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P55209

- NP1L1_HUMAN

UniProt

P55209 - NP1L1_HUMAN

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Protein
Nucleosome assembly protein 1-like 1
Gene
NAP1L1, NRP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in modulating chromatin formation and contribute to regulation of cell proliferation.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. DNA replication Source: ProtInc
  2. nucleosome assembly Source: ProtInc
  3. positive regulation of cell proliferation Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleosome assembly protein 1-like 1
Alternative name(s):
NAP-1-related protein
Short name:
hNRP
Gene namesi
Name:NAP1L1
Synonyms:NRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7637. NAP1L1.

Subcellular locationi

Nucleus. Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.1 Publication

GO - Cellular componenti

  1. melanosome Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 388387Nucleosome assembly protein 1-like 1
PRO_0000185652Add
BLAST
Propeptidei389 – 3913Removed in mature form Inferred
PRO_0000393943

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei62 – 621Phosphothreonine5 Publications
Modified residuei69 – 691Phosphoserine3 Publications
Modified residuei116 – 1161N6-acetyllysine1 Publication
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei388 – 3881Cysteine methyl ester Inferred
Lipidationi388 – 3881S-farnesyl cysteine1 Publication

Post-translational modificationi

Polyglutamylated by TTLL4, a modification that occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Some residues may also be monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human By similarity.

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP55209.
PaxDbiP55209.
PRIDEiP55209.

2D gel databases

OGPiP55209.

PTM databases

PhosphoSiteiP55209.

Miscellaneous databases

PMAP-CutDBP55209.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

ArrayExpressiP55209.
BgeeiP55209.
CleanExiHS_NAP1L1.
GenevestigatoriP55209.

Organism-specific databases

HPAiHPA028861.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CREBBPQ927933EBI-356392,EBI-81215
EP300Q094723EBI-356392,EBI-447295
NR2F6P105882EBI-356392,EBI-2681496
TTLL10Q6ZVT05EBI-356392,EBI-7844656

Protein-protein interaction databases

BioGridi110754. 65 interactions.
IntActiP55209. 46 interactions.
MINTiMINT-150144.
STRINGi9606.ENSP00000261182.

Structurei

3D structure databases

ProteinModelPortaliP55209.
SMRiP55209. Positions 64-347.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi273 – 2797Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 3021Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi129 – 14517Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi348 – 37831Asp/Glu-rich (acidic)
Add
BLAST

Domaini

The acidic domains are probably involved in the interaction with histones.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG285183.
HOGENOMiHOG000171827.
HOVERGENiHBG052653.
InParanoidiP55209.
KOiK11279.
OMAiPEYDPKK.
OrthoDBiEOG73Z2T8.
PhylomeDBiP55209.
TreeFamiTF314349.

Family and domain databases

InterProiIPR002164. NAP_family.
[Graphical view]
PANTHERiPTHR11875. PTHR11875. 1 hit.
PfamiPF00956. NAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P55209-1) [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

MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKLKARQLTV QMMQNPQILA    50
ALQERLDGLV ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH 100
DLERKYAVLY QPLFDKRFEI INAIYEPTEE ECEWKPDEED EISEELKEKA 150
KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL LSDMVQEHDE PILKHLKDIK 200
VKFSDAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD DSDPFSFDGP 250
EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF 300
FAPPEVPESG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD 350
DDDYDEEGEE ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q 391
Length:391
Mass (Da):45,374
Last modified:October 1, 1996 - v1
Checksum:iE5B2EAA4EAE551D2
GO
Isoform 2 (identifier: P55209-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     364-391: EGEEEGDEENDPDYDPKKDQNPAECKQQ → VMFTK

Note: No experimental confirmation available.

Show »
Length:368
Mass (Da):42,762
Checksum:i2EBD999BBE889411
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei364 – 39128EGEEE…ECKQQ → VMFTK in isoform 2.
VSP_053909Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86667 mRNA. Translation: AAC37544.1.
BT007023 mRNA. Translation: AAP35669.1.
AK055020 mRNA. Translation: BAG51450.1.
AL162068 mRNA. Translation: CAB82405.1.
AC011611 Genomic DNA. No translation available.
BC002387 mRNA. Translation: AAH02387.1.
CCDSiCCDS9013.1. [P55209-1]
PIRiS40510.
RefSeqiNP_004528.1. NM_004537.4. [P55209-1]
NP_631946.1. NM_139207.2. [P55209-1]
UniGeneiHs.524599.
Hs.695185.

