PRM2_HUMAN
ID PRM2_HUMAN Reviewed; 102 AA.
AC P04554; Q6ZMM0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protamine-2;
DE AltName: Full=Sperm histone P2;
DE AltName: Full=Sperm protamine P2;
DE Contains:
DE RecName: Full=Basic nuclear protein HPI1;
DE Contains:
DE RecName: Full=Basic nuclear protein HPI2;
DE Contains:
DE RecName: Full=Basic nuclear protein HPS1;
DE Contains:
DE RecName: Full=Basic nuclear protein HPS2;
DE Contains:
DE RecName: Full=Sperm histone HP4;
DE AltName: Full=Sperm protamine P4;
DE Contains:
DE RecName: Full=Sperm histone HP2;
DE AltName: Full=Sperm protamine P2;
DE Short=P2';
DE Contains:
DE RecName: Full=Sperm histone HP3;
DE AltName: Full=P2'';
DE AltName: Full=Sperm protamine P3;
GN Name=PRM2;
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).
RC TISSUE=Testis;
RX PubMed=3412906; DOI=10.1093/nar/16.15.7733;
RA Domenjoud L., Fronia C., Uhde F., Engel W.;
RT "Sequence of human protamine 2 cDNA.";
RL Nucleic Acids Res. 16:7733-7733(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2081589; DOI=10.1016/0888-7543(90)90234-l;
RA Domenjoud L., Nussbaum G., Adham I.M., Greeske G., Engel W.;
RT "Genomic sequences of human protamines whose genes, PRM1 and PRM2, are
RT clustered.";
RL Genomics 8:127-133(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7983046; DOI=10.1016/s0021-9258(18)47391-7;
RA Nelson J.E., Krawetz S.A.;
RT "Characterization of a human locus in transition.";
RL J. Biol. Chem. 269:31067-31073(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10659848; DOI=10.1038/35002070;
RA Wyckoff G.J., Wang W., Wu C.-I.;
RT "Rapid evolution of male reproductive genes in the descent of man.";
RL Nature 403:304-309(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [8]
RP PROTEIN SEQUENCE OF 2-102 (HPI1).
RC TISSUE=Sperm;
RX PubMed=2384091; DOI=10.1111/j.1432-1033.1990.tb19142.x;
RA Martinage A., Arkhis A., Alimi E., Sautiere P., Chevaillier P.;
RT "Molecular characterization of nuclear basic protein HPI1, a putative
RT precursor of human sperm protamines HP2 and HP3.";
RL Eur. J. Biochem. 191:449-451(1990).
RN [9]
RP PROTEIN SEQUENCE OF 22-102 (HPI2).
RX PubMed=8513794; DOI=10.1111/j.1432-1033.1993.tb17940.x;
RA Alimi E., Martinage A., Arkhis A., Belaiche D., Sautiere P.,
RA Chevaillier P.;
RT "Amino acid sequence of the human intermediate basic protein 2 (HPI2) from
RT sperm nuclei. Structural relationship with protamine P2.";
RL Eur. J. Biochem. 214:445-450(1993).
RN [10]
RP PROTEIN SEQUENCE OF 34-102 (HPS1 AND HPS2).
RC TISSUE=Sperm;
RX PubMed=3403514; DOI=10.1016/s0021-9258(18)37919-5;
RA Sautiere P., Martinage A., Belaiche D., Arkhis A., Chevaillier P.;
RT "Comparison of the amino acid sequences of human protamines HP2 and HP3 and
RT of intermediate basic nuclear proteins HPS1 and HPS2. Structural evidence
RT that HPS1 and HPS2 are pro-protamines.";
RL J. Biol. Chem. 263:11059-11063(1988).
RN [11]
RP PROTEIN SEQUENCE OF 46-102 (HP2 AND HP3).
