O75717 (WDHD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
WD repeat and HMG-box DNA-binding protein 1

Alternative name(s):
Acidic nucleoplasmic DNA-binding protein 1
Short name=And-1

Gene names

Name:	WDHD1
Synonyms:	AND1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1129 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Ref.9
Subunit structure	Interacts with the polymerase alpha catalytic subunit POLA1. Interacts with MCM10. Ref.5
Subcellular location	Nucleus › nucleoplasm By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10
Sequence similarities	Contains 1 HMG box DNA-binding domain. Contains 7 WD repeats.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat WD repeat
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Traceable author statement. Source: ProtInc nucleoplasm Traceable author statement. Source: ProtInc
Molecular function	DNA binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1129

1129

WD repeat and HMG-box DNA-binding protein 1

PRO_0000051338

Regions

Repeat

11 – 50

40

WD 1

Repeat

52 – 91

40

WD 2

Repeat

92 – 131

40

WD 3

Repeat

134 – 173

40

WD 4

Repeat

184 – 223

40

WD 5

Repeat

228 – 267

40

WD 6

Repeat

271 – 310

40

WD 7

DNA binding

1016 – 1079

64

HMG box

Compositional bias

829 – 836

8

Glu-rich (acidic)

Compositional bias

862 – 878

17

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

333

1

Phosphoserine Ref.7 Ref.10

Modified residue

374

1

Phosphoserine Ref.4 Ref.10

Modified residue

383

1

Phosphoserine Ref.4 Ref.7 Ref.10

Modified residue

387

1

Phosphoserine Ref.7

Modified residue

826

1

Phosphothreonine Ref.6

Modified residue

868

1

Phosphoserine Ref.4 Ref.7 Ref.8

Modified residue

962

1

N6-acetyllysine Ref.11

Modified residue

1041

1

Phosphoserine Ref.3

Modified residue

1090

1

Phosphoserine Ref.7

Modified residue

1127

1

N6-acetyllysine Ref.11

Natural variations

Natural variant

338

1

F → L.
Corresponds to variant rs8020032 [ dbSNP | Ensembl ].

VAR_053422

Natural variant

411

1

L → P.
Corresponds to variant rs17128116 [ dbSNP | Ensembl ].

VAR_053423

Natural variant

1102

1

E → K.
Corresponds to variant rs41309252 [ dbSNP | Ensembl ].

VAR_062100

Experimental info

Sequence conflict

612

1

Q → K in AAH43349. Ref.2

Sequence conflict

612

1

Q → K in AAH00622. Ref.2

Sequence conflict

613

1

I → K in AAH00622. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

1129

Helix Strand Turn

Details...

