NASP_BOVIN
ID NASP_BOVIN Reviewed; 777 AA.
AC Q2T9P4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Nuclear autoantigenic sperm protein;
DE Short=NASP;
GN Name=NASP {ECO:0000312|EMBL:AAI11330.2};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI11330.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI11330.2};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI11330.2};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for DNA replication, normal cell cycle progression
CC and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1
CC linker histones and stimulates HSP90 ATPase activity. NASP and H1
CC histone are subsequently released from the complex and translocate to
CC the nucleus where the histone is released for binding to DNA.
CC {ECO:0000250|UniProtKB:Q99MD9}.
CC -!- SUBUNIT: Binds to linker H1 histones but not to core histones (By
CC similarity). Interacts with histones H2A, H2B, H3 and H4 (By
CC similarity). Also binds to HSP90 in the cytoplasm. This interaction
CC stimulates binding of NASP to H1-6/H1T (By similarity).
CC {ECO:0000250|UniProtKB:P49321, ECO:0000250|UniProtKB:Q99MD9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99MD9}. Nucleus
CC {ECO:0000250|UniProtKB:Q99MD9}.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR EMBL; BC111329; AAI11330.2; -; mRNA.
DR RefSeq; NP_001033177.2; NM_001038088.3.
DR RefSeq; XP_010801905.1; XM_010803603.2.
DR AlphaFoldDB; Q2T9P4; -.
DR SMR; Q2T9P4; -.
DR STRING; 9913.ENSBTAP00000020401; -.
DR PaxDb; Q2T9P4; -.
DR PeptideAtlas; Q2T9P4; -.
DR PRIDE; Q2T9P4; -.
DR Ensembl; ENSBTAT00000020401; ENSBTAP00000020401; ENSBTAG00000015346.
DR GeneID; 512427; -.
DR KEGG; bta:512427; -.
DR CTD; 4678; -.
DR VEuPathDB; HostDB:ENSBTAG00000015346; -.
DR VGNC; VGNC:31887; NASP.
DR eggNOG; KOG4563; Eukaryota.
DR GeneTree; ENSGT00390000016650; -.
DR HOGENOM; CLU_010162_0_0_1; -.
DR InParanoid; Q2T9P4; -.
DR OMA; SSAFPCE; -.
DR OrthoDB; 1176629at2759; -.
DR TreeFam; TF317297; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000015346; Expressed in testis and 105 other tissues.
DR ExpressionAtlas; Q2T9P4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Coiled coil; Cytoplasm; DNA replication;
KW Isopeptide bond; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT CHAIN 2..777
FT /note="Nuclear autoantigenic sperm protein"
FT /id="PRO_0000262762"
FT REPEAT 44..77
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 531..564
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 573..606
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REGION 117..128
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 152..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..244
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 458..501
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 667..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..158
FT /evidence="ECO:0000255"
FT COILED 442..500
FT /evidence="ECO:0000255"
FT COILED 593..651
FT /evidence="ECO:0000255"
FT COILED 742..768
FT /evidence="ECO:0000255"
FT MOTIF 705..711
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 152..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 285
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 672
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT CROSSLNK 725
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P49321"
SQ SEQUENCE 777 AA; 83688 MW; DB1E58C80F5A82A3 CRC64;
MAAESTATAA ITAELVSADK IEEDAPAPST SADKVESLDV DSEAKKLLGL GQKHLVMGDI
PAAVNAFQEA ASLLGKKYGE TANECGEAFF FYGKSLLELA RMENGVLGNA LEGVHVEEEE
GEKTEEESLV ENNDNIDEEA REELREQVYD AMGEKEAQKT EDKSLVKPEM DKEQETEMEK
GGREDMDIGE PAEELQEKVK SAPDQLTETT EEGKGAAAPE GLSEAEVTSK KPDQEIPGAE
EGKSVSETDV QEECREKGGQ GEVIVSIEEK PKEASKEQPV VTLEKQGTPV EIEAVKPVDM
GGDEPKEQVA ASESERGKAI LEQLVGQELP SAEESPEVTT QAADASAAEA GSEVSEKPGG
QDTVLPQDGA VNGLSAAGDH ASTKPQTNAE GLIGTKDGSA LEKVRAELVP SQETKLSVEE
SEAAGDGVET EVAQGATEQS PEDKVKIAAN EEAQDKEEQM KEGEETEGSE EEDKENDKAE
ETLNDSALEN KSLQENEEEE IGNLELAWDM LDLAKIIFKR QDTKEAQLYA AQAHLKLGEV
SVESENYLQA VEEFQACLNL QEQYLEAHDR LLAETHYQLG LAYGYNSQYD EAVAQFSKSI
EVIEKRMAVL NEQMKEAEGS PTEYEKEIEE LKELLPEIRE KIEDAKESQR SGNVAELALK
ATLVESSTSG FTPSGGSSSV SMIASRKPTD GASSSNCVTD ISHLVRKKRK PEEESPRKDD
AKKAKQEPEV NGGSGDTIST GTEVAENMEE EAENKAESRA AVEGTVEAGA TVESTAC