RC TISSUE=Sperm;
RX PubMed=3527226; DOI=10.1515/bchm3.1986.367.1.515;
RA Ammer H., Henschen A., Lee C.-H.;
RT "Isolation and amino-acid sequence analysis of human sperm protamines P1
RT and P2. Occurrence of two forms of protamine P2.";
RL Biol. Chem. Hoppe-Seyler 367:515-522(1986).
RN [12]
RP PROTEIN SEQUENCE OF 46-102 (P2B).
RC TISSUE=Sperm;
RX PubMed=3956509; DOI=10.1111/j.1432-1033.1986.tb09540.x;
RA McKay D.J., Renaux B.S., Dixon G.H.;
RT "Human sperm protamines. Amino-acid sequences of two forms of protamine
RT P2.";
RL Eur. J. Biochem. 156:5-8(1986).
RN [13]
RP PROTEIN SEQUENCE OF 45-102 (HP4).
RC TISSUE=Sperm;
RX PubMed=1889406; DOI=10.1111/j.1432-1033.1991.tb16196.x;
RA Arkhis A., Martinage A., Sautiere P., Chevaillier P.;
RT "Molecular structure of human protamine P4 (HP4), a minor basic protein of
RT human sperm nuclei.";
RL Eur. J. Biochem. 200:387-392(1991).
CC -!- FUNCTION: Protamines substitute for histones in the chromatin of sperm
CC during the haploid phase of spermatogenesis. They compact sperm DNA
CC into a highly condensed, stable and inactive complex.
CC {ECO:0000250|UniProtKB:P07978}.
CC -!- SUBUNIT: Interacts with TDRP. {ECO:0000250|UniProtKB:P07978}.
CC -!- INTERACTION:
CC P04554; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-9681663, EBI-10172290;
CC P04554; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-9681663, EBI-11988175;
CC P04554; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-9681663, EBI-742426;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07978}.
CC Chromosome {ECO:0000250|UniProtKB:P07978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04554-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04554-2; Sequence=VSP_054786;
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- PTM: Proteolytic processing into mature chains is required for histone
CC eviction during spermatogenesis. Transition proteins (TNP1 and TNP2)
CC are required for processing. {ECO:0000250|UniProtKB:P07978}.
CC -!- SIMILARITY: Belongs to the protamine P2 family. {ECO:0000305}.
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DR EMBL; X07862; CAA30710.1; -; mRNA.
DR EMBL; M60332; AAA63250.1; -; Genomic_DNA.
DR EMBL; Z46940; CAA87066.1; -; Genomic_DNA.
DR EMBL; U15422; AAC50487.1; -; Genomic_DNA.
DR EMBL; AF215713; AAF34632.1; -; Genomic_DNA.
DR EMBL; AK131573; BAD18705.1; -; mRNA.
DR EMBL; AC009121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005303; AAH05303.1; -; mRNA.
DR EMBL; BC066338; AAH66338.1; -; mRNA.
DR CCDS; CCDS42118.1; -. [P04554-1]
DR CCDS; CCDS66944.1; -. [P04554-2]
DR PIR; B38515; HSHUP2.
DR RefSeq; NP_001273285.1; NM_001286356.1. [P04554-2]
DR RefSeq; NP_001273287.1; NM_001286358.1.
DR RefSeq; NP_001273288.1; NM_001286359.1.
DR RefSeq; NP_002753.2; NM_002762.3. [P04554-1]
DR AlphaFoldDB; P04554; -.
DR BioGRID; 111605; 44.
DR IntAct; P04554; 5.
DR STRING; 9606.ENSP00000403681; -.
DR iPTMnet; P04554; -.
DR PhosphoSitePlus; P04554; -.
DR BioMuta; PRM2; -.
DR DMDM; 123700; -.
DR MassIVE; P04554; -.
DR PaxDb; P04554; -.
DR PeptideAtlas; P04554; -.
DR PRIDE; P04554; -.
DR ProteomicsDB; 51717; -. [P04554-1]
DR ProteomicsDB; 67890; -.
