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Pachytene checkpoint protein 2 homolog (Human papillomavirus type 16 E1 protein-binding protein) (16E1-BP) (HPV16 E1 protein-binding protein) (Thyroid hormone receptor interactor 13) (Thyroid receptor-interacting protein 13) (TR-interacting protein 13) (TRIP-13)

 PCH2_HUMAN              Reviewed;         432 AA.
Q15645; C9K0T3; D3DTC0; O15324;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
30-AUG-2017, entry version 149.
RecName: Full=Pachytene checkpoint protein 2 homolog;
AltName: Full=Human papillomavirus type 16 E1 protein-binding protein;
Short=16E1-BP;
Short=HPV16 E1 protein-binding protein;
AltName: Full=Thyroid hormone receptor interactor 13;
AltName: Full=Thyroid receptor-interacting protein 13;
Short=TR-interacting protein 13;
Short=TRIP-13;
Name=TRIP13; Synonyms=PCH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HPV16 E1.
PubMed=9223484;
Yasugi T., Vidal M., Sakai H., Howley P.M., Benson J.D.;
"Two classes of human papillomavirus type 16 E1 mutants suggest
pleiotropic conformational constraints affecting E1 multimerization,
E2 interaction, and interaction with cellular proteins.";
J. Virol. 71:5942-5951(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-417 (ISOFORM 2), AND INTERACTION WITH
THRA.
PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
"Two classes of proteins dependent on either the presence or absence
of thyroid hormone for interaction with the thyroid hormone
receptor.";
Mol. Endocrinol. 9:243-254(1995).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- 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). {ECO:0000250}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:7776974,
ECO:0000269|PubMed:9223484}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-358993, EBI-358993;
Q96EJ4:-; NbExp=3; IntAct=EBI-358993, EBI-750454;
Q9Y303:AMDHD2; NbExp=3; IntAct=EBI-358993, EBI-2798672;
Q969Q4:ARL11; NbExp=3; IntAct=EBI-358993, EBI-751892;
P15289:ARSA; NbExp=9; IntAct=EBI-358993, EBI-2117357;
Q9H0W9:C11orf54; NbExp=3; IntAct=EBI-358993, EBI-740204;
Q8N1A6:C4orf33; NbExp=5; IntAct=EBI-358993, EBI-10264911;
P21964:COMT; NbExp=3; IntAct=EBI-358993, EBI-372265;
P21964-2:COMT; NbExp=3; IntAct=EBI-358993, EBI-10200977;
P53672:CRYBA2; NbExp=4; IntAct=EBI-358993, EBI-750444;
Q6BCY4:CYB5R2; NbExp=4; IntAct=EBI-358993, EBI-744761;
O95865:DDAH2; NbExp=5; IntAct=EBI-358993, EBI-749139;
Q14689:DIP2A; NbExp=3; IntAct=EBI-358993, EBI-2564275;
Q14689-6:DIP2A; NbExp=3; IntAct=EBI-358993, EBI-10233719;
O14531:DPYSL4; NbExp=3; IntAct=EBI-358993, EBI-719542;
Q96A09:FAM46B; NbExp=4; IntAct=EBI-358993, EBI-752030;
Q9UBX5:FBLN5; NbExp=3; IntAct=EBI-358993, EBI-947897;
Q53EP0-3:FNDC3B; NbExp=7; IntAct=EBI-358993, EBI-10242151;
Q8IVS8:GLYCTK; NbExp=8; IntAct=EBI-358993, EBI-748515;
Q9BSH5:HDHD3; NbExp=7; IntAct=EBI-358993, EBI-745201;
P59990:KRTAP12-1; NbExp=5; IntAct=EBI-358993, EBI-10210845;
