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Q14978

- NOLC1_HUMAN

UniProt

Q14978 - NOLC1_HUMAN

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Protein
Nucleolar and coiled-body phosphoprotein 1
Gene
NOLC1, KIAA0035, NS5ATP13
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. cell cycle Source: ProtInc
  2. mitotic nuclear division Source: ProtInc
  3. nucleolus organization Source: Ensembl
  4. rRNA processing Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolar and coiled-body phosphoprotein 1
Alternative name(s):
140 kDa nucleolar phosphoprotein
Short name:
Nopp140
Hepatitis C virus NS5A-transactivated protein 13
Short name:
HCV NS5A-transactivated protein 13
Nucleolar 130 kDa protein
Nucleolar phosphoprotein p130
Gene namesi
Name:NOLC1
Synonyms:KIAA0035, NS5ATP13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:15608. NOLC1.

Subcellular locationi

Nucleusnucleolus. Cytoplasm
Note: Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase.

GO - Cellular componenti

  1. Cajal body Source: Ensembl
  2. cytoplasm Source: ProtInc
  3. nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31679.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 699699Nucleolar and coiled-body phosphoprotein 1
PRO_0000096942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331N6-acetyllysine1 Publication
Modified residuei87 – 871Phosphoserine1 Publication
Modified residuei90 – 901Phosphoserine1 Publication
Modified residuei91 – 911Phosphoserine1 Publication
Modified residuei366 – 3661Phosphoserine1 Publication
Modified residuei397 – 3971Phosphoserine2 Publications
Modified residuei415 – 4151N6-acetyllysine1 Publication
Modified residuei508 – 5081Phosphoserine3 Publications
Modified residuei538 – 5381Phosphoserine4 Publications
Modified residuei563 – 5631Phosphoserine3 Publications
Modified residuei580 – 5801Phosphoserine2 Publications
Modified residuei582 – 5821Phosphoserine2 Publications
Modified residuei607 – 6071Phosphothreonine3 Publications
Modified residuei610 – 6101Phosphothreonine3 Publications
Modified residuei622 – 6221Phosphoserine1 Publication
Modified residuei643 – 6431Phosphoserine4 Publications
Modified residuei663 – 6631N6-acetyllysine1 Publication
Modified residuei686 – 6861Phosphoserine1 Publication
Modified residuei698 – 6981Phosphoserine6 Publications

Post-translational modificationi

Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. There is evidence suggesting that CDK1 kinase phosphorylates p130 at the M-phase.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14978.
PaxDbiQ14978.
PRIDEiQ14978.

PTM databases

PhosphoSiteiQ14978.

Expressioni

Gene expression databases

ArrayExpressiQ14978.
BgeeiQ14978.
CleanExiHS_NOLC1.
GenevestigatoriQ14978.

Organism-specific databases

HPAiHPA037366.
HPA050388.

Interactioni

Subunit structurei

Interacts with RNA polymerase I 194 kDa subunit (RPA194) and with casein kinase-II.

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494073EBI-396155,EBI-743313
ARRB2P321213EBI-396155,EBI-714559
gagP045912EBI-396155,EBI-6179719From a different organism.

Protein-protein interaction databases

BioGridi114654. 59 interactions.
IntActiQ14978. 13 interactions.
MINTiMINT-111465.
STRINGi9606.ENSP00000359024.

Structurei

3D structure databases

ProteinModelPortaliQ14978.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 4233LisH
Add
BLAST
Repeati84 – 9512Acidic serine cluster 1
Add
BLAST
Repeati125 – 13612Acidic serine cluster 2
Add
BLAST
Repeati167 – 17812Acidic serine cluster 3
Add
BLAST
Repeati221 – 23212Acidic serine cluster 4
Add
BLAST
Repeati264 – 27512Acidic serine cluster 5
Add
BLAST
Repeati325 – 33612Acidic serine cluster 6
Add
BLAST
Repeati363 – 37513Acidic serine cluster 7
Add
BLAST
Repeati425 – 43612Acidic serine cluster 8
Add
BLAST
Repeati470 – 48112Acidic serine cluster 9
Add
BLAST
Repeati519 – 52911Acidic serine cluster 10
Add
BLAST
Repeati555 – 56612Acidic serine cluster 11
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 56648311 X 12 AA approximate repeats of an acidic serine cluster
Add
BLAST
Regioni204 – 382179Interacts with RPA194
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi68 – 8215Nuclear localization signal Reviewed prediction
Add
BLAST
Motifi384 – 587204Nuclear localization signal Reviewed prediction
Add
BLAST
Motifi601 – 61717Nuclear localization signal Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 1 LisH domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG318801.
HOGENOMiHOG000113823.
HOVERGENiHBG075370.
OMAiMSIIQDL.
OrthoDBiEOG7GTT6H.
PhylomeDBiQ14978.
TreeFamiTF341730.

