG00000164332. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1000. 1 hit.

InterPro

IPR023214. HAD-like_dom.
IPR011943. HAD-SF_hydro_IIID.
IPR004274. NIF.
IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

Pfam

PF03031. NIF. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]

SMART

SM00577. CPDc. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR02245. HAD_IIID1. 1 hit.

PROSITE

PS50969. FCP1. 1 hit.
PS00299. UBIQUITIN_1. False negative.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

134510.

NextBio

83393.

SOURCE

Search...

Entry information

Entry name

UBCP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.