PCH2_HUMAN
ID PCH2_HUMAN Reviewed; 432 AA.
AC Q15645; C9K0T3; D3DTC0; O15324;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Pachytene checkpoint protein 2 homolog;
DE AltName: Full=Human papillomavirus type 16 E1 protein-binding protein;
DE Short=16E1-BP;
DE Short=HPV16 E1 protein-binding protein;
DE AltName: Full=Thyroid hormone receptor interactor 13;
DE AltName: Full=Thyroid receptor-interacting protein 13;
DE Short=TR-interacting protein 13;
DE Short=TRIP-13;
GN Name=TRIP13; Synonyms=PCH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HPV16 E1.
RX PubMed=9223484; DOI=10.1128/jvi.71.8.5942-5951.1997;
RA Yasugi T., Vidal M., Sakai H., Howley P.M., Benson J.D.;
RT "Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic
RT conformational constraints affecting E1 multimerization, E2 interaction,
RT and interaction with cellular proteins.";
RL J. Virol. 71:5942-5951(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-417 (ISOFORM 2), AND INTERACTION WITH THRA.
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP VARIANT MVA3 354-ARG--ILE-432 DEL, CHARACTERIZATION OF VARIANT MVA3
RP 354-ARG--ILE-432 DEL, AND FUNCTION.
RX PubMed=28553959; DOI=10.1038/ng.3883;
RA Yost S., de Wolf B., Hanks S., Zachariou A., Marcozzi C., Clarke M.,
RA de Voer R., Etemad B., Uijttewaal E., Ramsay E., Wylie H., Elliott A.,
RA Picton S., Smith A., Smithson S., Seal S., Ruark E., Houge G., Pines J.,
RA Kops G.J.P.L., Rahman N.;
RT "Biallelic TRIP13 mutations predispose to Wilms tumor and chromosome
RT missegregation.";
RL Nat. Genet. 49:1148-1151(2017).
RN [14]
RP VARIANTS OOMD9 ARG-26; GLN-173; VAL-198; MET-247 AND LYS-303,
RP CHARACTERIZATION OF VARIANT OOMD9 ARG-26, AND INVOLVEMENT IN OOMD9.
RX PubMed=32473092; DOI=10.1016/j.ajhg.2020.05.001;
RA Zhang Z., Li B., Fu J., Li R., Diao F., Li C., Chen B., Du J., Zhou Z.,
RA Mu J., Yan Z., Wu L., Liu S., Wang W., Zhao L., Dong J., He L., Liang X.,
RA Kuang Y., Sun X., Sang Q., Wang L.;
RT "Bi-allelic missense pathogenic variants in TRIP13 cause female infertility
RT characterized by oocyte maturation arrest.";
RL Am. J. Hum. Genet. 107:15-23(2020).
CC -!- FUNCTION: Plays a key role in chromosome recombination and chromosome
CC structure development during meiosis. Required at early steps in
CC meiotic recombination that leads to non-crossovers pathways. Also
CC needed for efficient completion of homologous synapsis by influencing
CC crossover distribution along the chromosomes affecting both crossovers
CC and non-crossovers pathways. Also required for development of higher-
CC order chromosome structures and is needed for synaptonemal-complex
CC formation. In males, required for efficient synapsis of the sex
CC chromosomes and for sex body formation. Promotes early steps of the DNA
CC double-strand breaks (DSBs) repair process upstream of the assembly of
CC RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from
CC synapsed chromosomes (By similarity). Plays a role in mitotic spindle
CC assembly checkpoint (SAC) activation (PubMed:28553959).
CC {ECO:0000250|UniProtKB:Q3UA06, ECO:0000269|PubMed:28553959}.
CC -!- SUBUNIT: Specifically interacts with the ligand binding domain of the
CC thyroid receptor (TR). This interaction does not require the presence
CC of thyroid hormone for its interaction. Interacts with HPV16 E1.
CC Interacts with proteasome subunit PSMA8; to participate in meiosis
CC progression during spermatogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q3UA06, ECO:0000269|PubMed:7776974,
CC ECO:0000269|PubMed:9223484}.
