Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nuclear autoantigenic sperm protein

Gene

NASP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • Hsp90 protein binding Source: UniProtKB
  • protein complex binding Source: UniProtKB

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:NASP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7644. NASP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31448.

Polymorphism and mutation databases

BioMutaiNASP.
DMDMi23503077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 788787Nuclear autoantigenic sperm proteinPRO_0000106299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei33 – 331N6-acetyllysineCombined sources
Modified residuei123 – 1231PhosphothreonineCombined sources
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei170 – 1701PhosphothreonineCombined sources
Modified residuei176 – 1761PhosphoserineCombined sources
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei191 – 1911PhosphoserineCombined sources
Modified residuei243 – 2431N6-acetyllysineBy similarity
Modified residuei244 – 2441PhosphoserineCombined sources
Modified residuei288 – 2881N6-acetyllysineBy similarity
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei390 – 3901PhosphothreonineCombined sources
Modified residuei397 – 3971PhosphoserineCombined sources
Modified residuei408 – 4081PhosphoserineCombined sources
Modified residuei421 – 4211PhosphoserineCombined sources
Modified residuei451 – 4511PhosphoserineCombined sources
Modified residuei464 – 4641PhosphothreonineCombined sources
Modified residuei477 – 4771PhosphothreonineCombined sources
Modified residuei480 – 4801PhosphoserineCombined sources
Modified residuei490 – 4901PhosphothreonineCombined sources
Modified residuei497 – 4971PhosphoserineCombined sources
Modified residuei503 – 5031PhosphoserineCombined sources
Modified residuei662 – 6621PhosphoserineCombined sources
Modified residuei683 – 6831PhosphothreonineCombined sources
Modified residuei705 – 7051PhosphoserineCombined sources
Modified residuei706 – 7061PhosphoserineCombined sources
Modified residuei726 – 7261PhosphoserineCombined sources
Cross-linki736 – 736Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei745 – 7451PhosphoserineCombined sources
Modified residuei751 – 7511PhosphoserineCombined sources
Modified residuei756 – 7561PhosphoserineCombined sources
Isoform 2 (identifier: P49321-2)
Modified residuei138 – 1381PhosphothreonineCombined sources
Modified residuei141 – 1411PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49321.
MaxQBiP49321.
PaxDbiP49321.
PeptideAtlasiP49321.
PRIDEiP49321.

PTM databases

iPTMnetiP49321.
PhosphoSiteiP49321.
SwissPalmiP49321.

Miscellaneous databases

PMAP-CutDBP49321.

Expressioni

Tissue specificityi

Isoform 1 is testis- and sperm-specific.

Gene expression databases

BgeeiP49321.
CleanExiHS_NASP.
ExpressionAtlasiP49321. baseline and differential.
GenevisibleiP49321. HS.

Organism-specific databases

HPAiHPA028136.
HPA030518.
HPA030520.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
H3F3BP842433EBI-7038920,EBI-120658
H3F3CQ6NXT23EBI-7038920,EBI-2868501
HIST1H3DP684314EBI-7038920,EBI-79722
TERF2IPQ9NYB02EBI-716205,EBI-750109

GO - Molecular functioni

  • Hsp90 protein binding Source: UniProtKB
  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110759. 53 interactions.
DIPiDIP-47269N.
IntActiP49321. 28 interactions.
MINTiMINT-4656497.
STRINGi9606.ENSP00000255120.