P59991:KRTAP12-2; NbExp=3; IntAct=EBI-358993, EBI-10176379;
Q6PEX3:KRTAP26-1; NbExp=3; IntAct=EBI-358993, EBI-3957672;
Q16773:KYAT1; NbExp=3; IntAct=EBI-358993, EBI-10238309;
Q14847:LASP1; NbExp=7; IntAct=EBI-358993, EBI-742828;
Q8TBB1:LNX1; NbExp=6; IntAct=EBI-358993, EBI-739832;
Q96JB6:LOXL4; NbExp=6; IntAct=EBI-358993, EBI-749562;
Q96L50:LRR1; NbExp=3; IntAct=EBI-358993, EBI-2510106;
Q8TC57:M1AP; NbExp=3; IntAct=EBI-358993, EBI-748182;
Q15013:MAD2L1BP; NbExp=7; IntAct=EBI-358993, EBI-712181;
A6NJ78-4:METTL15; NbExp=5; IntAct=EBI-358993, EBI-10174029;
Q6PF18:MORN3; NbExp=3; IntAct=EBI-358993, EBI-9675802;
Q15777:MPPED2; NbExp=7; IntAct=EBI-358993, EBI-2350461;
Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-358993, EBI-740897;
O00746:NME4; NbExp=3; IntAct=EBI-358993, EBI-744871;
P55771:PAX9; NbExp=4; IntAct=EBI-358993, EBI-12111000;
P30039:PBLD; NbExp=4; IntAct=EBI-358993, EBI-750589;
Q6PIM4:PCMTD2; NbExp=3; IntAct=EBI-358993, EBI-10253759;
Q96FA3:PELI1; NbExp=3; IntAct=EBI-358993, EBI-448369;
Q9NRY6:PLSCR3; NbExp=6; IntAct=EBI-358993, EBI-750734;
Q9NRQ2:PLSCR4; NbExp=3; IntAct=EBI-358993, EBI-769257;
P67775:PPP2CA; NbExp=5; IntAct=EBI-358993, EBI-712311;
O60260:PRKN; NbExp=3; IntAct=EBI-358993, EBI-716346;
P47897:QARS; NbExp=5; IntAct=EBI-358993, EBI-347462;
P47897-2:QARS; NbExp=3; IntAct=EBI-358993, EBI-10209725;
Q9BQY4:RHOXF2; NbExp=7; IntAct=EBI-358993, EBI-372094;
P22307:SCP2; NbExp=4; IntAct=EBI-358993, EBI-1050999;
Q13228:SELENBP1; NbExp=3; IntAct=EBI-358993, EBI-711619;
Q9NTN9:SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-6447340;
Q9NTN9-3:SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-9089805;
O15389:SIGLEC5; NbExp=4; IntAct=EBI-358993, EBI-750381;
Q5W111:SPRYD7; NbExp=3; IntAct=EBI-358993, EBI-10248098;
Q96LM6:TEX37; NbExp=6; IntAct=EBI-358993, EBI-743976;
Q9GZM7:TINAGL1; NbExp=5; IntAct=EBI-358993, EBI-715869;
Q9GZM7-3:TINAGL1; NbExp=3; IntAct=EBI-358993, EBI-10303636;
Q6P9B6:TLDC1; NbExp=3; IntAct=EBI-358993, EBI-746504;
Q8NDV7:TNRC6A; NbExp=3; IntAct=EBI-358993, EBI-2269715;
P13693:TPT1; NbExp=3; IntAct=EBI-358993, EBI-1783169;
P11473:VDR; NbExp=3; IntAct=EBI-358993, EBI-286357;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-358993, EBI-741158;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15645-1; Sequence=Displayed;
Name=2;
IsoId=Q15645-2; Sequence=VSP_016957;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC41732.1; Type=Frameshift; Positions=1, 5; Evidence={ECO:0000305};
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EMBL; U96131; AAB64095.1; -; mRNA.
EMBL; CR456744; CAG33025.1; -; mRNA.
EMBL; AC122719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471102; EAX08185.1; -; Genomic_DNA.
EMBL; CH471102; EAX08186.1; -; Genomic_DNA.
EMBL; BC000404; AAH00404.1; -; mRNA.
EMBL; BC019294; AAH19294.1; -; mRNA.
EMBL; L40384; AAC41732.1; ALT_FRAME; mRNA.