DR Antibodypedia; 58005; 56 antibodies from 15 providers.
DR DNASU; 5620; -.
DR Ensembl; ENST00000241808.9; ENSP00000241808.5; ENSG00000122304.11. [P04554-1]
DR Ensembl; ENST00000435245.2; ENSP00000403681.2; ENSG00000122304.11. [P04554-2]
DR GeneID; 5620; -.
DR KEGG; hsa:5620; -.
DR MANE-Select; ENST00000241808.9; ENSP00000241808.5; NM_002762.4; NP_002753.2.
DR UCSC; uc032drg.2; human. [P04554-1]
DR CTD; 5620; -.
DR DisGeNET; 5620; -.
DR GeneCards; PRM2; -.
DR HGNC; HGNC:9448; PRM2.
DR HPA; ENSG00000122304; Tissue enriched (testis).
DR MIM; 182882; gene.
DR MIM; 182890; gene.
DR neXtProt; NX_P04554; -.
DR OpenTargets; ENSG00000122304; -.
DR PharmGKB; PA33793; -.
DR VEuPathDB; HostDB:ENSG00000122304; -.
DR eggNOG; ENOG502TD5P; Eukaryota.
DR GeneTree; ENSGT00940000163619; -.
DR HOGENOM; CLU_175685_0_0_1; -.
DR InParanoid; P04554; -.
DR OMA; PCAPIPG; -.
DR OrthoDB; 1595135at2759; -.
DR TreeFam; TF338206; -.
DR PathwayCommons; P04554; -.
DR SignaLink; P04554; -.
DR BioGRID-ORCS; 5620; 17 hits in 1068 CRISPR screens.
DR ChiTaRS; PRM2; human.
DR GenomeRNAi; 5620; -.
DR Pharos; P04554; Tbio.
DR PRO; PR:P04554; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P04554; protein.
DR Bgee; ENSG00000122304; Expressed in right testis and 78 other tissues.
DR ExpressionAtlas; P04554; baseline and differential.
DR Genevisible; P04554; HS.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:ProtInc.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0046870; F:cadmium ion binding; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; TAS:ProtInc.
DR GO; GO:0006997; P:nucleus organization; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR000492; PRM2.
DR PANTHER; PTHR21341; PTHR21341; 1.
DR Pfam; PF00841; Protamine_P2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA condensation; DNA-binding; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..102
FT /note="Basic nuclear protein HPI1"
FT /id="PRO_0000025758"
FT CHAIN 22..102
FT /note="Basic nuclear protein HPI2"
FT /id="PRO_0000025759"
FT CHAIN 34..102
FT /note="Basic nuclear protein HPS1"
FT /id="PRO_0000025760"
FT CHAIN 37..102
FT /note="Basic nuclear protein HPS2"
FT /id="PRO_0000025761"
FT CHAIN 45..102
FT /note="Sperm histone HP4"
FT /id="PRO_0000025762"
FT CHAIN 46..102
FT /note="Sperm histone HP2"
FT /id="PRO_0000025763"
FT CHAIN 49..102
FT /note="Sperm histone HP3"
FT /id="PRO_0000025764"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..102
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11248"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11248"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11248"
FT VAR_SEQ 91..102
FT /note="GCRTRKRTCRRH -> ESLGDPLNQNFLSQKAAEPGREHAEGTKLPGPLTPS
FT WKLRKSRPKHQVRP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054786"
FT CONFLICT 38..39
FT /note="PE -> RM (in Ref. 1; CAA30710)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="H -> Q (in Ref. 1; CAA30710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 102 AA; 13051 MW; CBB8D6F2396F2F9C CRC64;
MVRYRVRSLS ERSHEVYRQQ LHGQEQGHHG QEEQGLSPEH VEVYERTHGQ SHYRRRHCSR
RRLHRIHRRQ HRSCRRRKRR SCRHRRRHRR GCRTRKRTCR RH