Structurei

3D structure databases

ProteinModelPortaliP49321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati43 – 7634TPR 1Add
BLAST
Repeati542 – 57534TPR 2Add
BLAST
Repeati584 – 61734TPR 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 12712Histone-bindingAdd
BLAST
Regioni211 – 24434Histone-bindingAdd
BLAST
Regioni469 – 51244Histone-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili136 – 16429Sequence analysisAdd
BLAST
Coiled coili460 – 48728Sequence analysisAdd
BLAST
Coiled coili597 – 66569Sequence analysisAdd
BLAST
Coiled coili753 – 77826Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi716 – 7227Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 658548Glu-rich (acidic)Add
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.
InParanoidiP49321.
KOiK11291.
OMAiSTEYEKE.
OrthoDBiEOG7X9G7Z.
PhylomeDBiP49321.
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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49321-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAMESTATAA VAAELVSADK IEDVPAPSTS ADKVESLDVD SEAKKLLGLG
60 70 80 90 100
QKHLVMGDIP AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR
110 120 130 140 150
MENGVLGNAL EGVHVEEEEG EKTEDESLVE NNDNIDEEAR EELREQVYDA
160 170 180 190 200
MGEKEEAKKT EDKSLAKPET DKEQDSEMEK GGREDMDISK SAEEPQEKVD
210 220 230 240 250
LTLDWLTETS EEAKGGAAPE GPNEAEVTSG KPEQEVPDAE EEKSVSGTDV
260 270 280 290 300
QEECREKGGQ EKQGEVIVSI EEKPKEVSEE QPVVTLEKQG TAVEVEAESL
310 320 330 340 350
DPTVKPVDVG GDEPEEKVVT SENEAGKAVL EQLVGQEVPP AEESPEVTTE
360 370 380 390 400
AAEASAVEAG SEVSEKPGQE APVLPKDGAV NGPSVVGDQT PIEPQTSIER
410 420 430 440 450
LTETKDGSGL EEKVRAKLVP SQEETKLSVE ESEAAGDGVD TKVAQGATEK
460 470 480 490 500
SPEDKVQIAA NEETQEREEQ MKEGEETEGS EEDDKENDKT EEMPNDSVLE
510 520 530 540 550
NKSLQENEEE EIGNLELAWD MLDLAKIIFK RQETKEAQLY AAQAHLKLGE
560 570 580 590 600
VSVESENYVQ AVEEFQSCLN LQEQYLEAHD RLLAETHYQL GLAYGYNSQY
610 620 630 640 650
DEAVAQFSKS IEVIENRMAV LNEQVKEAEG SSAEYKKEIE ELKELLPEIR
660 670 680 690 700
EKIEDAKESQ RSGNVAELAL KATLVESSTS GFTPGGGGSS VSMIASRKPT
710 720 730 740 750
DGASSSNCVT DISHLVRKKR KPEEESPRKD DAKKAKQEPE VNGGSGDAVP
760 770 780
SGNEVSENME EEAENQAESR AAVEGTVEAG ATVESTAC
Length:788
Mass (Da):85,238
Last modified:September 19, 2002 - v2
Checksum:i0F4EB2BBE71534E8
GO
Isoform 2 (identifier: P49321-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-476: Missing.

Show »
Length:449
Mass (Da):48,804
Checksum:iA69B7FE13AAA3433
GO
Isoform 3 (identifier: P49321-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MAMESTATAAVAAELVSADKIEDVPAPSTSADKVES → MFLLLLHLQIKWRATINLLSVTEDGLHFVEYYLNRIIH

Show »
Length:790
Mass (Da):86,268
Checksum:i6C7299FFBC62B4B2
GO
Isoform 4 (identifier: P49321-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-99: Missing.

Note: No experimental confirmation available.
Show »
Length:724
Mass (Da):78,450
Checksum:iB1917C4EF7BAE070
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152EL → DV in AAA36027 (PubMed:1426632).Curated
Sequence conflicti159 – 1591K → T in BAD96536 (Ref. 3) Curated
Sequence conflicti183 – 1831R → G in BAG61005 (PubMed:14702039).Curated
Sequence conflicti348 – 3481T → Q in AAA36027 (PubMed:1426632).Curated
Sequence conflicti633 – 6331Missing in AAA36027 (PubMed:1426632).Curated
Sequence conflicti767 – 7704AESR → LKRG in AAA36027 (PubMed:1426632).Curated
Sequence conflicti777 – 7771V → L in AAA36027 (PubMed:1426632).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti620 – 6201V → G.
Corresponds to variant rs34618000 [ dbSNP | Ensembl ].
VAR_052619

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MAMES…DKVES → MFLLLLHLQIKWRATINLLS VTEDGLHFVEYYLNRIIH in isoform 3. 1 PublicationVSP_036616Add
BLAST
Alternative sequencei36 – 9964Missing in isoform 4. 1 PublicationVSP_047028Add
BLAST
Alternative sequencei138 – 476339Missing in isoform 2. 1 PublicationVSP_006551Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97856 mRNA. Translation: AAA36027.1.
AK056161 mRNA. No translation available.
AK291637 mRNA. Translation: BAF84326.1.
AK298893 mRNA. Translation: BAG61005.1.
AK222816 mRNA. Translation: BAD96536.1.
AL355480 Genomic DNA. Translation: CAI22462.1.
AL355480 Genomic DNA. Translation: CAI22465.1.
CH471059 Genomic DNA. Translation: EAX06968.1.
CH471059 Genomic DNA. Translation: EAX06969.1.
BC003113 mRNA. Translation: AAH03113.1.
BC053608 mRNA. Translation: AAH53608.1.
BC010105 mRNA. Translation: AAH10105.1.
BC011580 mRNA. Translation: AAH11580.1.
CCDSiCCDS524.1. [P49321-1]
CCDS525.1. [P49321-2]
CCDS55597.1. [P49321-4]
PIRiA48819.
RefSeqiNP_001182122.1. NM_001195193.1. [P49321-4]
NP_002473.2. NM_002482.3. [P49321-1]
NP_689511.2. NM_152298.3. [P49321-2]
XP_005270945.1. XM_005270888.2. [P49321-3]
UniGeneiHs.319334.

