STP2_HUMAN
ID STP2_HUMAN Reviewed; 138 AA.
AC Q05952; Q9NZB0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Nuclear transition protein 2;
DE Short=TP-2;
DE Short=TP2;
GN Name=TNP2;
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 [GENOMIC DNA].
RX PubMed=8428967; DOI=10.1016/s0021-9258(18)53863-1;
RA Nelson J.E., Krawetz S.A.;
RT "Linkage of human spermatid-specific basic nuclear protein genes.
RT Definition and evolution of the P1-->P2-->TP2 locus.";
RL J. Biol. Chem. 268:2932-2936(1993).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1385303; DOI=10.1016/s0888-7543(05)80229-0;
RA Schluter G., Kremling H., Engel W.;
RT "The gene for human transition protein 2: nucleotide sequence, assignment
RT to the protamine gene cluster, and evidence for its low expression.";
RL Genomics 14:377-383(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-133.
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 TISSUE SPECIFICITY.
RX PubMed=9809674; DOI=10.1093/molehr/4.10.939;
RA Steger K., Klonisch T., Gavenis K., Drabent B., Doenecke D., Bergmann M.;
RT "Expression of mRNA and protein of nucleoproteins during human
RT spermiogenesis.";
RL Mol. Hum. Reprod. 4:939-945(1998).
CC -!- FUNCTION: Plays a key role in the replacement of histones to protamine
CC in the elongating spermatids of mammals. In condensing spermatids,
CC loaded onto the nucleosomes, where it promotes the recruitment and
CC processing of protamines, which are responsible for histone eviction.
CC {ECO:0000250|UniProtKB:P11378}.
CC -!- INTERACTION:
CC Q05952; Q92624: APPBP2; NbExp=3; IntAct=EBI-12039775, EBI-743771;
CC Q05952; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-12039775, EBI-11959885;
CC Q05952; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12039775, EBI-10171774;
CC Q05952; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-12039775, EBI-10172052;
CC Q05952; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-12039775, EBI-11953334;
CC Q05952; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-12039775, EBI-14065470;
CC Q05952; Q99750: MDFI; NbExp=4; IntAct=EBI-12039775, EBI-724076;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11101}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P11101}. Chromosome
CC {ECO:0000250|UniProtKB:P11101}. Note=Loaded onto the nucleosomes of
CC condensing spermatids (By similarity). Nuclear import is mediated by
CC IPO4. Nucleolar localization requires the protein to be phosphorylated
CC (By similarity). {ECO:0000250|UniProtKB:P11101,
CC ECO:0000250|UniProtKB:P11378}.
CC -!- TISSUE SPECIFICITY: Expressed by spermatids (at protein level).
CC {ECO:0000269|PubMed:9809674}.
CC -!- SIMILARITY: Belongs to the nuclear transition protein 2 family.
CC {ECO:0000305}.
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DR EMBL; L03378; AAA61203.1; -; Genomic_DNA.
DR EMBL; U15422; AAC50488.1; -; Genomic_DNA.
DR EMBL; X63758; CAA45290.1; -; mRNA.
DR EMBL; X63759; CAA45291.1; -; mRNA.
DR EMBL; Z46940; CAA87067.1; -; Genomic_DNA.
DR EMBL; AF215715; AAF35854.1; -; Genomic_DNA.
DR CCDS; CCDS45410.1; -.
DR PIR; A44477; BGHU2.
DR RefSeq; NP_005416.1; NM_005425.4.
DR AlphaFoldDB; Q05952; -.
DR BioGRID; 112996; 33.
DR IntAct; Q05952; 7.
DR STRING; 9606.ENSP00000325738; -.
DR iPTMnet; Q05952; -.
DR PhosphoSitePlus; Q05952; -.
DR BioMuta; TNP2; -.
DR DMDM; 464818; -.
DR PaxDb; Q05952; -.
DR PRIDE; Q05952; -.
DR Antibodypedia; 65957; 130 antibodies from 20 providers.
DR DNASU; 7142; -.
DR Ensembl; ENST00000312693.4; ENSP00000325738.3; ENSG00000178279.4.
DR GeneID; 7142; -.
DR KEGG; hsa:7142; -.
DR MANE-Select; ENST00000312693.4; ENSP00000325738.3; NM_005425.5; NP_005416.1.
DR CTD; 7142; -.
DR DisGeNET; 7142; -.
DR GeneCards; TNP2; -.
DR HGNC; HGNC:11952; TNP2.
DR HPA; ENSG00000178279; Tissue enriched (testis).
DR MIM; 190232; gene.
DR neXtProt; NX_Q05952; -.
DR OpenTargets; ENSG00000178279; -.
DR PharmGKB; PA36641; -.
DR VEuPathDB; HostDB:ENSG00000178279; -.
DR eggNOG; KOG4566; Eukaryota.
DR GeneTree; ENSGT00390000008176; -.
DR HOGENOM; CLU_152028_0_0_1; -.
DR InParanoid; Q05952; -.
DR OMA; RPQSHTC; -.
DR OrthoDB; 1586614at2759; -.
DR PhylomeDB; Q05952; -.
DR TreeFam; TF338516; -.
DR PathwayCommons; Q05952; -.
DR SignaLink; Q05952; -.
DR BioGRID-ORCS; 7142; 13 hits in 1064 CRISPR screens.
DR GeneWiki; TNP2; -.
DR GenomeRNAi; 7142; -.
DR Pharos; Q05952; Tbio.
DR PRO; PR:Q05952; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q05952; protein.
DR Bgee; ENSG00000178279; Expressed in sperm and 33 other tissues.
DR ExpressionAtlas; Q05952; baseline and differential.
DR Genevisible; Q05952; HS.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; IBA:GO_Central.
DR GO; GO:0007341; P:penetration of zona pellucida; IBA:GO_Central.
DR GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR InterPro; IPR000678; TP2.
DR PANTHER; PTHR17488; PTHR17488; 1.
DR Pfam; PF01254; TP2; 1.
DR PROSITE; PS00970; TP2_1; 1.
DR PROSITE; PS00971; TP2_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Zinc.
FT CHAIN 1..138
FT /note="Nuclear transition protein 2"
FT /id="PRO_0000191425"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 111..119
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT COMPBIAS 1..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT VARIANT 131
FT /note="R -> W (in dbSNP:rs11640138)"
FT /id="VAR_052157"
SQ SEQUENCE 138 AA; 15641 MW; 9D2A605556BF644E CRC64;
MDTQTHSLPI THTQLHSNSQ PQSRTCTRHC QTFSQSCRQS HRGSRSQSSS QSPASHRNPT
GAHSSSGHQS QSPNTSPPPK RHKKTMNSHH SPMRPTILHC RCPKNRKNLE GKLKKKKMAK
RIQQVYKTKT RSSGWKSN
