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Q9Y266

- NUDC_HUMAN

UniProt

Q9Y266 - NUDC_HUMAN

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Protein

Nuclear migration protein nudC

Gene

NUDC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation.By similarity2 Publications

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. mitotic cell cycle Source: Reactome
  3. mitotic nuclear division Source: UniProtKB-KW
  4. multicellular organismal development Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1932. Mitotic Telophase/Cytokinesis.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear migration protein nudC
Alternative name(s):
Nuclear distribution protein C homolog
Gene namesi
Name:NUDC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8045. NUDC.

Subcellular locationi

Cytoplasmcytoskeleton. Nucleus
Note: In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells. A small proportion is nuclear, in a punctate pattern.

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: Reactome
  3. microtubule Source: UniProtKB-KW
  4. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi274 – 2741S → A: Abolishes phosphorylation by PLK1; when associated with A-326. 1 Publication
Mutagenesisi326 – 3261S → A: Abolishes phosphorylation by PLK1; when associated with A-274. 1 Publication

Organism-specific databases

PharmGKBiPA31827.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Nuclear migration protein nudCPRO_0000057990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Phosphothreonine1 Publication
Modified residuei139 – 1391Phosphoserine4 Publications
Modified residuei145 – 1451Phosphothreonine4 Publications
Modified residuei239 – 2391N6-acetyllysine1 Publication
Modified residuei274 – 2741Phosphoserine; by PLK11 Publication
Modified residuei326 – 3261Phosphoserine; by PLK11 Publication

Post-translational modificationi

Reversibly phosphorylated on serine residues during the M phase of the cell cycle. Phosphorylation on Ser-274 and Ser-326 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Phosphorylated by PLK and other kinases.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y266.
PaxDbiQ9Y266.
PeptideAtlasiQ9Y266.
PRIDEiQ9Y266.

PTM databases

PhosphoSiteiQ9Y266.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in fetal liver, kidney, lung and brain. Highly expressed in adult pancreas, kidney, skeletal muscle, liver, lung, placenta, prostate, brain and heart.2 Publications

Inductioni

Up-regulated in actively dividing hematopoietic precursor cells. Up-regulated in cultured erythroleukemia TF-1 cells by granulocyte-macrophage colony-stimulating factor. Strongly down-regulated during maturation of erythroid precursor cells.1 Publication

Gene expression databases

BgeeiQ9Y266.
CleanExiHS_NUDC.
GenevestigatoriQ9Y266.

Organism-specific databases

HPAiHPA027183.
HPA028105.

Interactioni

Subunit structurei

Binds PLK1. Binds PAFAH1B1 (By similarity). Part of a complex containing PLK1, NUDC, dynein and dynactin.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DNAJA2O608842EBI-357298,EBI-352957
FBXW2Q9UKT82EBI-357298,EBI-914727

Protein-protein interaction databases

BioGridi115950. 46 interactions.
IntActiQ9Y266. 90 interactions.
MINTiMINT-1132616.
STRINGi9606.ENSP00000319664.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi173 – 1764
Beta strandi178 – 1869
Helixi195 – 1973
Beta strandi198 – 2036
Beta strandi206 – 2116
Beta strandi217 – 2248
Helixi228 – 2303
Beta strandi232 – 2365
Turni237 – 2393
Beta strandi240 – 25112
Helixi266 – 2683

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QORX-ray1.75A/B/C/D/E158-274[»]
ProteinModelPortaliQ9Y266.
SMRiQ9Y266. Positions 158-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini167 – 25892CSPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili60 – 13475Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi68 – 747Nuclear localization signalSequence Analysis

Sequence similaritiesi

Belongs to the nudC family.Curated
Contains 1 CS domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG292552.
GeneTreeiENSGT00530000063486.
HOGENOMiHOG000182245.
HOVERGENiHBG052690.
InParanoidiQ9Y266.
OMAiLKGHPPV.
OrthoDBiEOG7HQN8G.
PhylomeDBiQ9Y266.
TreeFamiTF300147.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR025934. NudC_N_dom.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF14050. Nudc_N. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y266-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM
60 70 80 90 100
AEKLITQTFS HHNQLAQKTR REKRARQEAE RREKAERAAR LAKEAKSETS
110 120 130 140 150
GPQIKELTDE EAERLQLEID QKKDAENHEA QLKNGSLDSP GKQDTEEDEE
160 170 180 190 200
EDEKDKGKLK PNLGNGADLP NYRWTQTLSE LDLAVPFCVN FRLKGKDMVV
210 220 230 240 250
DIQRRHLRVG LKGQPAIIDG ELYNEVKVEE SSWLIEDGKV VTVHLEKINK
260 270 280 290 300
MEWWSRLVSS DPEINTKKIN PENSKLSDLD SETRSMVEKM MYDQRQKSMG
310 320 330
LPTSDEQKKQ EILKKFMDQH PEMDFSKAKF N
Length:331
Mass (Da):38,243
Last modified:November 1, 1999 - v1
Checksum:i34F591170F7594AF
GO

Sequence cautioni

The sequence BAA76628.1 differs from that shown. Reason: Frameshift at positions 140, 231 and 273.
The sequence CAI13560.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI13563.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191Q → H in BAA76628. 1 PublicationCurated
Sequence conflicti69 – 691T → N in CAB66659. (PubMed:11230166)Curated
Sequence conflicti74 – 741R → I in BAA76628. 1 PublicationCurated
Sequence conflicti111 – 1111E → K in BAA76628. 1 PublicationCurated
Sequence conflicti114 – 1141R → K in BAA76628. 1 PublicationCurated
Sequence conflicti128 – 1281H → P in BAA76628. 1 PublicationCurated
Sequence conflicti149 – 1491E → V in CAB66659. (PubMed:11230166)Curated
Sequence conflicti169 – 1691L → P in CAB66659. (PubMed:11230166)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF130736 mRNA. Translation: AAD30517.1.
AF125465 mRNA. Translation: AAD39921.1.
AF100760 mRNA. Translation: AAD43024.1.
AB019408 mRNA. Translation: BAA76628.1. Frameshift.
AF086922 mRNA. Translation: AAP97152.1.
AL136725 mRNA. Translation: CAB66659.1.
AL356390 Genomic DNA. Translation: CAI13560.1. Sequence problems.
AL356390 Genomic DNA. Translation: CAI13561.1.
AL356390 Genomic DNA. Translation: CAI13563.1. Sequence problems.
BC002399 mRNA. Translation: AAH02399.1.
BC003132 mRNA. Translation: AAH03132.1.
BC006147 mRNA. Translation: AAH06147.1.
BC007280 mRNA. Translation: AAH07280.1.
BC015153 mRNA. Translation: AAH15153.1.
BC021139 mRNA. Translation: AAH21139.1.
CCDSiCCDS292.1.
RefSeqiNP_006591.1. NM_006600.3.
UniGeneiHs.263812.

Genome annotation databases

EnsembliENST00000321265; ENSP00000319664; ENSG00000090273.
GeneIDi10726.
KEGGihsa:10726.
UCSCiuc001bng.2. human.

Polymorphism databases

DMDMi62287138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF130736 mRNA. Translation: AAD30517.1 .
AF125465 mRNA. Translation: AAD39921.1 .
AF100760 mRNA. Translation: AAD43024.1 .
AB019408 mRNA. Translation: BAA76628.1 . Frameshift.
AF086922 mRNA. Translation: AAP97152.1 .
AL136725 mRNA. Translation: CAB66659.1 .
AL356390 Genomic DNA. Translation: CAI13560.1 . Sequence problems.
AL356390 Genomic DNA. Translation: CAI13561.1 .
AL356390 Genomic DNA. Translation: CAI13563.1 . Sequence problems.
BC002399 mRNA. Translation: AAH02399.1 .
BC003132 mRNA. Translation: AAH03132.1 .
BC006147 mRNA. Translation: AAH06147.1 .
BC007280 mRNA. Translation: AAH07280.1 .
BC015153 mRNA. Translation: AAH15153.1 .
BC021139 mRNA. Translation: AAH21139.1 .
CCDSi CCDS292.1.
RefSeqi NP_006591.1. NM_006600.3.
UniGenei Hs.263812.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QOR X-ray 1.75 A/B/C/D/E 158-274 [» ]
ProteinModelPortali Q9Y266.
SMRi Q9Y266. Positions 158-273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115950. 46 interactions.
IntActi Q9Y266. 90 interactions.
MINTi MINT-1132616.
STRINGi 9606.ENSP00000319664.

