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Q8NHV4 (NEDD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein NEDD1
Alternative name(s):
Neural precursor cell expressed developmentally down-regulated protein 1
Short name=NEDD-1
Gene names
Name:NEDD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. Ref.5 Ref.9

Subunit structure

Interacts with FAM29A and gamma-tubulin. Ref.5

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.5.

Post-translational modification

During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637. Phosphorylated NEDD1 can interact with gamma-tubulin for targeting the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Ref.9

Sequence similarities

Contains 8 WD repeats.

Sequence caution

The sequence AAH27605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NHV4-1)

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.
Isoform 2 (identifier: Q8NHV4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8NHV4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHFTGAVM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Protein NEDD1
PRO_0000051095

Regions

Repeat1 – 3131WD 1
Repeat32 – 7140WD 2
Repeat75 – 11440WD 3
Repeat117 – 15640WD 4
Repeat160 – 20041WD 5
Repeat204 – 24441WD 6
Repeat246 – 28540WD 7
Repeat289 – 33244WD 8

Amino acid modifications

Modified residue3821Phosphothreonine; by PLK1 Ref.9
Modified residue3971Phosphoserine; by PLK1 Ref.9
Modified residue4111Phosphoserine Ref.6
Modified residue4261Phosphoserine; by PLK1 Ref.9
Modified residue5161Phosphoserine Ref.7 Ref.10
Modified residue5501Phosphothreonine; by CDK1 Ref.9
Modified residue6371Phosphoserine; by PLK1 Ref.9

Natural variations

Alternative sequence1 – 8989Missing in isoform 2.
VSP_043411
Alternative sequence11M → MHFTGAVM in isoform 3.
VSP_053794

Experimental info

Sequence conflict1701Y → C in BAC04099. Ref.1
Sequence conflict4091M → V in BAC04099. Ref.1
Sequence conflict6491L → P in BAC04099. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 12817A567C13098B

FASTA66071,966
        10         20         30         40         50         60 
MQENLRFASS GDDIKIWDAS SMTLVDKFNP HTSPHGISSI CWSSNNNFLV TASSSGDKIV 

        70         80         90        100        110        120 
VSSCKCKPVP LLELAEGQKQ TCVNLNSTSM YLVSGGLNNT VNIWDLKSKR VHRSLKDHKD 

       130        140        150        160        170        180 
QVTCVTYNWN DCYIASGSLS GEIILHSVTT NLSSTPFGHG SNQSVRHLKY SLFKKSLLGS 

       190        200        210        220        230        240 
VSDNGIVTLW DVNSQSPYHN FDSVHKAPAS GICFSPVNEL LFVTIGLDKR IILYDTSSKK 

       250        260        270        280        290        300 
LVKTLVADTP LTAVDFMPDG ATLAIGSSRG KIYQYDLRML KSPVKTISAH KTSVQCIAFQ 

       310        320        330        340        350        360 
YSTVLTKSSL NKGCSNKPTT VNKRSVNVNA ASGGVQNSGI VREAPATSIA TVLPQPMTSA 

       370        380        390        400        410        420 
MGKGTVAVQE KAGLPRSINT DTLSKETDSG KNQDFSSFDD TGKSSLGDMF SPIRDDAVVN 

       430        440        450        460        470        480 
KGSDESIGKG DGFDFLPQLN SVFPPRKNPV TSSTSVLHSS PLNVFMGSPG KEENENRDLT 

       490        500        510        520        530        540 
AESKKIYMGK QESKDSFKQL AKLVTSGAES GNLNTSPSSN QTRNSEKFEK PENEIEAQLI 

       550        560        570        580        590        600 
CEPPINGSST PNPKIASSVT AGVASSLSEK IADSIGNNRQ NAPLTSIQIR FIQNMIQETL 

       610        620        630        640        650        660 
DDFREACHRD IVNLQVEMIK QFHMQLNEMH SLLERYSVNE GLVAEIERLR EENKRLRAHF 

« Hide

Isoform 2 [UniParc].

