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Protein

Pachytene checkpoint protein 2 homolog

Gene

TRIP13

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

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1868ATPSequence Analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • transcription cofactor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Differentiation, Meiosis, Oogenesis, Spermatogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:TRIP13
Synonyms:PCH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:12307. TRIP13.

Subcellular locationi

GO - Cellular componenti

  • male germ cell nucleus Source: Ensembl
  • nucleus Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36986.

Polymorphism and mutation databases

BioMutaiTRIP13.
DMDMi85541056.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Pachytene checkpoint protein 2 homologPRO_0000084782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15645.
PaxDbiQ15645.
PeptideAtlasiQ15645.
PRIDEiQ15645.

PTM databases

PhosphoSiteiQ15645.

Expressioni

Gene expression databases

BgeeiQ15645.
CleanExiHS_TRIP13.
ExpressionAtlasiQ15645. baseline and differential.
GenevisibleiQ15645. HS.

Organism-specific databases

HPAiHPA005727.
HPA053093.

Interactioni

Subunit structurei

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 E1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-358993,EBI-358993
AMDHD2Q9Y3033EBI-358993,EBI-2798672
ARL11Q969Q43EBI-358993,EBI-751892
ARSAP152894EBI-358993,EBI-2117357
C11orf54Q9H0W93EBI-358993,EBI-740204
C4orf33Q8N1A63EBI-358993,EBI-10264911
CCBL1Q167733EBI-358993,EBI-10238309
COMTP219643EBI-358993,EBI-372265
COMTP21964-23EBI-358993,EBI-10200977
CYB5R2Q6BCY44EBI-358993,EBI-744761
DDAH2O958653EBI-358993,EBI-749139
DIP2AQ146893EBI-358993,EBI-2564275
DIP2AQ14689-63EBI-358993,EBI-10233719
DPYSL4O145313EBI-358993,EBI-719542
FNDC3BQ53EP0-33EBI-358993,EBI-10242151
GLYCTKQ8IVS86EBI-358993,EBI-748515
HDHD3Q9BSH53EBI-358993,EBI-745201
KRTAP12-1P599903EBI-358993,EBI-10210845
KRTAP12-2P599913EBI-358993,EBI-10176379
KRTAP26-1Q6PEX33EBI-358993,EBI-3957672
LASP1Q148477EBI-358993,EBI-742828
LNX1Q8TBB14EBI-358993,EBI-739832
LOXL4Q96JB66EBI-358993,EBI-749562
LRR1Q96L503EBI-358993,EBI-2510106
M1APQ8TC573EBI-358993,EBI-748182
MAD2L1BPQ150135EBI-358993,EBI-712181
METTL15A6NJ78-43EBI-358993,EBI-10174029
MORN3Q6PF183EBI-358993,EBI-9675802
MPPED2Q157775EBI-358993,EBI-2350461
NIF3L1Q9GZT83EBI-358993,EBI-740897
PARK2O602603EBI-358993,EBI-716346
PBLDP300394EBI-358993,EBI-750589
PCMTD2Q6PIM43EBI-358993,EBI-10253759
PELI1Q96FA33EBI-358993,EBI-448369
PLSCR3Q9NRY64EBI-358993,EBI-750734
PPP2CAP677753EBI-358993,EBI-712311
QARSP478973EBI-358993,EBI-347462
QARSP47897-23EBI-358993,EBI-10209725
RHOXF2Q9BQY45EBI-358993,EBI-372094
SCP2P223074EBI-358993,EBI-1050999
SEMA4GQ9NTN93EBI-358993,EBI-6447340
SEMA4GQ9NTN9-33EBI-358993,EBI-9089805
SIGLEC5O153894EBI-358993,EBI-750381
SPRYD7Q5W1113EBI-358993,EBI-10248098
TEX37Q96LM64EBI-358993,EBI-743976
TINAGL1Q9GZM73EBI-358993,EBI-715869
TINAGL1Q9GZM7-33EBI-358993,EBI-10303636
TLDC1Q6P9B63EBI-358993,EBI-746504
TNRC6AQ8NDV73EBI-358993,EBI-2269715
TPT1P136933EBI-358993,EBI-1783169
WDYHV1Q96HA83EBI-358993,EBI-741158

Protein-protein interaction databases

BioGridi114730. 104 interactions.
DIPiDIP-34493N.
IntActiQ15645. 78 interactions.
MINTiMINT-1146352.
STRINGi9606.ENSP00000166345.

Structurei

3D structure databases

ProteinModelPortaliQ15645.
SMRiQ15645. Positions 71-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family. PCH2 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00390000017432.
HOGENOMiHOG000234557.
HOVERGENiHBG052830.
InParanoidiQ15645.
OMAiVQIHVEV.
OrthoDBiEOG71VST9.
PhylomeDBiQ15645.
TreeFamiTF313507.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR001270. ClpA/B.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15645-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDEAVGDLKQ ALPCVAESPT VHVEVHQRGS STAKKEDINL SVRKLLNRHN
60 70 80 90 100
IVFGDYTWTE FDEPFLTRNV QSVSIIDTEL KVKDSQPIDL SACTVALHIF
110 120 130 140 150
QLNEDGPSSE NLEEETENII AANHWVLPAA EFHGLWDSLV YDVEVKSHLL
160 170 180 190 200
DYVMTTLLFS DKNVNSNLIT WNRVVLLHGP PGTGKTSLCK ALAQKLTIRL
210 220 230 240 250
SSRYRYGQLI EINSHSLFSK WFSESGKLVT KMFQKIQDLI DDKDALVFVL
260 270 280 290 300
IDEVESLTAA RNACRAGTEP SDAIRVVNAV LTQIDQIKRH SNVVILTTSN
310 320 330 340 350
ITEKIDVAFV DRADIKQYIG PPSAAAIFKI YLSCLEELMK CQIIYPRQQL
360 370 380 390 400
LTLRELEMIG FIENNVSKLS LLLNDISRKS EGLSGRVLRK LPFLAHALYV
410 420 430
QAPTVTIEGF LQALSLAVDK QFEERKKLAA YI
Length:432
Mass (Da):48,551
Last modified:January 10, 2006 - v2
Checksum:iDFB0B37462D1D581
GO
Isoform 2 (identifier: Q15645-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     171-406: Missing.

Note: No experimental confirmation available.
Show »
Length:196
Mass (Da):22,084
Checksum:i74AF9425508B518A
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei171 – 406236Missing in isoform 2. 1 PublicationVSP_016957Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3858.1. [Q15645-1]
RefSeqiNP_004228.1. NM_004237.3. [Q15645-1]
UniGeneiHs.436187.

Genome annotation databases

EnsembliENST00000166345; ENSP00000166345; ENSG00000071539. [Q15645-1]
GeneIDi9319.
KEGGihsa:9319.
UCSCiuc003jbr.3. human. [Q15645-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3858.1. [Q15645-1]
RefSeqiNP_004228.1. NM_004237.3. [Q15645-1]
UniGeneiHs.436187.

3D structure databases

ProteinModelPortaliQ15645.
SMRiQ15645. Positions 71-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114730. 104 interactions.
DIPiDIP-34493N.
IntActiQ15645. 78 interactions.
MINTiMINT-1146352.
STRINGi9606.ENSP00000166345.

PTM databases

PhosphoSiteiQ15645.

Polymorphism and mutation databases

BioMutaiTRIP13.
DMDMi85541056.

Proteomic databases

MaxQBiQ15645.
PaxDbiQ15645.
PeptideAtlasiQ15645.
PRIDEiQ15645.

Protocols and materials databases

DNASUi9319.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000166345; ENSP00000166345; ENSG00000071539. [Q15645-1]
GeneIDi9319.
KEGGihsa:9319.
UCSCiuc003jbr.3. human. [Q15645-1]

Organism-specific databases

CTDi9319.
GeneCardsiGC05P000892.
HGNCiHGNC:12307. TRIP13.
HPAiHPA005727.
HPA053093.
MIMi604507. gene.
neXtProtiNX_Q15645.
PharmGKBiPA36986.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00390000017432.
HOGENOMiHOG000234557.
HOVERGENiHBG052830.
InParanoidiQ15645.
OMAiVQIHVEV.
OrthoDBiEOG71VST9.
PhylomeDBiQ15645.
TreeFamiTF313507.

Miscellaneous databases

GeneWikiiTRIP13.
GenomeRNAii9319.
NextBioi34909.
PROiQ15645.
SOURCEiSearch...

Gene expression databases

BgeeiQ15645.
CleanExiHS_TRIP13.
ExpressionAtlasiQ15645. baseline and differential.
GenevisibleiQ15645. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR001270. ClpA/B.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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].

Entry informationi

Entry nameiPCH2_HUMAN
AccessioniPrimary (citable) accession number: Q15645
Secondary accession number(s): C9K0T3, D3DTC0, O15324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 10, 2006
Last modified: June 24, 2015
This is version 128 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

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. 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.