PTM databases

PhosphoSitei Q9Y266.

Polymorphism databases

DMDMi 62287138.

Proteomic databases

MaxQBi Q9Y266.
PaxDbi Q9Y266.
PeptideAtlasi Q9Y266.
PRIDEi Q9Y266.

Protocols and materials databases

DNASUi 10726.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321265 ; ENSP00000319664 ; ENSG00000090273 .
GeneIDi 10726.
KEGGi hsa:10726.
UCSCi uc001bng.2. human.

Organism-specific databases

CTDi 10726.
GeneCardsi GC01P027226.
HGNCi HGNC:8045. NUDC.
HPAi HPA027183.
HPA028105.
MIMi 610325. gene.
neXtProti NX_Q9Y266.
PharmGKBi PA31827.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292552.
GeneTreei ENSGT00530000063486.
HOGENOMi HOG000182245.
HOVERGENi HBG052690.
InParanoidi Q9Y266.
OMAi LKGHPPV.
OrthoDBi EOG7HQN8G.
PhylomeDBi Q9Y266.
TreeFami TF300147.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1932. Mitotic Telophase/Cytokinesis.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

GeneWikii NUDC.
GenomeRNAii 10726.
NextBioi 40723.
PROi Q9Y266.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y266.
CleanExi HS_NUDC.
Genevestigatori Q9Y266.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR025934. NudC_N_dom.
[Graphical view ]
Pfami PF04969. CS. 1 hit.
PF14050. Nudc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS51203. CS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A homolog of the fungal nuclear migration gene nudC is involved in normal and malignant human hematopoiesis."
    Miller B.A., Zhang M.-Y., Gocke C.D., De Souza C., Osmani A.H., Lynch C., Davies J., Bell L., Osmani S.A.
    Exp. Hematol. 27:742-750(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Heart.
  2. "Molecular cloning and characterization of the human NUDC gene."
    Matsumoto N., Ledbetter D.H.
    Hum. Genet. 104:498-504(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Human MNUDC protein gene."
    Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary.
  4. "Unique genes expressed in fibroblasts of periodontal ligament."
    Yamamoto T., Takashiba S., Myokai F., Washio N., Nishimura F., Arai H., Murayama Y.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Periodontal ligament.
  5. "Cloning and characterization of a novel human cDNA homology to murine SIG-92 mRNA."
    Li N.G., Yu L., Tu Q., Fu Q., Wang X.K., Zhao S.Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  7. "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].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye, Kidney, Lung and Skin.
  9. "A role for Plk1 phosphorylation of NudC in cytokinesis."
    Zhou T., Aumais J.P., Liu X., Yu-Lee L.-Y., Erikson R.L.
    Dev. Cell 5:127-138(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLK1, IDENTIFICATION IN A COMPLEX WITH DYNACTIN AND DYNEIN, MUTAGENESIS OF SER-274 AND SER-326, PHOSPHORYLATION AT SER-274 AND SER-326.
  10. "Role for NudC, a dynein-associated nuclear movement protein, in mitosis and cytokinesis."
    Aumais J.P., Williams S.N., Luo W., Nishino M., Caldwell K.A., Caldwell G.A., Lin S.-H., Yu-Lee L.-Y.
    J. Cell Sci. 116:1991-2003(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  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-139 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  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-239, 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-108; SER-139 AND THR-145, 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 SER-139 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUDC_HUMAN
AccessioniPrimary (citable) accession number: Q9Y266
Secondary accession number(s): Q5QP31
, Q5QP35, Q9H0N2, Q9Y2B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 128 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3