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Protein

Nuclear autoantigenic sperm protein

Gene

Nasp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA replication, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear autoantigenic sperm protein
Short name:
NASP
Gene namesi
Name:NaspImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1359609. Nasp.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 776775Nuclear autoantigenic sperm proteinPRO_0000261598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei33 – 331N6-acetyllysineBy similarity
Modified residuei123 – 1231PhosphothreonineBy similarity
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei241 – 2411N6-acetyllysineBy similarity
Modified residuei242 – 2421PhosphoserineCombined sources
Modified residuei251 – 2511N6-acetyllysineBy similarity
Modified residuei286 – 2861N6-acetyllysineBy similarity
Modified residuei306 – 3061PhosphoserineCombined sources
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei379 – 3791PhosphothreonineCombined sources
Modified residuei398 – 3981PhosphoserineCombined sources
Modified residuei452 – 4521PhosphothreonineCombined sources
Modified residuei465 – 4651PhosphothreonineBy similarity
Modified residuei468 – 4681PhosphoserineCombined sources
Modified residuei482 – 4821PhosphothreonineCombined sources
Modified residuei485 – 4851PhosphoserineCombined sources
Modified residuei671 – 6711PhosphothreonineBy similarity
Modified residuei714 – 7141PhosphoserineCombined sources
Modified residuei739 – 7391PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ66HD3.
PRIDEiQ66HD3.

PTM databases

iPTMnetiQ66HD3.
PhosphoSiteiQ66HD3.

Expressioni

Gene expression databases

GenevisibleiQ66HD3. RN.

Interactioni

Subunit structurei

Binds to linker H1 histones but not to core histones. Also binds to HSP90 in the cytoplasm. This interaction stimulates binding of NASP to HIST1H1T/H1T (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022170.

Structurei

3D structure databases

ProteinModelPortaliQ66HD3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati43 – 7634TPR 1Sequence analysisAdd
BLAST
Repeati530 – 56334TPR 2Sequence analysisAdd
BLAST
Repeati572 – 60534TPR 3Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 12712Histone-bindingBy similarityAdd
BLAST
Regioni210 – 24233Histone-bindingBy similarityAdd
BLAST
Regioni457 – 50044Histone-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili126 – 16035Sequence analysisAdd
BLAST
Coiled coili191 – 21626Sequence analysisAdd
BLAST
Coiled coili597 – 65054Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi704 – 7107Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 646536Glu-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the NASP family.Curated
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG4563. Eukaryota.
ENOG4110P5E. LUCA.
GeneTreeiENSGT00390000016650.
HOGENOMiHOG000013120.
HOVERGENiHBG002186.
InParanoidiQ66HD3.
KOiK11291.
OMAiSTEYEKE.
OrthoDBiEOG7X9G7Z.
PhylomeDBiQ66HD3.
TreeFamiTF317297.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR019544. Tetratricopeptide_SHNi-TPR_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF10516. SHNi-TPR. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q66HD3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATESTATAA IAAELVSADK VEDAPAPSTS ADKMESLDVD SEAKKLLGLG
60 70 80 90 100
QKHLVMGDIP AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR
110 120 130 140 150
MENGVLGNAL EGVHVEEEEG EKTEDESLVE NNDNVDEEAR EELREQVYDA
160 170 180 190 200
MGEKEAKKAE GQSLTKPETD KEQESEVEKG GREDMDISEP AEKLQEKVES
210 220 230 240 250
TSKQLTESSE EAKEAAIPGL NEDEVTSGKT EQESLCTEEG KSISGVYVQN
260 270 280 290 300
KEFREAVPQE EGEEMISLEK KPKETSEDQT IGAPEKQDTL MKVVEIEAEI
310 320 330 340 350
DSEVKSVDVG GEEPKDQGAI SESELGKAVL MQLSGQDVEV SPVVAAEAGS
360 370 380 390 400
EVSEKPGQEI TVLPNNGPVV GQSSAGDQTP SEPQNSAERL SETKDGASVE
410 420 430 440 450
EVKAELVPEQ EEAMPPVEES EAAGDGVETK VAQRATEKAP EDKFKIAANE
460 470 480 490 500
ETQERDEQMK EGEETEGSEE EDKENDKAEE TTNESVLEKK TLQENEEEEI
510 520 530 540 550
GNLELAWDML DLAKIIFKRQ ETKEAQLYAA QAHLKLGEVS VESENYIQAV
560 570 580 590 600
EEFQACLSLQ EQYLEAHDRL LAETHYQLGL AYGYNSQYDE AVAQFGKSID
610 620 630 640 650
VIEKRMAVLL EQMKEAEGSF TEYEKEIEEL KELLPEIREK IEDAKESQRS
660 670 680 690 700
GNVAELALKA TLVESSTSGF TPSGAGASVS MIASRKPTDG ASSSNCVTDI
710 720 730 740 750
SHLVRKKRKP EEESPRKDDA KKAKPEPEVN GGSGDAVSSG NEVSENMEAE
760 770
AENQAESQTT AEGTVDSAAT VKSTAC
Length:776
Mass (Da):84,200
Last modified:October 11, 2004 - v1
Checksum:i8E36041F0B86272F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081913 mRNA. Translation: AAH81913.1.
RefSeqiNP_001005543.1. NM_001005543.1.
XP_006238708.1. XM_006238646.2.
XP_008762215.1. XM_008763993.1.
UniGeneiRn.48344.

Genome annotation databases

EnsembliENSRNOT00000022170; ENSRNOP00000022170; ENSRNOG00000016454.
GeneIDi298441.
KEGGirno:298441.
UCSCiRGD:1359609. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081913 mRNA. Translation: AAH81913.1.
RefSeqiNP_001005543.1. NM_001005543.1.
XP_006238708.1. XM_006238646.2.
XP_008762215.1. XM_008763993.1.
UniGeneiRn.48344.

3D structure databases

ProteinModelPortaliQ66HD3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022170.

PTM databases

iPTMnetiQ66HD3.
PhosphoSiteiQ66HD3.

Proteomic databases

PaxDbiQ66HD3.
PRIDEiQ66HD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022170; ENSRNOP00000022170; ENSRNOG00000016454.
GeneIDi298441.
KEGGirno:298441.
UCSCiRGD:1359609. rat.

Organism-specific databases

CTDi4678.
RGDi1359609. Nasp.

Phylogenomic databases

eggNOGiKOG4563. Eukaryota.
ENOG4110P5E. LUCA.
GeneTreeiENSGT00390000016650.
HOGENOMiHOG000013120.
HOVERGENiHBG002186.
InParanoidiQ66HD3.
KOiK11291.
OMAiSTEYEKE.
OrthoDBiEOG7X9G7Z.
PhylomeDBiQ66HD3.
TreeFamiTF317297.

Miscellaneous databases

PROiQ66HD3.

Gene expression databases

GenevisibleiQ66HD3. RN.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR019544. Tetratricopeptide_SHNi-TPR_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF10516. SHNi-TPR. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: TestisImported.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-242; SER-306; SER-321; THR-379; SER-398; THR-452; SER-468; THR-482; SER-485 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNASP_RAT
AccessioniPrimary (citable) accession number: Q66HD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.