Family and domain databases

InterProiIPR006594. LisH_dimerisation.
IPR007718. SRP40_C.
[Graphical view]
PfamiPF05022. SRP40_C. 1 hit.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: Q14978-1) [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

MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL    50
LDIYSFWLKS AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP 100
PAKKAAVPAK RVGLPPGKAA AKASESSSSE ESSDDDDEED QKKQPVQKGV 150
KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP KNQKPKITPV TVKAQTKAPP 200
KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK KTVPKKQVVA 250
KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS SVPPPSAPPP 300
KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT 350
KPPPAKKAAE SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV 400
KPAAAPKQPV GGGQKLLTRK ADSSSSEEES SSSEEEKTKK MVATTKPKAT 450
AKAALSLPAK QAPQGSRDSS SDSDSSSSEE EEEKTSKSAV KKKPQKVAGG 500
AAPSKPASAK KGKAESSNSS SSDDSSEEEE EKLKGKGSPR PQAPKANGTS 550
ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE AAKEAETPQA 600
KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA 650
AGDWGERANQ VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE 699
Length:699
Mass (Da):73,603
Last modified:April 17, 2007 - v2
Checksum:i7C5C4F25677E2E61
GO
Isoform Beta (identifier: Q14978-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     241-241: K → KVWTITSVRAE

Show »
Length:709
Mass (Da):74,747
Checksum:i5A02742A231255AB
GO
Isoform 3 (identifier: Q14978-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-59: LK → LNR

Show »
Length:700
Mass (Da):73,745
Checksum:i5F8699563FBA24A9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti412 – 4121G → V.
Corresponds to variant rs11191224 [ dbSNP | Ensembl ].
VAR_031677
Natural varianti456 – 4561S → P.1 Publication
Corresponds to variant rs1049455 [ dbSNP | Ensembl ].
VAR_031678

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 592LK → LNR in isoform 3.
VSP_035415
Alternative sequencei241 – 2411K → KVWTITSVRAE in isoform Beta.
VSP_004338

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31D → A in BAA04803. 1 Publication
Sequence conflicti133 – 1331S → R in CAA84063. 1 Publication
Sequence conflicti291 – 2922SV → YA in CAA84063. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z34289 mRNA. Translation: CAA84063.1.
AY820769 mRNA. Translation: AAV67777.1.
AL500527 Genomic DNA. Translation: CAH72220.1.
CH471066 Genomic DNA. Translation: EAW49714.1.
CH471066 Genomic DNA. Translation: EAW49715.1.
BC001883 mRNA. Translation: AAH01883.1.
D21262 mRNA. Translation: BAA04803.1.
CCDSiCCDS65925.1. [Q14978-3]
CCDS65926.1. [Q14978-2]
CCDS7530.1. [Q14978-1]
PIRiI38073.
RefSeqiNP_001271317.1. NM_001284388.1. [Q14978-2]
NP_001271318.1. NM_001284389.1. [Q14978-3]
NP_004732.2. NM_004741.4. [Q14978-1]
UniGeneiHs.523238.

Genome annotation databases

EnsembliENST00000405356; ENSP00000385410; ENSG00000166197. [Q14978-2]
ENST00000488254; ENSP00000475080; ENSG00000166197. [Q14978-3]
ENST00000605788; ENSP00000474710; ENSG00000166197. [Q14978-1]
GeneIDi9221.
KEGGihsa:9221.
UCSCiuc001kuo.2. human. [Q14978-1]
uc001kup.2. human. [Q14978-2]
uc001kuq.2. human. [Q14978-3]

Polymorphism databases

DMDMi145559503.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z34289 mRNA. Translation: CAA84063.1 .
AY820769 mRNA. Translation: AAV67777.1 .
AL500527 Genomic DNA. Translation: CAH72220.1 .
CH471066 Genomic DNA. Translation: EAW49714.1 .
CH471066 Genomic DNA. Translation: EAW49715.1 .
BC001883 mRNA. Translation: AAH01883.1 .
D21262 mRNA. Translation: BAA04803.1 .
CCDSi CCDS65925.1. [Q14978-3 ]
CCDS65926.1. [Q14978-2 ]
CCDS7530.1. [Q14978-1 ]
PIRi I38073.
RefSeqi NP_001271317.1. NM_001284388.1. [Q14978-2 ]
NP_001271318.1. NM_001284389.1. [Q14978-3 ]
NP_004732.2. NM_004741.4. [Q14978-1 ]
UniGenei Hs.523238.