Helix

1021 – 1036

16

Helix

1043 – 1054

12

Beta strand

1055 – 1057

3

Helix

1059 – 1068

10

Beta strand

1071 – 1076

6

Helix

1081 – 1083

3

Sequences

	Sequence		Length	Mass (Da)
	O75717 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: DD3E3613CA6AE70A	FASTA	1,129	125,967
	10 20 30 40 50 60 MPATRKPMRY GHTEGHTEVC FDDSGSFIVT CGSDGDVRIW EDLDDDDPKF INVGEKAYSC 70 80 90 100 110 120 ALKSGKLVTA VSNNTIQVHT FPEGVPDGIL TRFTTNANHV VFNGDGTKIA AGSSDFLVKI 130 140 150 160 170 180 VDVMDSSQQK TFRGHDAPVL SLSFDPKDIF LASASCDGSV RVWQISDQTC AISWPLLQKC 190 200 210 220 230 240 NDVINAKSIC RLAWQPKSGK LLAIPVEKSV KLYRRESWSH QFDLSDNFIS QTLNIVTWSP 250 260 270 280 290 300 CGQYLAAGSI NGLIIVWNVE TKDCMERVKH EKGYAICGLA WHPTCGRISY TDAEGNLGLL 310 320 330 340 350 360 ENVCDPSGKT SSSKVSSRVE KDYNDLFDGD DMSNAGDFLN DNAVEIPSFS KGIINDDEDD 370 380 390 400 410 420 EDLMMASGRP RQRSHILEDD ENSVDISMLK TGSSLLKEEE EDGQEGSIHN LPLVTSQRPF 430 440 450 460 470 480 YDGPMPTPRQ KPFQSGSTPL HLTHRFMVWN SIGIIRCYND EQDNAIDVEF HDTSIHHATH 490 500 510 520 530 540 LSNTLNYTIA DLSHEAILLA CESTDELASK LHCLHFSSWD SSKEWIIDLP QNEDIEAICL 550 560 570 580 590 600 GQGWAAAATS ALLLRLFTIG GVQKEVFSLA GPVVSMAGHG EQLFIVYHRG TGFDGDQCLG 610 620 630 640 650 660 VQLLELGKKK KQILHGDPLP LTRKSYLAWI GFSAEGTPCY VDSEGIVRML NRGLGNTWTP 670 680 690 700 710 720 ICNTREHCKG KSDHYWVVGI HENPQQLRCI PCKGSRFPPT LPRPAVAILS FKLPYCQIAT 730 740 750 760 770 780 EKGQMEEQFW RSVIFHNHLD YLAKNGYEYE ESTKNQATKE QQELLMKMLA LSCKLEREFR 790 800 810 820 830 840 CVELADLMTQ NAVNLAIKYA SRSRKLILAQ KLSELAVEKA AELTATQVEE EEEEEDFRKK 850 860 870 880 890 900 LNAGYSNTAT EWSQPRFRNQ VEEDAEDSGE ADDEEKPEIH KPGQNSFSKS TNSSDVSAKS 910 920 930 940 950 960 GAVTFSSQGR VNPFKVSASS KEPAMSMNSA RSTNILDNMG KSSKKSTALS RTTNNEKSPI 970 980 990 1000 1010 1020 IKPLIPKPKP KQASAASYFQ KRNSQTNKTE EVKEENLKNV LSETPAICPP QNTENQRPKT 1030 1040 1050 1060 1070 1080 GFQMWLEENR SNILSDNPDF SDEADIIKEG MIRFRVLSTE ERKVWANKAK GETASEGTEA 1090 1100 1110 1120 KKRKRVVDES DETENQEEKA KENLNLSKKQ KPLDFSTNQK LSAFAFKQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Koehler A. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver, Skin and Uterus.
[3]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-383 AND SER-868, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Mcm10 and And-1/CTF4 recruit DNA polymerase alpha to chromatin for initiation of DNA replication." Zhu W., Ukomadu C., Jha S., Senga T., Dhar S.K., Wohlschlegel J.A., Nutt L.K., Kornbluth S., Dutta A. Genes Dev. 21:2288-2299(2007) [PubMed: 17761813] [Abstract] Cited for: INTERACTION WITH POLA1 AND MCM10.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-826, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-383; SER-387; SER-868 AND SER-1090, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-868, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Assembly of the Cdc45-Mcm2-7-GINS complex in human cells requires the Ctf4/And-1, RecQL4, and Mcm10 proteins." Im J.S., Ki S.H., Farina A., Jung D.S., Hurwitz J., Lee J.K. Proc. Natl. Acad. Sci. U.S.A. 106:15628-15632(2009) [PubMed: 19805216] [Abstract] Cited for: FUNCTION.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-374 AND SER-383, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-962 AND LYS-1127, MASS SPECTROMETRY.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Solution structure of the HMG box domain from human WD repeat and HMG-box DNA binding protein 1." RIKEN structural genomics initiative (RSGI) Submitted (MAY-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1017-1084.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ006266 mRNA. Translation: CAA06932.1.
BC000622 mRNA. Translation: AAH00622.1.
BC043349 mRNA. Translation: AAH43349.1.
BC063041 mRNA. Translation: AAH63041.1.

IPI

IPI00411614.

RefSeq

NP_001008397.1. NM_001008396.2.
NP_009017.1. NM_007086.3.

UniGene

Hs.385998.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D7L	NMR	-	A	1017-1084	[»]

ProteinModelPortal

O75717.

SMR

O75717. Positions 8-302, 1017-1084.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75717. 1 interaction.

STRING

O75717.

PTM databases

PhosphoSite

O75717.

Proteomic databases

PRIDE

O75717.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360586; ENSP00000353793; ENSG00000198554.

GeneID

11169.

KEGG

hsa:11169.

UCSC

uc001xbm.1. human.

Organism-specific databases

CTD

11169.

GeneCards

GC14M055405.

H-InvDB

HIX0011678.

HGNC

HGNC:23170. WDHD1.

HPA

HPA001122.

MIM

608126. gene.

neXtProt

NX_O75717.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11908.

HOGENOM

HBG357300.

HOVERGEN

HBG074190.

InParanoid

O75717.

OMA

DNFISQT.

OrthoDB

EOG4W6NV9.

PhylomeDB

O75717.

Gene expression databases

ArrayExpress

O75717.

Bgee

O75717.

CleanEx

HS_WDHD1.

Genevestigator

O75717.

GermOnline

ENSG00000198554. Homo sapiens.

Family and domain databases

InterPro

IPR022100. DUF3639.
IPR000910. HMG_HMG1/HMG2.
IPR009071. HMG_superfamily.
IPR013979. TIF2A_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]

Gene3D

G3DSA:1.10.30.10. HMG-box. 1 hit.
G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.

KO

K11274.

Pfam

PF12341. DUF3639. 1 hit.
PF08662. eIF2A. 1 hit.
PF00505. HMG_box. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]

SMART

SM00398. HMG. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]

SUPFAM

SSF47095. HMG-box. 1 hit.
SSF50978. WD40_like. 1 hit.

PROSITE

PS50118. HMG_BOX_2. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

42497.

SOURCE

Search...

Entry information

Entry name

WDHD1_HUMAN

Accession

Primary (citable) accession number: O75717

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2003
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.