CC -!- INTERACTION:
CC Q15645; Q9Y303: AMDHD2; NbExp=3; IntAct=EBI-358993, EBI-2798672;
CC Q15645; Q9Y303-2: AMDHD2; NbExp=3; IntAct=EBI-358993, EBI-12323557;
CC Q15645; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-358993, EBI-12102070;
CC Q15645; Q969Q4: ARL11; NbExp=4; IntAct=EBI-358993, EBI-751892;
CC Q15645; P15289: ARSA; NbExp=13; IntAct=EBI-358993, EBI-2117357;
CC Q15645; Q8WXK3-2: ASB13; NbExp=3; IntAct=EBI-358993, EBI-12015080;
CC Q15645; Q9H0W9: C11orf54; NbExp=3; IntAct=EBI-358993, EBI-740204;
CC Q15645; Q9H0W9-3: C11orf54; NbExp=3; IntAct=EBI-358993, EBI-12108466;
CC Q15645; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-358993, EBI-11976299;
CC Q15645; Q8N1A6: C4orf33; NbExp=7; IntAct=EBI-358993, EBI-10264911;
CC Q15645; Q9Y2V0: CDIN1; NbExp=3; IntAct=EBI-358993, EBI-1047601;
CC Q15645; Q9Y4F5-3: CEP170B; NbExp=3; IntAct=EBI-358993, EBI-12950757;
CC Q15645; A0A0S2Z515: CFP; NbExp=3; IntAct=EBI-358993, EBI-16434710;
CC Q15645; Q8N3C7: CLIP4; NbExp=3; IntAct=EBI-358993, EBI-5655540;
CC Q15645; P21964: COMT; NbExp=3; IntAct=EBI-358993, EBI-372265;
CC Q15645; P21964-2: COMT; NbExp=3; IntAct=EBI-358993, EBI-10200977;
CC Q15645; P53672: CRYBA2; NbExp=5; IntAct=EBI-358993, EBI-750444;
CC Q15645; Q6BCY4: CYB5R2; NbExp=4; IntAct=EBI-358993, EBI-744761;
CC Q15645; Q6BCY4-2: CYB5R2; NbExp=3; IntAct=EBI-358993, EBI-12102608;
CC Q15645; O75935-2: DCTN3; NbExp=3; IntAct=EBI-358993, EBI-12091947;
CC Q15645; O95865: DDAH2; NbExp=6; IntAct=EBI-358993, EBI-749139;
CC Q15645; Q14689: DIP2A; NbExp=3; IntAct=EBI-358993, EBI-2564275;
CC Q15645; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-358993, EBI-10233719;
CC Q15645; O14531: DPYSL4; NbExp=3; IntAct=EBI-358993, EBI-719542;
CC Q15645; Q96G04: EEF2KMT; NbExp=3; IntAct=EBI-358993, EBI-747840;
CC Q15645; Q9UBX5: FBLN5; NbExp=3; IntAct=EBI-358993, EBI-947897;
CC Q15645; A0A0S2Z576: FBXO8; NbExp=3; IntAct=EBI-358993, EBI-16434722;
CC Q15645; Q53EP0-3: FNDC3B; NbExp=6; IntAct=EBI-358993, EBI-10242151;
CC Q15645; A0A0S2Z4I0: GALT; NbExp=3; IntAct=EBI-358993, EBI-16434744;
CC Q15645; P07902: GALT; NbExp=4; IntAct=EBI-358993, EBI-750827;
CC Q15645; Q8IVS8: GLYCTK; NbExp=9; IntAct=EBI-358993, EBI-748515;
CC Q15645; Q9BSH5: HDHD3; NbExp=6; IntAct=EBI-358993, EBI-745201;
CC Q15645; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-358993, EBI-11955401;
CC Q15645; P14784: IL2RB; NbExp=3; IntAct=EBI-358993, EBI-2866779;
CC Q15645; Q0VD86: INCA1; NbExp=3; IntAct=EBI-358993, EBI-6509505;
CC Q15645; P59990: KRTAP12-1; NbExp=6; IntAct=EBI-358993, EBI-10210845;
CC Q15645; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-358993, EBI-10176379;
CC Q15645; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-358993, EBI-10176396;
CC Q15645; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-358993, EBI-3957672;
CC Q15645; Q3LI64: KRTAP6-1; NbExp=4; IntAct=EBI-358993, EBI-12111050;
CC Q15645; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-358993, EBI-11962084;
CC Q15645; Q16773: KYAT1; NbExp=3; IntAct=EBI-358993, EBI-10238309;
CC Q15645; Q14847: LASP1; NbExp=7; IntAct=EBI-358993, EBI-742828;
CC Q15645; Q14847-2: LASP1; NbExp=3; IntAct=EBI-358993, EBI-9088686;
CC Q15645; Q8TBB1: LNX1; NbExp=8; IntAct=EBI-358993, EBI-739832;
CC Q15645; Q96JB6: LOXL4; NbExp=6; IntAct=EBI-358993, EBI-749562;
CC Q15645; Q96L50: LRR1; NbExp=3; IntAct=EBI-358993, EBI-2510106;
CC Q15645; Q8TC57: M1AP; NbExp=3; IntAct=EBI-358993, EBI-748182;
CC Q15645; Q15013: MAD2L1BP; NbExp=9; IntAct=EBI-358993, EBI-712181;
CC Q15645; Q6P9B6: MEAK7; NbExp=4; IntAct=EBI-358993, EBI-746504;
CC Q15645; A6NJ78-4: METTL15; NbExp=6; IntAct=EBI-358993, EBI-10174029;
CC Q15645; Q6PF18: MORN3; NbExp=3; IntAct=EBI-358993, EBI-9675802;
CC Q15645; Q15777: MPPED2; NbExp=8; IntAct=EBI-358993, EBI-2350461;
CC Q15645; Q96EZ4: MYEOV; NbExp=3; IntAct=EBI-358993, EBI-12260130;
CC Q15645; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-358993, EBI-740897;
CC Q15645; O00746: NME4; NbExp=4; IntAct=EBI-358993, EBI-744871;
CC Q15645; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-358993, EBI-741158;
CC Q15645; P55771: PAX9; NbExp=3; IntAct=EBI-358993, EBI-12111000;
CC Q15645; P30039: PBLD; NbExp=4; IntAct=EBI-358993, EBI-750589;
CC Q15645; Q6PIM4: PCMTD2; NbExp=3; IntAct=EBI-358993, EBI-10253759;
CC Q15645; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-358993, EBI-11956269;
CC Q15645; Q96FA3: PELI1; NbExp=3; IntAct=EBI-358993, EBI-448369;
CC Q15645; Q9NRY6: PLSCR3; NbExp=7; IntAct=EBI-358993, EBI-750734;
CC Q15645; Q9NRQ2: PLSCR4; NbExp=5; IntAct=EBI-358993, EBI-769257;
CC Q15645; P62875: POLR2L; NbExp=3; IntAct=EBI-358993, EBI-359527;
CC Q15645; P67775: PPP2CA; NbExp=6; IntAct=EBI-358993, EBI-712311;
CC Q15645; P54646: PRKAA2; NbExp=3; IntAct=EBI-358993, EBI-1383852;
CC Q15645; O60260: PRKN; NbExp=4; IntAct=EBI-358993, EBI-716346;
CC Q15645; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-358993, EBI-740924;
CC Q15645; P28062-2: PSMB8; NbExp=3; IntAct=EBI-358993, EBI-372312;
CC Q15645; P47897: QARS1; NbExp=6; IntAct=EBI-358993, EBI-347462;
CC Q15645; P47897-2: QARS1; NbExp=3; IntAct=EBI-358993, EBI-10209725;
CC Q15645; Q9BQY4: RHOXF2; NbExp=8; IntAct=EBI-358993, EBI-372094;
CC Q15645; P78317: RNF4; NbExp=3; IntAct=EBI-358993, EBI-2340927;
CC Q15645; P22307: SCP2; NbExp=4; IntAct=EBI-358993, EBI-1050999;
CC Q15645; O00560: SDCBP; NbExp=3; IntAct=EBI-358993, EBI-727004;
CC Q15645; Q13228: SELENBP1; NbExp=6; IntAct=EBI-358993, EBI-711619;
CC Q15645; Q13214-2: SEMA3B; NbExp=3; IntAct=EBI-358993, EBI-11017428;
CC Q15645; Q9NTN9: SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-6447340;
CC Q15645; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-9089805;
CC Q15645; Q9H0F6-2: SHARPIN; NbExp=3; IntAct=EBI-358993, EBI-9843813;
CC Q15645; O15389: SIGLEC5; NbExp=4; IntAct=EBI-358993, EBI-750381;
CC Q15645; Q5W111: SPRYD7; NbExp=3; IntAct=EBI-358993, EBI-10248098;
CC Q15645; O95630: STAMBP; NbExp=4; IntAct=EBI-358993, EBI-396676;
CC Q15645; Q96A09: TENT5B; NbExp=3; IntAct=EBI-358993, EBI-752030;
CC Q15645; Q96LM6: TEX37; NbExp=7; IntAct=EBI-358993, EBI-743976;
CC Q15645; Q9GZM7: TINAGL1; NbExp=6; IntAct=EBI-358993, EBI-715869;
CC Q15645; Q9GZM7-3: TINAGL1; NbExp=3; IntAct=EBI-358993, EBI-10303636;
CC Q15645; Q8NDV7: TNRC6A; NbExp=3; IntAct=EBI-358993, EBI-2269715;
CC Q15645; P13693: TPT1; NbExp=3; IntAct=EBI-358993, EBI-1783169;
CC Q15645; Q15645: TRIP13; NbExp=8; IntAct=EBI-358993, EBI-358993;
CC Q15645; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-358993, EBI-10180829;
CC Q15645; P11473: VDR; NbExp=3; IntAct=EBI-358993, EBI-286357;
CC Q15645; O95231: VENTX; NbExp=3; IntAct=EBI-358993, EBI-10191303;
CC Q15645; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-358993, EBI-17634549;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15645-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15645-2; Sequence=VSP_016957;
CC -!- DISEASE: Mosaic variegated aneuploidy syndrome 3 (MVA3) [MIM:617598]: A
CC form of mosaic variegated aneuploidy syndrome, a severe disorder
CC characterized by mosaic aneuploidies, predominantly trisomies and
CC monosomies, involving multiple different chromosomes and tissues.
CC Affected individuals typically present with severe intrauterine growth
CC retardation and microcephaly. Eye anomalies, mild dysmorphism, variable
CC developmental delay, and a broad spectrum of additional congenital
CC abnormalities and medical conditions may also occur. The risk of
CC malignancy is high, with rhabdomyosarcoma, Wilms tumor and leukemia
CC reported in several cases. MVA3 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:28553959}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. MVA3 is caused by
CC biallelic mutations in the TRIP13 gene.
CC -!- DISEASE: Oocyte maturation defect 9 (OOMD9) [MIM:619011]: An autosomal
CC recessive infertility disorder due to oocyte meiotic arrest at
CC metaphase I. Abnormal zygotic cleavage has been observed in some
CC patients. {ECO:0000269|PubMed:32473092}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC41732.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U96131; AAB64095.1; -; mRNA.
DR EMBL; CR456744; CAG33025.1; -; mRNA.
DR EMBL; AC122719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471102; EAX08185.1; -; Genomic_DNA.
DR EMBL; CH471102; EAX08186.1; -; Genomic_DNA.
DR EMBL; BC000404; AAH00404.1; -; mRNA.
DR EMBL; BC019294; AAH19294.1; -; mRNA.
DR EMBL; L40384; AAC41732.1; ALT_FRAME; mRNA.
DR CCDS; CCDS3858.1; -. [Q15645-1]
DR RefSeq; NP_004228.1; NM_004237.3. [Q15645-1]
DR RefSeq; XP_011512465.1; XM_011514163.2. [Q15645-1]
DR PDB; 5VQ9; X-ray; 3.02 A; D=1-432.
DR PDB; 5VQA; X-ray; 2.54 A; A=1-432.
DR PDB; 5WC2; X-ray; 2.50 A; A=1-432.
DR PDB; 6F0X; EM; 4.60 A; A/B/C/D/E/F=1-432.
DR PDB; 6LK0; X-ray; 2.60 A; A=1-432.
DR PDB; 7L9P; EM; 3.60 A; A/B/C/D/E/F=2-432.
DR PDBsum; 5VQ9; -.
DR PDBsum; 5VQA; -.
DR PDBsum; 5WC2; -.
DR PDBsum; 6F0X; -.
DR PDBsum; 6LK0; -.
DR PDBsum; 7L9P; -.
DR AlphaFoldDB; Q15645; -.
DR SMR; Q15645; -.
DR BioGRID; 114730; 266.
DR DIP; DIP-34493N; -.
DR IntAct; Q15645; 152.
DR MINT; Q15645; -.
DR STRING; 9606.ENSP00000166345; -.
DR GlyGen; Q15645; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15645; -.
DR MetOSite; Q15645; -.
DR PhosphoSitePlus; Q15645; -.
DR SwissPalm; Q15645; -.
DR BioMuta; TRIP13; -.
DR DMDM; 85541056; -.
DR EPD; Q15645; -.
DR jPOST; Q15645; -.
DR MassIVE; Q15645; -.
DR MaxQB; Q15645; -.
DR PaxDb; Q15645; -.
DR PeptideAtlas; Q15645; -.
DR PRIDE; Q15645; -.
DR ProteomicsDB; 60681; -. [Q15645-1]
DR ProteomicsDB; 60682; -. [Q15645-2]
DR Antibodypedia; 8906; 335 antibodies from 33 providers.
DR DNASU; 9319; -.
DR Ensembl; ENST00000166345.8; ENSP00000166345.3; ENSG00000071539.14. [Q15645-1]
DR GeneID; 9319; -.
DR KEGG; hsa:9319; -.
DR MANE-Select; ENST00000166345.8; ENSP00000166345.3; NM_004237.4; NP_004228.1.
DR UCSC; uc003jbr.4; human. [Q15645-1]
DR CTD; 9319; -.
DR DisGeNET; 9319; -.
DR GeneCards; TRIP13; -.
DR HGNC; HGNC:12307; TRIP13.
DR HPA; ENSG00000071539; Tissue enhanced (testis).
DR MalaCards; TRIP13; -.
DR MIM; 604507; gene.
DR MIM; 617598; phenotype.
DR MIM; 619011; phenotype.
DR neXtProt; NX_Q15645; -.
DR OpenTargets; ENSG00000071539; -.
DR Orphanet; 1052; Mosaic variegated aneuploidy syndrome.
DR Orphanet; 654; Nephroblastoma.
DR PharmGKB; PA36986; -.
DR VEuPathDB; HostDB:ENSG00000071539; -.
DR eggNOG; KOG0744; Eukaryota.
DR GeneTree; ENSGT00390000017432; -.
DR HOGENOM; CLU_028208_0_1_1; -.
DR InParanoid; Q15645; -.
DR OMA; VQIHVEV; -.
DR OrthoDB; 1036414at2759; -.
DR PhylomeDB; Q15645; -.
DR TreeFam; TF313507; -.
DR PathwayCommons; Q15645; -.
DR SignaLink; Q15645; -.
DR SIGNOR; Q15645; -.
DR BioGRID-ORCS; 9319; 202 hits in 1090 CRISPR screens.
DR ChiTaRS; TRIP13; human.
DR GeneWiki; TRIP13; -.
DR GenomeRNAi; 9319; -.
DR Pharos; Q15645; Tbio.
DR PRO; PR:Q15645; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q15645; protein.
DR Bgee; ENSG00000071539; Expressed in bronchial epithelial cell and 139 other tissues.
DR ExpressionAtlas; Q15645; baseline and differential.
DR Genevisible; Q15645; HS.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003712; F:transcription coregulator activity; TAS:ProtInc.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044539; Pch2-like.
DR PANTHER; PTHR45991; PTHR45991; 1.
DR Pfam; PF00004; AAA; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Differentiation; Disease variant; Meiosis; Nucleotide-binding; Oogenesis;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..432
FT /note="Pachytene checkpoint protein 2 homolog"
FT /id="PRO_0000084782"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT VAR_SEQ 171..406
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7776974"
FT /id="VSP_016957"
FT VARIANT 26
FT /note="H -> R (in OOMD9; decreased protein level in patient
FT cells; dbSNP:rs780778324)"
FT /evidence="ECO:0000269|PubMed:32473092"
FT /id="VAR_084761"
FT VARIANT 173
FT /note="R -> Q (in OOMD9; unknown pathological significance;
FT dbSNP:rs759712974)"
FT /evidence="ECO:0000269|PubMed:32473092"
FT /id="VAR_084762"
FT VARIANT 198
FT /note="I -> V (in OOMD9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32473092"
FT /id="VAR_084763"
FT VARIANT 247
FT /note="V -> M (in OOMD9; unknown pathological significance;
FT dbSNP:rs1203102465)"
FT /evidence="ECO:0000269|PubMed:32473092"
FT /id="VAR_084764"
FT VARIANT 303
FT /note="E -> K (in OOMD9; unknown pathological significance;
FT dbSNP:rs772834014)"
FT /evidence="ECO:0000269|PubMed:32473092"
FT /id="VAR_084765"
FT VARIANT 354..432
FT /note="Missing (in MVA3; loss of protein expression;
FT impairment of spindle assembly checkpoint)"
FT /evidence="ECO:0000269|PubMed:28553959"
FT /id="VAR_079275"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5VQA"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:5WC2"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:5WC2"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:5WC2"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5VQA"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:5WC2"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 324..340
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:5WC2"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:5WC2"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:5WC2"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:5WC2"
FT HELIX 407..428
FT /evidence="ECO:0007829|PDB:5WC2"
SQ 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
