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Q15645 (PCH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pachytene checkpoint protein 2 homolog
Alternative name(s):
Human papillomavirus type 16 E1 protein-binding protein
Short name=16E1-BP
Short name=HPV16 E1 protein-binding protein
Thyroid hormone receptor interactor 13
Thyroid receptor-interacting protein 13
Short name=TR-interacting protein 13
Short name=TRIP-13
Gene names
Name:TRIP13
Synonyms:PCH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in chromosome recombination and chromosome structure development during meiosis. Required at early steps in meiotic recombination that leads to non-crossovers pathways. Also needed for efficient completion of homologous synapsis by influencing crossover distribution along the chromosomes affecting both crossovers and non-crossovers pathways. Also required for development of higher-order chromosome structures and is needed for synaptonemal-complex formation. In males, required for efficient synapsis of the sex chromosomes and for sex body formation. Promotes early steps of the DNA double-strand breaks (DSBs) repair process upstream of the assembly of RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from synapsed chromosomes By similarity.

Subunit structure

Specifically interacts with the ligand binding domain of the thyroid receptor (TR). This interaction does not require the presence of thyroid hormone for its interaction. Interacts with HPV16 E1. Ref.1 Ref.5

Sequence similarities

Belongs to the AAA ATPase family. PCH2 subfamily.

Sequence caution

The sequence AAC41732.1 differs from that shown. Reason: Frameshift at positions 1 and 5.

Ontologies

Keywords
   Biological processDifferentiation
Meiosis
Oogenesis
Spermatogenesis
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdouble-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

female meiosis I

Inferred from electronic annotation. Source: Ensembl

male meiosis I

Inferred from electronic annotation. Source: Ensembl

oocyte maturation

Inferred from electronic annotation. Source: Ensembl

oogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

reciprocal meiotic recombination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of RNA biosynthetic process

Traceable author statement Ref.5. Source: GOC

spermatid development

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

synaptonemal complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from RNA polymerase II promoter

Traceable author statement Ref.5. Source: ProtInc

   Cellular_componentmale germ cell nucleus

Inferred from electronic annotation. Source: Ensembl

nucleus

Traceable author statement Ref.5. Source: ProtInc

   Molecular_functionATP binding

Non-traceable author statement Ref.1. Source: UniProtKB

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

transcription cofactor activity

Traceable author statement Ref.5. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15645-1)

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: Q15645-2)

The sequence of this isoform differs from the canonical sequence as follows:
     171-406: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Pachytene checkpoint protein 2 homolog
PRO_0000084782

Regions

Nucleotide binding179 – 1868ATP Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.12

Natural variations

Alternative sequence171 – 406236Missing in isoform 2.
VSP_016957

Sequences

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

Last modified January 10, 2006. Version 2.
Checksum: DFB0B37462D1D581

FASTA43248,551
        10         20         30         40         50         60 
MDEAVGDLKQ ALPCVAESPT VHVEVHQRGS STAKKEDINL SVRKLLNRHN IVFGDYTWTE 

        70         80         90        100        110        120 
FDEPFLTRNV QSVSIIDTEL KVKDSQPIDL SACTVALHIF QLNEDGPSSE NLEEETENII 

       130        140        150        160        170        180 
AANHWVLPAA EFHGLWDSLV YDVEVKSHLL DYVMTTLLFS DKNVNSNLIT WNRVVLLHGP 

       190        200        210        220        230        240 
PGTGKTSLCK ALAQKLTIRL SSRYRYGQLI EINSHSLFSK WFSESGKLVT KMFQKIQDLI 

       250        260        270        280        290        300 
DDKDALVFVL IDEVESLTAA RNACRAGTEP SDAIRVVNAV LTQIDQIKRH SNVVILTTSN 

       310        320        330        340        350        360 
ITEKIDVAFV DRADIKQYIG PPSAAAIFKI YLSCLEELMK CQIIYPRQQL LTLRELEMIG 

       370        380        390        400        410        420 
FIENNVSKLS LLLNDISRKS EGLSGRVLRK LPFLAHALYV QAPTVTIEGF LQALSLAVDK 

       430 
QFEERKKLAA YI 

« Hide

Isoform 2 [UniParc].

Checksum: 74AF9425508B518A
Show »

FASTA19622,084

References

« Hide 'large scale' references
[1]"Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteins."
Yasugi T., Vidal M., Sakai H., Howley P.M., Benson J.D.
J. Virol. 71:5942-5951(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HPV16 E1.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] (ISOFORM 1).
Tissue: Lung.
[5]"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-417 (ISOFORM 2), INTERACTION WITH THRA.
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96131 mRNA. Translation: AAB64095.1.
CR456744 mRNA. Translation: CAG33025.1.
AC122719 Genomic DNA. No translation available.
CH471102 Genomic DNA. Translation: EAX08185.1.
CH471102 Genomic DNA. Translation: EAX08186.1.
BC000404 mRNA. Translation: AAH00404.1.
BC019294 mRNA. Translation: AAH19294.1.
L40384 mRNA. Translation: AAC41732.1. Frameshift.
RefSeqNP_004228.1. NM_004237.3.
UniGeneHs.436187.

3D structure databases

ProteinModelPortalQ15645.
SMRQ15645. Positions 71-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114730. 73 interactions.
DIPDIP-34493N.
IntActQ15645. 58 interactions.
MINTMINT-1146352.
STRING9606.ENSP00000166345.

PTM databases

PhosphoSiteQ15645.

Polymorphism databases

DMDM85541056.

Proteomic databases

PaxDbQ15645.
PeptideAtlasQ15645.
PRIDEQ15645.

Protocols and materials databases

DNASU9319.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000166345; ENSP00000166345; ENSG00000071539. [Q15645-1]
GeneID9319.
KEGGhsa:9319.
UCSCuc003jbr.3. human. [Q15645-1]

Organism-specific databases

CTD9319.
GeneCardsGC05P000892.
HGNCHGNC:12307. TRIP13.
HPAHPA005727.
HPA053093.
MIM604507. gene.
neXtProtNX_Q15645.
PharmGKBPA36986.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000234557.
HOVERGENHBG052830.
InParanoidQ15645.
OMAAASHWVL.
OrthoDBEOG71VST9.
PhylomeDBQ15645.
TreeFamTF313507.

Gene expression databases

BgeeQ15645.
CleanExHS_TRIP13.
GenevestigatorQ15645.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR001270. ClpA/B.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTRIP13.
GenomeRNAi9319.
NextBio34909.
PROQ15645.
SOURCESearch...

Entry information

Entry namePCH2_HUMAN
AccessionPrimary (citable) accession number: Q15645
Secondary accession number(s): C9K0T3, D3DTC0, O15324
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 115 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

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