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 11-NOV-2015, entry version 134. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA 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 RT project: 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) RT from 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; RA Sautiere P., Martinage A., Belaiche D., Arkhis A., Chevaillier P.; RT "Comparison of the amino acid sequences of human protamines HP2 and RT HP3 and of intermediate basic nuclear proteins HPS1 and HPS2. RT Structural evidence 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; RA Ammer H., Henschen A., Lee C.-H.; RT "Isolation and amino-acid sequence analysis of human sperm protamines RT P1 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 RT protamine 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 RT protein of human sperm nuclei."; RL Eur. J. Biochem. 200:387-392(1991). CC -!- FUNCTION: Protamines substitute for histones in the chromatin of CC sperm during the haploid phase of spermatogenesis. They compact CC sperm DNA into a highly condensed, stable and inactive complex. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. 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 Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Testis. CC -!- SIMILARITY: Belongs to the protamine P2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.2324; -. DR PDB; 2AWR; Model; -; B=46-102. DR PDBsum; 2AWR; -. DR ProteinModelPortal; P04554; -. DR BioGrid; 111605; 2. DR IntAct; P04554; 2. DR STRING; 9606.ENSP00000241808; -. DR PhosphoSite; P04554; -. DR DMDM; 123700; -. DR PaxDb; P04554; -. DR PRIDE; P04554; -. DR DNASU; 5620; -. DR Ensembl; ENST00000241808; ENSP00000241808; ENSG00000122304. [P04554-1] DR Ensembl; ENST00000435245; ENSP00000403681; ENSG00000122304. [P04554-2] DR GeneID; 5620; -. DR KEGG; hsa:5620; -. DR UCSC; uc002dau.1; human. [P04554-1] DR CTD; 5620; -. DR GeneCards; PRM2; -. DR HGNC; HGNC:9448; PRM2. DR HPA; CAB032738; -. DR HPA; HPA056386; -. DR MIM; 182882; gene. DR MIM; 182890; gene. DR neXtProt; NX_P04554; -. DR PharmGKB; PA33793; -. DR eggNOG; ENOG410KFYE; Eukaryota. DR eggNOG; ENOG4110SVE; LUCA. DR GeneTree; ENSGT00730000111973; -. DR HOGENOM; HOG000143619; -. DR HOVERGEN; HBG082177; -. DR InParanoid; P04554; -. DR OMA; HVEVYER; -. DR OrthoDB; EOG7SXW6X; -. DR TreeFam; TF338206; -. DR GenomeRNAi; 5620; -. DR NextBio; 21840; -. DR PRO; PR:P04554; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; P04554; -. DR CleanEx; HS_PRM2; -. DR ExpressionAtlas; P04554; baseline and differential. DR Genevisible; P04554; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:ProtInc. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW. DR GO; GO:0006323; P:DNA packaging; TAS:ProtInc. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc. DR InterPro; IPR000492; PRM2. DR PANTHER; PTHR21341; PTHR21341; 1. DR Pfam; PF00841; Protamine_P2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; Complete proteome; KW Developmental protein; Differentiation; Direct protein sequencing; KW DNA condensation; DNA-binding; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Spermatogenesis. FT CHAIN 2 102 Basic nuclear protein HPI1. FT /FTId=PRO_0000025758. FT CHAIN 22 102 Basic nuclear protein HPI2. FT /FTId=PRO_0000025759. FT CHAIN 34 102 Basic nuclear protein HPS1. FT /FTId=PRO_0000025760. FT CHAIN 37 102 Basic nuclear protein HPS2. FT /FTId=PRO_0000025761. FT CHAIN 45 102 Sperm histone HP4. FT /FTId=PRO_0000025762. FT CHAIN 46 102 Sperm histone HP2. FT /FTId=PRO_0000025763. FT CHAIN 49 102 Sperm histone HP3. FT /FTId=PRO_0000025764. FT MOD_RES 8 8 Phosphoserine. FT {ECO:0000250|UniProtKB:P11248}. FT MOD_RES 10 10 Phosphoserine. FT {ECO:0000250|UniProtKB:P11248}. FT MOD_RES 37 37 Phosphoserine. FT {ECO:0000250|UniProtKB:P11248}. FT VAR_SEQ 91 102 GCRTRKRTCRRH -> ESLGDPLNQNFLSQKAAEPGREHAE FT GTKLPGPLTPSWKLRKSRPKHQVRP (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054786. FT CONFLICT 38 39 PE -> RM (in Ref. 1; CAA30710). FT {ECO:0000305}. FT CONFLICT 52 52 H -> Q (in Ref. 1; CAA30710). FT {ECO:0000305}. SQ SEQUENCE 102 AA; 13051 MW; CBB8D6F2396F2F9C CRC64; MVRYRVRSLS ERSHEVYRQQ LHGQEQGHHG QEEQGLSPEH VEVYERTHGQ SHYRRRHCSR RRLHRIHRRQ HRSCRRRKRR SCRHRRRHRR GCRTRKRTCR RH //