Genome annotation databases

EnsembliENST00000261182; ENSP00000261182; ENSG00000187109.
ENST00000393263; ENSP00000376947; ENSG00000187109.
ENST00000549596; ENSP00000447793; ENSG00000187109.
GeneIDi4673.
KEGGihsa:4673.
UCSCiuc001sxw.2. human. [P55209-1]

Polymorphism databases

DMDMi1709337.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86667 mRNA. Translation: AAC37544.1 .
BT007023 mRNA. Translation: AAP35669.1 .
AK055020 mRNA. Translation: BAG51450.1 .
AL162068 mRNA. Translation: CAB82405.1 .
AC011611 Genomic DNA. No translation available.
BC002387 mRNA. Translation: AAH02387.1 .
CCDSi CCDS9013.1. [P55209-1 ]
PIRi S40510.
RefSeqi NP_004528.1. NM_004537.4. [P55209-1 ]
NP_631946.1. NM_139207.2. [P55209-1 ]
UniGenei Hs.524599.
Hs.695185.

3D structure databases

ProteinModelPortali P55209.
SMRi P55209. Positions 64-347.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110754. 65 interactions.
IntActi P55209. 46 interactions.
MINTi MINT-150144.
STRINGi 9606.ENSP00000261182.

PTM databases

PhosphoSitei P55209.

Polymorphism databases

DMDMi 1709337.

2D gel databases

OGPi P55209.

Proteomic databases

MaxQBi P55209.
PaxDbi P55209.
PRIDEi P55209.

Protocols and materials databases

DNASUi 4673.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261182 ; ENSP00000261182 ; ENSG00000187109 .
ENST00000393263 ; ENSP00000376947 ; ENSG00000187109 .
ENST00000549596 ; ENSP00000447793 ; ENSG00000187109 .
GeneIDi 4673.
KEGGi hsa:4673.
UCSCi uc001sxw.2. human. [P55209-1 ]

Organism-specific databases

CTDi 4673.
GeneCardsi GC12M076438.
HGNCi HGNC:7637. NAP1L1.
HPAi HPA028861.
MIMi 164060. gene.
neXtProti NX_P55209.
PharmGKBi PA31439.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285183.
HOGENOMi HOG000171827.
HOVERGENi HBG052653.
InParanoidi P55209.
KOi K11279.
OMAi PEYDPKK.
OrthoDBi EOG73Z2T8.
PhylomeDBi P55209.
TreeFami TF314349.

Miscellaneous databases

ChiTaRSi NAP1L1. human.
GeneWikii NAP1L1.
GenomeRNAii 4673.
NextBioi 18010.
PMAP-CutDB P55209.
PROi P55209.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55209.
Bgeei P55209.
CleanExi HS_NAP1L1.
Genevestigatori P55209.

Family and domain databases

InterProi IPR002164. NAP_family.
[Graphical view ]
PANTHERi PTHR11875. PTHR11875. 1 hit.
Pfami PF00956. NAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell proliferation."
    Simon H.-U., Mills G.B., Kozlowski M., Hogg D., Branch D., Ishimi Y., Siminovitch K.A.
    Biochem. J. 297:389-397(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Thymus.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 2).
    Tissue: Cerebellum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Melanoma.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Muscle.
  7. "A tagging-via-substrate technology for detection and proteomics of farnesylated proteins."
    Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.
    Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-388.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-62; SER-69 AND SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds HIV-1 Tat and promotes viral transcription."
    Vardabasso C., Manganaro L., Lusic M., Marcello A., Giacca M.
    Retrovirology 5:8-8(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "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 THR-62 AND SER-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-62 AND SER-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNP1L1_HUMAN
AccessioniPrimary (citable) accession number: P55209
Secondary accession number(s): B3KNT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 135 of the entry and version 1 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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