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Protein

WD repeat-containing protein 70

Gene

WDR70

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ9NW82.

Names & Taxonomyi

Protein namesi
Recommended name:
WD repeat-containing protein 70
Gene namesi
Name:WDR70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:25495. WDR70.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670603.

Polymorphism and mutation databases

BioMutaiWDR70.
DMDMi74761752.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654WD repeat-containing protein 70PRO_0000305144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki296 – 296Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei452 – 4521N6-acetyllysineCombined sources
Modified residuei621 – 6211PhosphoserineCombined sources
Modified residuei638 – 6381PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NW82.
MaxQBiQ9NW82.
PaxDbiQ9NW82.
PeptideAtlasiQ9NW82.
PRIDEiQ9NW82.

PTM databases

iPTMnetiQ9NW82.
PhosphoSiteiQ9NW82.

Expressioni

Gene expression databases

BgeeiQ9NW82.
CleanExiHS_WDR70.
ExpressionAtlasiQ9NW82. baseline and differential.
GenevisibleiQ9NW82. HS.

Organism-specific databases

HPAiHPA043064.
HPA048149.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120410. 18 interactions.
IntActiQ9NW82. 8 interactions.
STRINGi9606.ENSP00000265107.

Structurei

3D structure databases

ProteinModelPortaliQ9NW82.
SMRiQ9NW82. Positions 175-502.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati180 – 21940WD 1Add
BLAST
Repeati227 – 26842WD 2Add
BLAST
Repeati281 – 32141WD 3Add
BLAST
Repeati330 – 36940WD 4Add
BLAST
Repeati376 – 41540WD 5Add
BLAST
Repeati421 – 46646WD 6Add
BLAST
Repeati469 – 50840WD 7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi84 – 11330Ser-richAdd
BLAST
Compositional biasi148 – 16417Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat GAD-1 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0772. Eukaryota.
ENOG410XP76. LUCA.
GeneTreeiENSGT00390000015433.
HOGENOMiHOG000172867.
HOVERGENiHBG108671.
InParanoidiQ9NW82.
OMAiNDATVRT.
OrthoDBiEOG7ZKS9Q.
PhylomeDBiQ9NW82.
TreeFamiTF105809.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NW82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERSGPSEVT GSDASGPDPQ LAVTMGFTGF GKKARTFDLE AMFEQTRRTA
60 70 80 90 100
VERSRKTLEA REKEEEMNRE KELRRQNEDI EPTSSRSNVV RDCSKSSSRD
110 120 130 140 150
TSSSESEQSS DSSDDELIGP PLPPKMVGKP VNFMEEDILG PLPPPLNEEE
160 170 180 190 200
EEAEEEEEEE EEEENPVHKI PDSHEITLKH GTKTVSALGL DPSGARLVTG
210 220 230 240 250
GYDYDVKFWD FAGMDASFKA FRSLQPCECH QIKSLQYSNT GDMILVVSGS
260 270 280 290 300
SQAKVIDRDG FEVMECIKGD QYIVDMANTK GHTAMLHTGS WHPKIKGEFM
310 320 330 340 350
TCSNDATVRT WEVENPKKQK SVFKPRTMQG KKVIPTTCTY SRDGNLIAAA
360 370 380 390 400
CQNGSIQIWD RNLTVHPKFH YKQAHDSGTD TSCVTFSYDG NVLASRGGDD
410 420 430 440 450
SLKLWDIRQF NKPLFSASGL PTMFPMTDCC FSPDDKLIVT GTSIQRGCGS
460 470 480 490 500
GKLVFFERRT FQRVYEIDIT DASVVRCLWH PKLNQIMVGT GNGLAKVYYD
510 520 530 540 550
PNKSQRGAKL CVVKTQRKAK QAETLTQDYI ITPHALPMFR EPRQRSTRKQ
560 570 580 590 600
LEKDRLDPLK SHKPEPPVAG PGRGGRVGTH GGTLSSYIVK NIALDKTDDS
610 620 630 640 650
NPREAILRHA KAAEDSPYWV SPAYSKTQPK TMFAQVESDD EEAKNEPEWK

KRKI
Length:654
Mass (Da):73,201
Last modified:October 1, 2000 - v1
Checksum:i5AE0E1B43A5B8E18
GO

Sequence cautioni

The sequence CAC21644.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001095 mRNA. Translation: BAA91502.1.
AL512685 mRNA. Translation: CAC21644.1. Different initiation.
BC009648 mRNA. Translation: AAH09648.1.
BC025315 mRNA. Translation: AAH25315.1.
CCDSiCCDS34147.1.
RefSeqiNP_060504.1. NM_018034.2.
UniGeneiHs.213690.

Genome annotation databases

EnsembliENST00000265107; ENSP00000265107; ENSG00000082068.
GeneIDi55100.
KEGGihsa:55100.
UCSCiuc003jkv.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001095 mRNA. Translation: BAA91502.1.
AL512685 mRNA. Translation: CAC21644.1. Different initiation.
BC009648 mRNA. Translation: AAH09648.1.
BC025315 mRNA. Translation: AAH25315.1.
CCDSiCCDS34147.1.
RefSeqiNP_060504.1. NM_018034.2.
UniGeneiHs.213690.

3D structure databases

ProteinModelPortaliQ9NW82.
SMRiQ9NW82. Positions 175-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120410. 18 interactions.
IntActiQ9NW82. 8 interactions.
STRINGi9606.ENSP00000265107.

PTM databases

iPTMnetiQ9NW82.
PhosphoSiteiQ9NW82.

Polymorphism and mutation databases

BioMutaiWDR70.
DMDMi74761752.

Proteomic databases

EPDiQ9NW82.
MaxQBiQ9NW82.
PaxDbiQ9NW82.
PeptideAtlasiQ9NW82.
PRIDEiQ9NW82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265107; ENSP00000265107; ENSG00000082068.
GeneIDi55100.
KEGGihsa:55100.
UCSCiuc003jkv.4. human.

Organism-specific databases

CTDi55100.
GeneCardsiWDR70.
H-InvDBHIX0004772.
HIX0004821.
HGNCiHGNC:25495. WDR70.
HPAiHPA043064.
HPA048149.
neXtProtiNX_Q9NW82.
PharmGKBiPA142670603.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0772. Eukaryota.
ENOG410XP76. LUCA.
GeneTreeiENSGT00390000015433.
HOGENOMiHOG000172867.
HOVERGENiHBG108671.
InParanoidiQ9NW82.
OMAiNDATVRT.
OrthoDBiEOG7ZKS9Q.
PhylomeDBiQ9NW82.
TreeFamiTF105809.

Enzyme and pathway databases

SignaLinkiQ9NW82.

Miscellaneous databases

ChiTaRSiWDR70. human.
GenomeRNAii55100.
NextBioi58689.
PROiQ9NW82.

Gene expression databases

BgeeiQ9NW82.
CleanExiHS_WDR70.
ExpressionAtlasiQ9NW82. baseline and differential.
GenevisibleiQ9NW82. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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].
    Tissue: Embryo.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "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: Brain and Placenta.
  4. "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-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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 SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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].
  7. "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-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiWDR70_HUMAN
AccessioniPrimary (citable) accession number: Q9NW82
Secondary accession number(s): Q9H053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 123 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.