ID   HOP2_HUMAN              Reviewed;         217 AA.
AC   Q9P2W1; C5ILB7; Q14458; Q8WXG2; Q96HA2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Homologous-pairing protein 2 homolog;
DE   AltName: Full=Nuclear receptor coactivator GT198;
DE   AltName: Full=PSMC3-interacting protein;
DE   AltName: Full=Proteasome 26S ATPase subunit 3-interacting protein;
DE   AltName: Full=Tat-binding protein 1-interacting protein;
DE            Short=TBP-1-interacting protein;
GN   Name=PSMC3IP; Synonyms=HOP2, TBPIP;
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 TISSUE SPECIFICITY.
RX   PubMed=7490091; DOI=10.1006/geno.1995.1185;
RA   Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T.,
RA   Samson C., Ferri L., Narod S., Morgan K., Simard J.;
RT   "Generation of a transcription map at the HSD17B locus centromeric to BRCA1
RT   at 17q21.";
RL   Genomics 28:530-542(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP   PSMC3.
RX   PubMed=10806355; DOI=10.1016/s0378-1119(00)00141-4;
RA   Ijichi H., Tanaka T., Nakamura T., Yagi H., Hakuba A., Sato M.;
RT   "Molecular cloning and characterization of a human homologue of TBPIP, a
RT   BRCA1 locus-related gene.";
RL   Gene 248:99-107(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RA   Peng M., Ko L.;
RT   "Alternative splicing of GT198 in the BRCA1 locus.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11739747; DOI=10.1128/mcb.22.1.357-369.2002;
RA   Ko L., Cardona G.R., Henrion-Caude A., Chin W.W.;
RT   "Identification and characterization of a tissue-specific coactivator,
RT   GT198, that interacts with the DNA-binding domains of nuclear receptors.";
RL   Mol. Cell. Biol. 22:357-369(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
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   [7]
RP   INTERACTION WITH MND1, AND FUNCTION.
RX   PubMed=16407260; DOI=10.1074/jbc.m506506200;
RA   Enomoto R., Kinebuchi T., Sato M., Yagi H., Kurumizaka H., Yokoyama S.;
RT   "Stimulation of DNA strand exchange by the human TBPIP/Hop2-Mnd1 complex.";
RL   J. Biol. Chem. 281:5575-5581(2006).
RN   [8]
RP   INDUCTION.
RX   PubMed=17716379; DOI=10.1186/1477-7827-5-34;
RA   Pan Q., Luo X., Chegini N.;
RT   "Genomic and proteomic profiling I: leiomyomas in African Americans and
RT   Caucasians.";
RL   Reprod. Biol. Endocrinol. 5:34-34(2007).
RN   [9]
RP   FUNCTION, VARIANT ODG3 GLU-201 DEL, AND CHARACTERIZATION OF VARIANT ODG3
RP   GLU-201 DEL.
RX   PubMed=21963259; DOI=10.1016/j.ajhg.2011.09.006;
RA   Zangen D., Kaufman Y., Zeligson S., Perlberg S., Fridman H., Kanaan M.,
RA   Abdulhadi-Atwan M., Abu Libdeh A., Gussow A., Kisslov I., Carmel L.,
RA   Renbaum P., Levy-Lahad E.;
RT   "XX ovarian dysgenesis is caused by a PSMC3IP/HOP2 mutation that abolishes
RT   coactivation of estrogen-driven transcription.";
RL   Am. J. Hum. Genet. 89:572-579(2011).
RN   [10]
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).
CC   -!- FUNCTION: Plays an important role in meiotic recombination. Stimulates
CC       DMC1-mediated strand exchange required for pairing homologous
CC       chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA,
CC       stimulates the recombinase activity of DMC1 as well as DMC1 D-loop
CC       formation from double-strand DNA. This complex stabilizes presynaptic
CC       RAD51 and DMC1 filaments formed on single strand DNA to capture double-
CC       strand DNA. This complex stimulates both synaptic and presynaptic
CC       critical steps in RAD51 and DMC1-promoted homologous pairing. May
CC       inhibit HIV-1 viral protein TAT activity and modulate the activity of
CC       proteasomes through association with PSMC3. Acts as a tissue specific
CC       coactivator of hormone-dependent transcription mediated by nuclear
CC       receptors. {ECO:0000269|PubMed:10806355, ECO:0000269|PubMed:16407260,
CC       ECO:0000269|PubMed:21963259}.
CC   -!- SUBUNIT: Interacts with the DNA-binding domain of the nuclear receptors
CC       NR3C1/GR, ESR2/ER-beta, THRB and RXRA (By similarity). Forms a stable
CC       heterodimer with MND1. Interacts with PSMC3/TBP1. {ECO:0000250,
CC       ECO:0000269|PubMed:10806355, ECO:0000269|PubMed:16407260}.
CC   -!- INTERACTION:
CC       Q9P2W1; Q9BWT6: MND1; NbExp=5; IntAct=EBI-9057595, EBI-11137441;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739747}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9P2W1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P2W1-2; Sequence=VSP_030213;
CC       Name=3;
CC         IsoId=Q9P2W1-3; Sequence=VSP_047716;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis and colon.
CC       {ECO:0000269|PubMed:11739747, ECO:0000269|PubMed:7490091}.
CC   -!- INDUCTION: Overexpressed in leiomyomas compared to myometrium.
CC       {ECO:0000269|PubMed:17716379}.
CC   -!- PTM: PTM: Phosphorylated by PKA, PKC and MAPK. {ECO:0000250}.
CC   -!- DISEASE: Ovarian dysgenesis 3 (ODG3) [MIM:614324]: A disorder
CC       characterized by lack of spontaneous pubertal development, primary
CC       amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism as a
CC       result of streak gonads. {ECO:0000269|PubMed:21963259}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the HOP2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC41915.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L38933; AAC41915.1; ALT_FRAME; mRNA.
DR   EMBL; AB030304; BAA92872.1; -; mRNA.
DR   EMBL; AF440240; AAL33609.1; -; mRNA.
DR   EMBL; FJ952180; ACR46655.1; -; mRNA.
DR   EMBL; FJ952181; ACR46656.1; -; mRNA.
DR   EMBL; FJ952182; ACR46657.1; -; mRNA.
DR   EMBL; FJ952183; ACR46658.1; -; mRNA.
DR   EMBL; GQ851964; ACX30903.1; -; mRNA.
DR   EMBL; GQ851965; ACX30904.1; -; mRNA.
DR   EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC008792; AAH08792.1; -; mRNA.
DR   CCDS; CCDS11431.1; -. [Q9P2W1-2]
DR   CCDS; CCDS45688.1; -. [Q9P2W1-1]
DR   PIR; I68521; I68521.
DR   RefSeq; NP_001242943.1; NM_001256014.1.
DR   RefSeq; NP_001242944.1; NM_001256015.1.
DR   RefSeq; NP_001242945.1; NM_001256016.1.
DR   RefSeq; NP_037422.2; NM_013290.6. [Q9P2W1-2]
DR   RefSeq; NP_057640.1; NM_016556.3. [Q9P2W1-1]
DR   AlphaFoldDB; Q9P2W1; -.
DR   SMR; Q9P2W1; -.
DR   BioGRID; 118945; 42.
DR   ComplexPortal; CPX-6661; HOP2-MND1 recombination assembly factor complex.
DR   CORUM; Q9P2W1; -.
DR   IntAct; Q9P2W1; 16.
DR   MINT; Q9P2W1; -.
DR   STRING; 9606.ENSP00000377384; -.
DR   iPTMnet; Q9P2W1; -.
DR   PhosphoSitePlus; Q9P2W1; -.
DR   BioMuta; PSMC3IP; -.
DR   DMDM; 74719969; -.
DR   EPD; Q9P2W1; -.
DR   jPOST; Q9P2W1; -.
DR   MassIVE; Q9P2W1; -.
DR   MaxQB; Q9P2W1; -.
DR   PaxDb; 9606-ENSP00000377384; -.
DR   PeptideAtlas; Q9P2W1; -.
DR   ProteomicsDB; 83901; -. [Q9P2W1-1]
DR   ProteomicsDB; 83902; -. [Q9P2W1-2]
DR   Pumba; Q9P2W1; -.
DR   Antibodypedia; 29297; 89 antibodies from 22 providers.
DR   DNASU; 29893; -.
DR   Ensembl; ENST00000253789.9; ENSP00000253789.4; ENSG00000131470.15. [Q9P2W1-2]
DR   Ensembl; ENST00000393795.8; ENSP00000377384.2; ENSG00000131470.15. [Q9P2W1-1]
DR   Ensembl; ENST00000590760.5; ENSP00000466381.1; ENSG00000131470.15. [Q9P2W1-3]
DR   GeneID; 29893; -.
DR   KEGG; hsa:29893; -.
DR   MANE-Select; ENST00000393795.8; ENSP00000377384.2; NM_016556.4; NP_057640.1.
DR   UCSC; uc002iai.4; human. [Q9P2W1-1]
DR   AGR; HGNC:17928; -.
DR   CTD; 29893; -.
DR   DisGeNET; 29893; -.
DR   GeneCards; PSMC3IP; -.
DR   HGNC; HGNC:17928; PSMC3IP.
DR   HPA; ENSG00000131470; Tissue enhanced (testis).
DR   MalaCards; PSMC3IP; -.
DR   MIM; 608665; gene.
DR   MIM; 614324; phenotype.
DR   neXtProt; NX_Q9P2W1; -.
DR   OpenTargets; ENSG00000131470; -.
DR   Orphanet; 243; 46,XX gonadal dysgenesis.
DR   PharmGKB; PA143485584; -.
DR   VEuPathDB; HostDB:ENSG00000131470; -.
DR   eggNOG; KOG4603; Eukaryota.
DR   GeneTree; ENSGT00390000006890; -.
DR   HOGENOM; CLU_181023_0_0_1; -.
DR   InParanoid; Q9P2W1; -.
DR   OMA; QKYHREW; -.
DR   OrthoDB; 25380at2759; -.
DR   PhylomeDB; Q9P2W1; -.
DR   TreeFam; TF328666; -.
DR   PathwayCommons; Q9P2W1; -.
DR   Reactome; R-HSA-912446; Meiotic recombination.
DR   SignaLink; Q9P2W1; -.
DR   BioGRID-ORCS; 29893; 36 hits in 1161 CRISPR screens.
DR   ChiTaRS; PSMC3IP; human.
DR   GenomeRNAi; 29893; -.
DR   Pharos; Q9P2W1; Tbio.
DR   PRO; PR:Q9P2W1; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9P2W1; Protein.
DR   Bgee; ENSG00000131470; Expressed in tendon of biceps brachii and 190 other cell types or tissues.
DR   ExpressionAtlas; Q9P2W1; baseline and differential.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR   GO; GO:0120231; C:DNA recombinase auxiliary factor complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:UniProtKB.
DR   GO; GO:0120230; F:recombinase activator activity; IBA:GO_Central.
DR   GO; GO:0007129; P:homologous chromosome pairing at meiosis; IDA:ComplexPortal.
DR   GO; GO:0000709; P:meiotic joint molecule formation; IBA:GO_Central.
DR   GO; GO:0010774; P:meiotic strand invasion involved in reciprocal meiotic recombination; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IDA:ComplexPortal.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR010776; Hop2_WH_dom.
DR   InterPro; IPR040661; LZ3wCH.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR15938:SF0; HOMOLOGOUS-PAIRING PROTEIN 2 HOMOLOG; 1.
DR   PANTHER; PTHR15938; TBP-1 INTERACTING PROTEIN; 1.
DR   Pfam; PF18517; LZ3wCH; 1.
DR   Pfam; PF07106; TBPIP; 1.
DR   Genevisible; Q9P2W1; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disease variant; DNA recombination;
KW   DNA-binding; Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..217
FT                   /note="Homologous-pairing protein 2 homolog"
FT                   /id="PRO_0000314135"
FT   REGION          118..182
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   COILED          93..153
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..125
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_047716"
FT   VAR_SEQ         113..124
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030213"
FT   VARIANT         163
FT                   /note="Y -> N (in dbSNP:rs2292754)"
FT                   /id="VAR_037841"
FT   VARIANT         201
FT                   /note="Missing (in ODG3; impairs function as estrogen
FT                   receptor coactivator)"
FT                   /evidence="ECO:0000269|PubMed:21963259"
FT                   /id="VAR_066636"
FT   CONFLICT        8
FT                   /note="Missing (in Ref. 1; AAC41915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="S -> T (in Ref. 1; AAC41915 and 5; AAL33609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="S -> L (in Ref. 5; AAL33609)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   217 AA;  24906 MW;  892B7D20CAA0A121 CRC64;
     MSKGRAEAAA GAAGILLRYL QEQNRPYSSQ DVFGNLQREH GLGKAVVVKT LEQLAQQGKI
     KEKMYGKQKI YFADQDQFDM VSDADLQVLD GKIVALTAKV QSLQQSCRYM EAELKELSSA
     LTTPEMQKEI QELKKECAGY RERLKNIKAA TNHVTPEEKE QVYRERQKYC KEWRKRKRMA
     TELSDAILEG YPKSKKQFFE EVGIETDEDY NVTLPDP
//