3D structure databases

ProteinModelPortali Q14978.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114654. 59 interactions.
IntActi Q14978. 13 interactions.
MINTi MINT-111465.
STRINGi 9606.ENSP00000359024.

PTM databases

PhosphoSitei Q14978.

Polymorphism databases

DMDMi 145559503.

Proteomic databases

MaxQBi Q14978.
PaxDbi Q14978.
PRIDEi Q14978.

Protocols and materials databases

DNASUi 9221.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000405356 ; ENSP00000385410 ; ENSG00000166197 . [Q14978-2 ]
ENST00000488254 ; ENSP00000475080 ; ENSG00000166197 . [Q14978-3 ]
ENST00000605788 ; ENSP00000474710 ; ENSG00000166197 . [Q14978-1 ]
GeneIDi 9221.
KEGGi hsa:9221.
UCSCi uc001kuo.2. human. [Q14978-1 ]
uc001kup.2. human. [Q14978-2 ]
uc001kuq.2. human. [Q14978-3 ]

Organism-specific databases

CTDi 9221.
GeneCardsi GC10P103902.
H-InvDB HIX0009150.
HGNCi HGNC:15608. NOLC1.
HPAi HPA037366.
HPA050388.
MIMi 602394. gene.
neXtProti NX_Q14978.
PharmGKBi PA31679.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG318801.
HOGENOMi HOG000113823.
HOVERGENi HBG075370.
OMAi MSIIQDL.
OrthoDBi EOG7GTT6H.
PhylomeDBi Q14978.
TreeFami TF341730.

Miscellaneous databases

ChiTaRSi NOLC1. human.
GeneWikii Nucleolar_phosphoprotein_p130.
GenomeRNAii 9221.
NextBioi 34571.
PROi Q14978.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14978.
Bgeei Q14978.
CleanExi HS_NOLC1.
Genevestigatori Q14978.

Family and domain databases

InterProi IPR006594. LisH_dimerisation.
IPR007718. SRP40_C.
[Graphical view ]
Pfami PF05022. SRP40_C. 1 hit.
[Graphical view ]
SMARTi SM00667. LisH. 1 hit.
[Graphical view ]
PROSITEi PS50896. LISH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis."
    Pai C.-Y., Chen H.-K., Sheu H.-L., Yeh N.-H.
    J. Cell Sci. 108:1911-1920(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    Tissue: Leukemia.
  2. Ying Z.L., Hong D., Jun C.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 3).
    Tissue: Lung.
  6. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-699 (ISOFORM BETA), VARIANT PRO-456.
    Tissue: Bone marrow.
  7. "Cell proliferation-dependent expression of two isoforms of the nucleolar phosphoprotein p130."
    Pai C.-Y., Yeh N.-H.
    Biochem. Biophys. Res. Commun. 221:581-587(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  8. "The nucleolar phosphoprotein P130 is a GTPase/ATPase with intrinsic property to form large complexes triggered by F- and Mg2+."
    Chen H.-K., Yeh N.-H.
    Biochem. Biophys. Res. Commun. 230:370-375(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Human Nopp140, which interacts with RNA polymerase I: implications for rRNA gene transcription and nucleolar structural organization."
    Chen H.-K., Pai C.-Y., Huang J.-Y., Yeh N.-H.
    Mol. Cell. Biol. 19:8536-8546(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-538; SER-563 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-607; THR-610; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508; SER-538; THR-607; THR-610 AND SER-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-90; SER-91; SER-366; SER-508; SER-580; SER-582; SER-686 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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; LYS-415 AND LYS-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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 SER-397; SER-508; SER-538; SER-563; SER-580; SER-582; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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 SER-397; SER-538; SER-622; SER-643 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNOLC1_HUMAN
AccessioniPrimary (citable) accession number: Q14978
Secondary accession number(s): Q15030, Q5VV70, Q9BUV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 17, 2007
Last modified: September 3, 2014
This is version 140 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 10
    Human chromosome 10: 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

External Data

Dasty 3

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