CCDS; CCDS3858.1; -. [Q15645-1]
RefSeq; NP_004228.1; NM_004237.3. [Q15645-1]
RefSeq; XP_011512465.1; XM_011514163.2. [Q15645-1]
UniGene; Hs.436187; -.
PDB; 5VQ9; X-ray; 3.02 A; D=1-432.
PDB; 5VQA; X-ray; 2.54 A; A=1-432.
PDBsum; 5VQ9; -.
PDBsum; 5VQA; -.
ProteinModelPortal; Q15645; -.
BioGrid; 114730; 125.
DIP; DIP-34493N; -.
IntAct; Q15645; 117.
MINT; MINT-1146352; -.
STRING; 9606.ENSP00000166345; -.
iPTMnet; Q15645; -.
PhosphoSitePlus; Q15645; -.
SwissPalm; Q15645; -.
BioMuta; TRIP13; -.
DMDM; 85541056; -.
EPD; Q15645; -.
MaxQB; Q15645; -.
PaxDb; Q15645; -.
PeptideAtlas; Q15645; -.
PRIDE; Q15645; -.
DNASU; 9319; -.
Ensembl; ENST00000166345; ENSP00000166345; ENSG00000071539. [Q15645-1]
GeneID; 9319; -.
KEGG; hsa:9319; -.
UCSC; uc003jbr.4; human. [Q15645-1]
CTD; 9319; -.
DisGeNET; 9319; -.
GeneCards; TRIP13; -.
HGNC; HGNC:12307; TRIP13.
HPA; HPA005727; -.
HPA; HPA053093; -.
MIM; 604507; gene.
neXtProt; NX_Q15645; -.
OpenTargets; ENSG00000071539; -.
PharmGKB; PA36986; -.
eggNOG; KOG0744; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00390000017432; -.
HOGENOM; HOG000234557; -.
HOVERGEN; HBG052830; -.
InParanoid; Q15645; -.
OMA; WENLIYD; -.
OrthoDB; EOG091G0D83; -.
PhylomeDB; Q15645; -.
TreeFam; TF313507; -.
GeneWiki; TRIP13; -.
GenomeRNAi; 9319; -.
PRO; PR:Q15645; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000071539; -.
CleanEx; HS_TRIP13; -.
ExpressionAtlas; Q15645; baseline and differential.
Genevisible; Q15645; HS.
GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR001270; ClpA/B.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 1.
PRINTS; PR00300; CLPPROTEASEA.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Differentiation; Meiosis; Nucleotide-binding;
Oogenesis; Reference proteome; Spermatogenesis.
CHAIN 1 432 Pachytene checkpoint protein 2 homolog.
/FTId=PRO_0000084782.
NP_BIND 179 186 ATP. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
VAR_SEQ 171 406 Missing (in isoform 2).
{ECO:0000303|PubMed:7776974}.
/FTId=VSP_016957.
SEQUENCE 432 AA; 48551 MW; DFB0B37462D1D581 CRC64;
MDEAVGDLKQ ALPCVAESPT VHVEVHQRGS STAKKEDINL SVRKLLNRHN IVFGDYTWTE
FDEPFLTRNV QSVSIIDTEL KVKDSQPIDL SACTVALHIF QLNEDGPSSE NLEEETENII
AANHWVLPAA EFHGLWDSLV YDVEVKSHLL DYVMTTLLFS DKNVNSNLIT WNRVVLLHGP
PGTGKTSLCK ALAQKLTIRL SSRYRYGQLI EINSHSLFSK WFSESGKLVT KMFQKIQDLI
DDKDALVFVL IDEVESLTAA RNACRAGTEP SDAIRVVNAV LTQIDQIKRH SNVVILTTSN
ITEKIDVAFV DRADIKQYIG PPSAAAIFKI YLSCLEELMK CQIIYPRQQL LTLRELEMIG
FIENNVSKLS LLLNDISRKS EGLSGRVLRK LPFLAHALYV QAPTVTIEGF LQALSLAVDK
QFEERKKLAA YI


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Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
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GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


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81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

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GENTAUR Italy
SRL IVA IT03841300167
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Fax 02 36 00 65 94
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