Genome annotation databases

EnsembliENST00000350030; ENSP00000255120; ENSG00000132780. [P49321-1]
ENST00000351223; ENSP00000255121; ENSG00000132780. [P49321-2]
ENST00000537798; ENSP00000438871; ENSG00000132780. [P49321-4]
GeneIDi4678.
KEGGihsa:4678.
UCSCiuc001coi.3. human. [P49321-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97856 mRNA. Translation: AAA36027.1.
AK056161 mRNA. No translation available.
AK291637 mRNA. Translation: BAF84326.1.
AK298893 mRNA. Translation: BAG61005.1.
AK222816 mRNA. Translation: BAD96536.1.
AL355480 Genomic DNA. Translation: CAI22462.1.
AL355480 Genomic DNA. Translation: CAI22465.1.
CH471059 Genomic DNA. Translation: EAX06968.1.
CH471059 Genomic DNA. Translation: EAX06969.1.
BC003113 mRNA. Translation: AAH03113.1.
BC053608 mRNA. Translation: AAH53608.1.
BC010105 mRNA. Translation: AAH10105.1.
BC011580 mRNA. Translation: AAH11580.1.
CCDSiCCDS524.1. [P49321-1]
CCDS525.1. [P49321-2]
CCDS55597.1. [P49321-4]
PIRiA48819.
RefSeqiNP_001182122.1. NM_001195193.1. [P49321-4]
NP_002473.2. NM_002482.3. [P49321-1]
NP_689511.2. NM_152298.3. [P49321-2]
XP_005270945.1. XM_005270888.2. [P49321-3]
UniGeneiHs.319334.

3D structure databases

ProteinModelPortaliP49321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110759. 53 interactions.
DIPiDIP-47269N.
IntActiP49321. 28 interactions.
MINTiMINT-4656497.
STRINGi9606.ENSP00000255120.

PTM databases

iPTMnetiP49321.
PhosphoSiteiP49321.
SwissPalmiP49321.

Polymorphism and mutation databases

BioMutaiNASP.
DMDMi23503077.

Proteomic databases

EPDiP49321.
MaxQBiP49321.
PaxDbiP49321.
PeptideAtlasiP49321.
PRIDEiP49321.

Protocols and materials databases

DNASUi4678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350030; ENSP00000255120; ENSG00000132780. [P49321-1]
ENST00000351223; ENSP00000255121; ENSG00000132780. [P49321-2]
ENST00000537798; ENSP00000438871; ENSG00000132780. [P49321-4]
GeneIDi4678.
KEGGihsa:4678.
UCSCiuc001coi.3. human. [P49321-1]

Organism-specific databases

CTDi4678.
GeneCardsiNASP.
HGNCiHGNC:7644. NASP.
HPAiHPA028136.
HPA030518.
HPA030520.
MIMi603185. gene.
neXtProtiNX_P49321.
PharmGKBiPA31448.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4563. Eukaryota.
ENOG4110P5E. LUCA.
GeneTreeiENSGT00390000016650.
HOGENOMiHOG000013120.
HOVERGENiHBG002186.
InParanoidiP49321.
KOiK11291.
OMAiSTEYEKE.
OrthoDBiEOG7X9G7Z.
PhylomeDBiP49321.
TreeFamiTF317297.

Miscellaneous databases

ChiTaRSiNASP. human.
GeneWikiiNASP_(gene).
GenomeRNAii4678.
PMAP-CutDBP49321.
PROiP49321.
SOURCEiSearch...

Gene expression databases

BgeeiP49321.
CleanExiHS_NASP.
ExpressionAtlasiP49321. baseline and differential.
GenevisibleiP49321. HS.

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

« Hide 'large scale' publications
  1. "Sequence and localization of human NASP: conservation of a Xenopus histone-binding protein."
    O'Rand M.G., Richardson R.T., Zimmerman L.J., Widgren E.E.
    Dev. Biol. 154:37-44(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-635 (ISOFORM 3).
    Tissue: Placenta and Teratocarcinoma.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Eye, Lung, Placenta and Testis.
  7. "Histone-binding domains in a human nuclear autoantigenic sperm protein."
    Batova I., O'Rand M.G.
    Biol. Reprod. 54:1238-1244(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: HISTONE-BINDING REGIONS.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-451; SER-503 AND SER-726, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-244; THR-390; SER-408 AND THR-683, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123; SER-127; SER-189; SER-451; THR-490; SER-497 AND SER-503, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-141 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123; SER-127; SER-189; SER-244; SER-321; THR-390; SER-408; SER-421; SER-451; THR-464; THR-477; SER-480; THR-490; SER-497; SER-503; SER-726 AND SER-751, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-141 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-176; SER-189; SER-191; SER-244; SER-299; THR-390; SER-397; SER-421; THR-464; THR-477; SER-480; THR-490; SER-497; SER-662; SER-705; SER-706; SER-745; SER-751 AND SER-756, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNASP_HUMAN
AccessioniPrimary (citable) accession number: P49321
Secondary accession number(s): A8K6H2
, B4DQP3, D3DQ07, F5H3J2, Q53GW5, Q5T622, Q5T625, Q96A69, Q9BTW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: September 19, 2002
Last modified: July 6, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.