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P55209

- NP1L1_HUMAN

UniProt

P55209 - NP1L1_HUMAN

Protein

Nucleosome assembly protein 1-like 1

Gene

NAP1L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

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

    GO - Cellular componenti

    1. melanosome Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB
    3. nucleus Source: UniProtKB-SubCell

    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 1PRO_0000185652Add
    BLAST
    Propeptidei389 – 3913Removed in mature formCuratedPRO_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 esterCurated
    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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi273 – 2797Nuclear localization signalSequence Analysis

    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. 1 PublicationVSP_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. [P55209-1]
    ENST00000393263; ENSP00000376947; ENSG00000187109. [P55209-1]
    ENST00000549596; ENSP00000447793; ENSG00000187109. [P55209-2]
    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 . [P55209-1 ]
    ENST00000393263 ; ENSP00000376947 ; ENSG00000187109 . [P55209-1 ]
    ENST00000549596 ; ENSP00000447793 ; ENSG00000187109 . [P55209-2 ]
    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

    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: October 1, 2014
    This is version 136 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