Checksum: 1FBE4E895B36789B
Show »

FASTA57162,379
Isoform 3 [UniParc].

Checksum: CD60E653689DF81A
Show »

FASTA66772,710

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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 2).
Tissue: Testis, Thymus and Tongue.
[2]"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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Testis.
[5]"FAM29A promotes microtubule amplification via recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle."
Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G.
J. Cell Biol. 183:835-848(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAM29A, SUBCELLULAR LOCATION, FUNCTION.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
[9]"Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for targeting of the gammaTuRC to the centrosome."
Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C.
J. Cell Sci. 122:2240-2251(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-550 BY CDK1, PHOSPHORYLATION AT THR-382; SER-397; SER-426 AND SER-637 BY PLK1.
[10]"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-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK093221 mRNA. Translation: BAC04099.1.
AK303656 mRNA. Translation: BAG64657.1.
AK315821 mRNA. Translation: BAF98712.1.
AC007564 Genomic DNA. No translation available.
AC013417 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97577.1.
CH471054 Genomic DNA. Translation: EAW97579.1.
CH471054 Genomic DNA. Translation: EAW97580.1.
BC027605 mRNA. Translation: AAH27605.1. Different initiation.
CCDSCCDS44956.1. [Q8NHV4-2]
CCDS9063.1. [Q8NHV4-1]
RefSeqNP_001128647.1. NM_001135175.1. [Q8NHV4-3]
NP_001128648.1. NM_001135176.1. [Q8NHV4-1]
NP_001128649.1. NM_001135177.1. [Q8NHV4-2]
NP_690869.1. NM_152905.3. [Q8NHV4-1]
XP_005268701.1. XM_005268644.1. [Q8NHV4-3]
XP_006719299.1. XM_006719236.1. [Q8NHV4-1]
XP_006719300.1. XM_006719237.1. [Q8NHV4-2]
UniGeneHs.270084.

3D structure databases

ProteinModelPortalQ8NHV4.
SMRQ8NHV4. Positions 7-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125728. 13 interactions.
DIPDIP-48838N.
IntActQ8NHV4. 6 interactions.
STRING9606.ENSP00000407964.

PTM databases

PhosphoSiteQ8NHV4.

Polymorphism databases

DMDM74762597.

Proteomic databases

MaxQBQ8NHV4.
PaxDbQ8NHV4.
PRIDEQ8NHV4.

Protocols and materials databases

DNASU121441.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266742; ENSP00000266742; ENSG00000139350. [Q8NHV4-1]
ENST00000411739; ENSP00000411307; ENSG00000139350. [Q8NHV4-2]
ENST00000429527; ENSP00000404978; ENSG00000139350. [Q8NHV4-1]
ENST00000457368; ENSP00000407964; ENSG00000139350. [Q8NHV4-2]
ENST00000557644; ENSP00000451211; ENSG00000139350.
GeneID121441.
KEGGhsa:121441.
UCSCuc001teu.4. human. [Q8NHV4-1]
uc001tew.3. human.

Organism-specific databases

CTD121441.
GeneCardsGC12P097301.
HGNCHGNC:7723. NEDD1.
HPAHPA038591.
MIM600372. gene.
neXtProtNX_Q8NHV4.
PharmGKBPA31531.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000034642.
HOVERGENHBG055623.
InParanoidQ8NHV4.
KOK16547.
OMAVFPPRKT.
OrthoDBEOG79KPDX.
PhylomeDBQ8NHV4.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
SignaLinkQ8NHV4.

Gene expression databases

ArrayExpressQ8NHV4.
BgeeQ8NHV4.
CleanExHS_NEDD1.
GenevestigatorQ8NHV4.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 3 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNEDD1.
GenomeRNAi121441.
NextBio80736.
PROQ8NHV4.
SOURCESearch...

Entry information

Entry nameNEDD1_HUMAN
AccessionPrimary (citable) accession number: Q8NHV4
Secondary accession number(s): B0AZN0 expand/collapse secondary AC list , B4E145, G3V3F1, Q8NA30
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM