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Q8WW12 (PCNP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PEST proteolytic signal-containing nuclear protein

Short name=PCNP
Short name=PEST-containing nuclear protein
Gene names
Name:PCNP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in cell cycle regulation.

Subunit structure

Interacts with UHRF2/NIRF. Ref.1 Ref.7

Subcellular location

Nucleus Ref.1.

Post-translational modification

Ubiquitinated; mediated by UHRF2 and leading to its subsequent proteasomal degradation. Ref.7

N-terminally acetylated in a HYPK-dependent manner by the NatA acetyltransferase complex which is composed of NAA10 and NAA15. Ref.11

Sequence caution

The sequence EAW79790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence EAW79792.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.7. Source: HGNC

protein ubiquitination

Inferred from direct assay Ref.7. Source: HGNC

   Cellular_componentnucleus

Inferred from direct assay Ref.1. Source: HGNC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WW12-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WW12-2)

The sequence of this isoform differs from the canonical sequence as follows:
     119-130: SEPEEMPPEAKM → GYTNISWTKLLQ
     131-178: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8WW12-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 178177PEST proteolytic signal-containing nuclear protein
PRO_0000058253

Amino acid modifications

Modified residue21N-acetylalanine Ref.11
Modified residue641N6-acetyllysine Ref.10
Modified residue871Phosphoserine Ref.8
Modified residue1191Phosphoserine Ref.8 Ref.13
Modified residue1391Phosphothreonine Ref.8
Modified residue1471Phosphoserine Ref.13
Modified residue1501N6-acetyllysine Ref.10
Modified residue1521N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 123123Missing in isoform 3.
VSP_013879
Alternative sequence119 – 13012SEPEE…PEAKM → GYTNISWTKLLQ in isoform 2.
VSP_013880
Alternative sequence131 – 17848Missing in isoform 2.
VSP_013881

Experimental info

Sequence conflict1261P → Q in AAH22001. Ref.6
Sequence conflict1501K → E in BAD96698. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: B79D49B362892AE1

FASTA17818,925
        10         20         30         40         50         60 
MADGKAGDEK PEKSQRAGAA GGPEEEAEKP VKTKTVSSSN GGESSSRSAE KRSAEEEAAD 

        70         80         90        100        110        120 
LPTKPTKISK FGFAIGSQTT KKASAISIKL GSSKPKETVP TLAPKTLSVA AAFNEDEDSE 

       130        140        150        160        170 
PEEMPPEAKM RMKNIGRDTP TSAGPNSFNK GKHGFSDNQK LWERNIKSHL GNVHDQDN 

« Hide

Isoform 2 [UniParc].

Checksum: 60256023D3435196
Show »

FASTA13013,544
Isoform 3 [UniParc].

Checksum: C95818E33C1461F0
Show »

FASTA556,233

References

« Hide 'large scale' references
[1]"NIRF, a novel RING finger protein, is involved in cell-cycle regulation."
Mori T., Li Y., Hata H., Ono K., Kochi H.
Biochem. Biophys. Res. Commun. 296:530-536(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH UHRF2.
Tissue: 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] (ISOFORM 1).
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Small intestine.
[4]"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] (ISOFORM 3).
Tissue: Brain cortex.
[5]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].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Brain and Testis.
[7]"NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein."
Mori T., Li Y., Hata H., Kochi H.
FEBS Lett. 557:209-214(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH UHRF2.
[8]"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-87; SER-119 AND THR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-64; LYS-150 AND LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation."
Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.
Mol. Cell. Biol. 30:1898-1909(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT ALA-2 BY NATA ACETYLTRANSFERASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"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].
[13]"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-119 AND SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB037675 mRNA. Translation: BAB03501.1.
AK314629 mRNA. Translation: BAG37194.1.
AK222978 mRNA. Translation: BAD96698.1.
CR627371 mRNA. Translation: CAH10470.1.
CH471052 Genomic DNA. Translation: EAW79790.1. Different initiation.
CH471052 Genomic DNA. Translation: EAW79792.1. Different initiation.
BC013916 mRNA. Translation: AAH13916.1.
BC022001 mRNA. Translation: AAH22001.1.
RefSeqNP_065090.1. NM_020357.1.
UniGeneHs.744968.

3D structure databases

ProteinModelPortalQ8WW12.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121360. 6 interactions.
STRING9606.ENSP00000265260.

PTM databases

PhosphoSiteQ8WW12.

Polymorphism databases

DMDM67460963.

Proteomic databases

PaxDbQ8WW12.
PRIDEQ8WW12.

Protocols and materials databases

DNASU57092.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265260; ENSP00000265260; ENSG00000081154. [Q8WW12-1]
ENST00000296024; ENSP00000296024; ENSG00000081154. [Q8WW12-2]
ENST00000469941; ENSP00000470810; ENSG00000081154. [Q8WW12-3]
GeneID57092.
KEGGhsa:57092.
UCSCuc003dva.3. human. [Q8WW12-1]
uc003dvd.3. human. [Q8WW12-2]

Organism-specific databases

CTD57092.
GeneCardsGC03P101292.
HGNCHGNC:30023. PCNP.
HPAHPA035011.
MIM615210. gene.
neXtProtNX_Q8WW12.
PharmGKBPA143485572.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46363.
HOVERGENHBG059581.
InParanoidQ8WW12.
OMAPAKMSKF.
OrthoDBEOG7J70HR.
PhylomeDBQ8WW12.
TreeFamTF333058.

Gene expression databases

ArrayExpressQ8WW12.
BgeeQ8WW12.
CleanExHS_PCNP.
GenevestigatorQ8WW12.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSPCNP. human.
GenomeRNAi57092.
NextBio35489760.
PROQ8WW12.
SOURCESearch...

Entry information

Entry namePCNP_HUMAN
AccessionPrimary (citable) accession number: Q8WW12
Secondary accession number(s): B2RBE7 expand/collapse secondary AC list , D3DN52, Q53GF3, Q6AI44, Q96CU3, Q9NS81
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 19, 2014
This is version 89 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

MIM cross-references

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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM