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Homologous-pairing protein 2 homolog (PSMC3-interacting protein) (Proteasome 26S ATPase subunit 3-interacting protein) (Tat-binding protein 1-interacting protein) (TBP-1-interacting protein)

 HOP2_MOUSE              Reviewed;         217 AA.
O35047; Q3V035;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
29-SEP-2021, entry version 133.
RecName: Full=Homologous-pairing protein 2 homolog;
AltName: Full=PSMC3-interacting protein;
AltName: Full=Proteasome 26S ATPase subunit 3-interacting protein;
AltName: Full=Tat-binding protein 1-interacting protein;
Short=TBP-1-interacting protein;
Name=Psmc3ip; Synonyms=Hop2, Tbpip;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PSMC3, TISSUE SPECIFICITY, AND
FUNCTION.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=9345291; DOI=10.1006/bbrc.1997.7447;
Tanaka T., Nakamura T., Takagi H., Sato M.;
"Molecular cloning and characterization of a novel TBP-1 interacting
protein (TBPIP): enhancement of TBP-1 action on Tat by TBPIP.";
Biochem. Biophys. Res. Commun. 239:176-181(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
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]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
PubMed=11739747; DOI=10.1128/mcb.22.1.357-369.2002;
Ko L., Cardona G.R., Henrion-Caude A., Chin W.W.;
"Identification and characterization of a tissue-specific coactivator,
GT198, that interacts with the DNA-binding domains of nuclear receptors.";
Mol. Cell. Biol. 22:357-369(2002).
[6]
DISRUPTION PHENOTYPE.
PubMed=14667414; DOI=10.1016/s1534-5807(03)00369-1;
Petukhova G.V., Romanienko P.J., Camerini-Otero R.D.;
"The Hop2 protein has a direct role in promoting interhomolog interactions
during mouse meiosis.";
Dev. Cell 5:927-936(2003).
[7]
FUNCTION, AND DNA-BINDING REGION.
PubMed=15192114; DOI=10.1074/jbc.m402481200;
Enomoto R., Kinebuchi T., Sato M., Yagi H., Shibata T., Kurumizaka H.,
Yokoyama S.;
"Positive role of the mammalian TBPIP/HOP2 protein in DMC1-mediated
homologous pairing.";
J. Biol. Chem. 279:35263-35272(2004).
[8]
FUNCTION, DNA-BINDING REGION, MUTAGENESIS OF GLU-136, AND INTERACTION WITH
MND1.
PubMed=16675459; DOI=10.1074/jbc.m601073200;
Pezza R.J., Petukhova G.V., Ghirlando R., Camerini-Otero R.D.;
"Molecular activities of meiosis-specific proteins Hop2, Mnd1, and the
Hop2-Mnd1 complex.";
J. Biol. Chem. 281:18426-18434(2006).
[9]
FUNCTION.
PubMed=17639080; DOI=10.1101/gad.1563007;
Chi P., San Filippo J., Sehorn M.G., Petukhova G.V., Sung P.;
"Bipartite stimulatory action of the Hop2-Mnd1 complex on the Rad51
recombinase.";
Genes Dev. 21:1747-1757(2007).
[10]
FUNCTION.
PubMed=17639081; DOI=10.1101/gad.1562907;
Pezza R.J., Voloshin O.N., Vanevski F., Camerini-Otero R.D.;
"Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous
pairing.";
Genes Dev. 21:1758-1766(2007).
[11]
FUNCTION.
PubMed=17426123; DOI=10.1093/nar/gkm174;
Ploquin M., Petukhova G.V., Morneau D., Dery U., Bransi A., Stasiak A.,
Camerini-Otero R.D., Masson J.-Y.;
"Stimulation of fission yeast and mouse Hop2-Mnd1 of the Dmc1 and Rad51
recombinases.";
Nucleic Acids Res. 35:2719-2733(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays an important role in meiotic recombination. Stimulates
DMC1-mediated strand exchange required for pairing homologous
chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA,
stimulates the recombinase activity of DMC1 as well as DMC1 D-loop
formation from double-strand DNA. This complex stabilizes presynaptic
RAD51 and DMC1 filaments formed on single strand DNA to capture double-
strand DNA. This complex stimulates both synaptic and presynaptic
critical steps in RAD51 and DMC1-promoted homologous pairing. May
inhibit HIV-1 viral protein TAT activity and modulate the activity of
proteasomes through association with PSMC3.
{ECO:0000269|PubMed:15192114, ECO:0000269|PubMed:16675459,
ECO:0000269|PubMed:17426123, ECO:0000269|PubMed:17639080,
ECO:0000269|PubMed:17639081, ECO:0000269|PubMed:9345291}.
-!- SUBUNIT: Interacts with the DNA-binding domain of the nuclear receptors
NR3C1/GR, ESR2/ER-beta, THRB and RXRA (By similarity). Forms a stable
heterodimer with MND1. Interacts with PSMC3/TBP1. {ECO:0000250,
ECO:0000269|PubMed:16675459, ECO:0000269|PubMed:9345291}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739747}.
-!- TISSUE SPECIFICITY: Highly expressed in testis and more specifically in
spermatocytes. Detected in spleen, ovary and thymus.
{ECO:0000269|PubMed:11739747, ECO:0000269|PubMed:9345291}.
-!- DEVELOPMENTAL STAGE: Overexpressed at day 11 in the embryo.
{ECO:0000269|PubMed:11739747}.
-!- PTM: Phosphorylated by PKA, PKC and MAPK. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Infertility. Males exhibit testicular hypoplasia
with lack of spermatozoa. Spermatocytes arrest at the stage of
pachytene-like chromosome condensation and spermatogenesis is blocked
at prophase of meiosis I. Axial elements are fully developed, but
synapsis is limited. While meiotic double-stranded breaks are formed
and processed, they fail to be repaired. {ECO:0000269|PubMed:14667414}.
-!- SIMILARITY: Belongs to the HOP2 family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AB000121; BAA23155.1; -; mRNA.
EMBL; AK133462; BAE21670.1; -; mRNA.
EMBL; BX255926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030169; AAH30169.1; -; mRNA.
CCDS; CCDS25448.1; -.
PIR; JC5710; JC5710.
RefSeq; NP_032975.1; NM_008949.3.
PDB; 2MH2; NMR; -; A=1-84.
PDBsum; 2MH2; -.
BMRB; O35047; -.
SMR; O35047; -.
BioGRID; 202429; 1.
CORUM; O35047; -.
STRING; 10090.ENSMUSP00000019447; -.
PhosphoSitePlus; O35047; -.
EPD; O35047; -.
MaxQB; O35047; -.
PaxDb; O35047; -.
PRIDE; O35047; -.
ProteomicsDB; 273379; -.
Antibodypedia; 29297; 70 antibodies.
DNASU; 19183; -.
Ensembl; ENSMUST00000019447; ENSMUSP00000019447; ENSMUSG00000019303.
GeneID; 19183; -.
KEGG; mmu:19183; -.
UCSC; uc007lnh.2; mouse.
CTD; 29893; -.
MGI; MGI:1098610; Psmc3ip.
VEuPathDB; HostDB:ENSMUSG00000019303; -.
eggNOG; KOG4603; Eukaryota.
GeneTree; ENSGT00390000006890; -.
HOGENOM; CLU_063266_1_0_1; -.
InParanoid; O35047; -.
OMA; IETDEDC; -.
OrthoDB; 1498024at2759; -.
PhylomeDB; O35047; -.
TreeFam; TF328666; -.
BioGRID-ORCS; 19183; 2 hits in 62 CRISPR screens.
ChiTaRS; Psmc3ip; mouse.
PRO; PR:O35047; -.
Proteomes; UP000000589; Chromosome 11.
RNAct; O35047; protein.
Bgee; ENSMUSG00000019303; Expressed in testis and 250 other tissues.
ExpressionAtlas; O35047; baseline and differential.
Genevisible; O35047; MM.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0050681; F:androgen receptor binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0050692; F:DNA binding domain binding; ISO:MGI.
GO; GO:0030331; F:estrogen receptor binding; ISO:MGI.
GO; GO:0035259; F:glucocorticoid receptor binding; ISO:MGI.
GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0046966; F:thyroid hormone receptor binding; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0007131; P:reciprocal meiotic recombination; IEA:InterPro.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR040461; Hop2.
InterPro; IPR010776; Hop2_WH_dom.
InterPro; IPR040661; LZ3wCH.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR15938; PTHR15938; 1.
Pfam; PF18517; LZ3wCH; 1.
Pfam; PF07106; TBPIP; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; DNA recombination; DNA-binding; Meiosis;
Nucleus; Reference proteome.
CHAIN 1..217
/note="Homologous-pairing protein 2 homolog"
/id="PRO_0000314136"
REGION 118..182
/note="DNA binding"
COILED 84..152
/evidence="ECO:0000255"
MUTAGEN 136
/note="E->P: Alters PSMC3/MND1 formation."
/evidence="ECO:0000269|PubMed:16675459"
CONFLICT 80
/note="T -> K (in Ref. 2; BAE21670)"
/evidence="ECO:0000305"
HELIX 12..23
/evidence="ECO:0007829|PDB:2MH2"
HELIX 29..37
/evidence="ECO:0007829|PDB:2MH2"
TURN 38..40
/evidence="ECO:0007829|PDB:2MH2"
HELIX 44..57
/evidence="ECO:0007829|PDB:2MH2"
STRAND 59..65
/evidence="ECO:0007829|PDB:2MH2"
STRAND 68..73
/evidence="ECO:0007829|PDB:2MH2"
SEQUENCE 217 AA; 24748 MW; 18E834492C2609EC CRC64;
MSKSRAEAAA GAPGIILRYL QEQNRPYSAQ DVFGNLQKEH GLGKAAVVKA LDQLAQEGKI
KEKTYGKQKI YFADQNQFDT VSDADLHGLD ASIVALTAKV QSLQQSCRHM EAELKELTSA
LTTPEMQKEI QELKKECAQY TERLKNIKAA TNHVTPEEKE KVYRDRQKYC KEWRKRKRMT
TELCDAILEG YPKSKKQFFE EVGIETDEDH NVLLPDP


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[RPT5 YTA1 YOR117W O3258 YOR3258W] 26S proteasome regulatory subunit 6A (Tat-binding protein homolog 1) (TBP-1)
[PSMC2 MSS1] 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1) (Proteasome 26S subunit ATPase 2) (Protein MSS1)
[RUVBL1 INO80H NMP238 TIP49 TIP49A] RuvB-like 1 (EC 3.6.4.12) (49 kDa TATA box-binding protein-interacting protein) (49 kDa TBP-interacting protein) (54 kDa erythrocyte cytosolic protein) (ECP-54) (INO80 complex subunit H) (Nuclear matrix protein 238) (NMP 238) (Pontin 52) (TIP49a) (TIP60-associated protein 54-alpha) (TAP54-alpha)
[PSMC6 SUG2] 26S proteasome regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4) (Proteasome 26S subunit ATPase 6) (Proteasome subunit p42)
[RPT3 YNT1 YTA2 YDR394W D9509.14] 26S proteasome regulatory subunit 6B homolog (Protein YNT1) (Tat-binding homolog 2)
[RUVBL2 INO80J TIP48 TIP49B CGI-46] RuvB-like 2 (EC 3.6.4.12) (48 kDa TATA box-binding protein-interacting protein) (48 kDa TBP-interacting protein) (51 kDa erythrocyte cytosolic protein) (ECP-51) (INO80 complex subunit J) (Repressing pontin 52) (Reptin 52) (TIP49b) (TIP60-associated protein 54-beta) (TAP54-beta)
[KAT5 HTATIP TIP60] Histone acetyltransferase KAT5 (EC 2.3.1.48) (60 kDa Tat-interactive protein) (Tip60) (Histone acetyltransferase HTATIP) (HIV-1 Tat interactive protein) (Lysine acetyltransferase 5) (cPLA(2)-interacting protein)
[RPT1 CIM5 YTA3 YKL145W] 26S proteasome regulatory subunit 7 homolog (Protein CIM5) (Tat-binding homolog 3)
[PSMD4 MCB1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)
[PSMC1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[PSMD1] 26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) (26S proteasome subunit p112)
[RPT2A HLR At4g29040 F19B15.70 F25O24.6] 26S proteasome regulatory subunit 4 homolog A (26S proteasome AAA-ATPase subunit RPT2a) (26S proteasome subunit 4 homolog A) (Protein HALTED ROOT) (Regulatory particle triple-A ATPase subunit 2a)
[RPN10 MBP1 MCB1 At4g38630 F20M13.190 T9A14.7] 26S proteasome non-ATPase regulatory subunit 4 homolog (26S proteasome regulatory subunit RPN10) (AtRPN10) (26S proteasome regulatory subunit S5A homolog) (Multiubiquitin chain-binding protein 1) (AtMCB1)
[BNIP3L BNIP3A BNIP3H NIX] BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like (Adenovirus E1B19K-binding protein B5) (BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A) (NIP3-like protein X) (NIP3L)
[Psmd4 Mcb1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Multiubiquitin chain-binding protein)
[UBQLN4 C1orf6 CIP75 UBIN] Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein) (A1Up) (Ataxin-1 ubiquitin-like-interacting protein A1U) (Connexin43-interacting protein of 75 kDa) (CIP75)
[TERF2IP DRIP5 RAP1 PP8000] Telomeric repeat-binding factor 2-interacting protein 1 (TERF2-interacting telomeric protein 1) (TRF2-interacting telomeric protein 1) (Dopamine receptor-interacting protein 5) (Repressor/activator protein 1 homolog) (RAP1 homolog) (hRap1)
[RPT2 YHS4 YTA5 YDL007W D2920] 26S proteasome regulatory subunit 4 homolog (Tat-binding homolog 5)
[RPT2B At2g20140 T2G17.6] 26S proteasome regulatory subunit 4 homolog B (26S proteasome AAA-ATPase subunit RPT2b) (26S proteasome subunit 4 homolog B) (Regulatory particle triple-A ATPase subunit 2b)
[Ubqln4 Cip75 Ubin] Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein) (A1Up) (Ataxin-1 ubiquitin-like-interacting protein A1U) (Connexin43-interacting protein of 75 kDa) (CIP75)

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