Q15645 (PCH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	432 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Differentiation Meiosis Oogenesis Spermatogenesis
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB female meiosis I Inferred from electronic annotation. Source: Compara male meiosis I Inferred from electronic annotation. Source: Compara oocyte maturation Inferred from electronic annotation. Source: Compara oogenesis Inferred from sequence or structural similarity. Source: UniProtKB pachytene Inferred from electronic annotation. Source: Compara reciprocal meiotic recombination Inferred from sequence or structural similarity. Source: UniProtKB spermatid development Inferred from electronic annotation. Source: Compara 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_component	male germ cell nucleus Inferred from electronic annotation. Source: Compara nucleus Traceable author statement Ref.5. Source: ProtInc
Molecular_function	ATP 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARL11	Q969Q4	3	EBI-358993,EBI-751892
C11orf54	Q9H0W9	3	EBI-358993,EBI-740204
COMT	Q9BWC7	3	EBI-358993,EBI-743305
DDAH2	O95865	3	EBI-358993,EBI-749139
GLYCTK	Q8IVS8	3	EBI-358993,EBI-748515
HDHD3	Q9BSH5	3	EBI-358993,EBI-745201
KIAA1609	Q6P9B6	3	EBI-358993,EBI-746504
LASP1	Q14847	3	EBI-358993,EBI-742828
LOXL4	Q96JB6	3	EBI-358993,EBI-749562
MAD2L1BP	Q15013	5	EBI-358993,EBI-712181
NIF3L1	Q9GZT8	3	EBI-358993,EBI-740897
PARK2	O60260	3	EBI-358993,EBI-716346
PPP2CA	P67775	3	EBI-358993,EBI-712311
WDYHV1	Q96HA8	3	EBI-358993,EBI-741158

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 432	432	Pachytene checkpoint protein 2 homolog		PRO_0000084782
Regions
	Nucleotide binding	179 – 186	8	ATP Potential
Natural variations
	Alternative sequence	171 – 406	236	Missing in isoform 2.		VSP_016957

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 10, 2006. Version 2. Checksum: DFB0B37462D1D581	FASTA	432	48,551
	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
	Isoform 2 [UniParc]. Checksum: 74AF9425508B518A	FASTA	196	22,084
	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 IEGFLQALSL 190 AVDKQFEERK KLAAYI

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[10]	"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].
+	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.
IPI	IPI00003505. IPI00847729.
RefSeq	NP_004228.1. NM_004237.3.
UniGene	Hs.731712.
3D structure databases
ProteinModelPortal	Q15645.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15645. 51 interactions.
MINT	MINT-1146352.
STRING	9606.ENSP00000166345.
PTM databases
PhosphoSite	Q15645.
Polymorphism databases
DMDM	85541056.
Proteomic databases
PaxDb	Q15645.
PeptideAtlas	Q15645.
PRIDE	Q15645.
Protocols and materials databases
DNASU	9319.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000166345; ENSP00000166345; ENSG00000071539.
GeneID	9319.
KEGG	hsa:9319.
UCSC	uc003jbr.3. human.
Organism-specific databases
CTD	9319.
GeneCards	GC05P000892.
HGNC	HGNC:12307. TRIP13.
HPA	HPA005727.
MIM	604507. gene.
neXtProt	NX_Q15645.
PharmGKB	PA36986.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0464.
HOGENOM	HOG000234557.
HOVERGEN	HBG052830.
InParanoid	Q15645.
OMA	TEKIDMA.
OrthoDB	EOG4STS4K.
PhylomeDB	Q15645.
Gene expression databases
Bgee	Q15645.
CleanEx	HS_TRIP13.
Genevestigator	Q15645.
GermOnline	ENSG00000071539. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR001270. Chaprnin_ClpA/B. [Graphical view]
Pfam	PF00004. AAA. 1 hit. [Graphical view]
PRINTS	PR00300. CLPPROTEASEA.
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9319.
NextBio	34909.
SOURCE	Search...

Entry information

Entry name

PCH2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 107 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.