Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chromodomain-helicase-DNA-binding protein 4

Gene

Chd4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri363 – 41048PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri442 – 48948PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi744 – 7518ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-6804758. Regulation of TP53 Activity through Acetylation.
R-MMU-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein 4 (EC:3.6.4.12)
Short name:
CHD-4
Gene namesi
Name:Chd4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1344380. Chd4.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • membrane Source: MGI
  • nuclear chromatin Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • NuRD complex Source: MGI
  • protein complex Source: MGI
  • protein-DNA complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19151915Chromodomain-helicase-DNA-binding protein 4PRO_0000080229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei301 – 3011PhosphoserineCombined sources
Modified residuei302 – 3021PhosphoserineCombined sources
Modified residuei303 – 3031PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei360 – 3601PhosphothreonineBy similarity
Modified residuei421 – 4211PhosphoserineCombined sources
Modified residuei508 – 5081PhosphoserineCombined sources
Modified residuei510 – 5101PhosphothreonineBy similarity
Modified residuei522 – 5221PhosphothreonineCombined sources
Modified residuei524 – 5241PhosphoserineCombined sources
Modified residuei696 – 6961PhosphothreonineBy similarity
Modified residuei1202 – 12021PhosphoserineCombined sources
Cross-linki1297 – 1297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1301 – 13011PhosphoserineCombined sources
Modified residuei1342 – 13421PhosphoserineBy similarity
Modified residuei1524 – 15241PhosphoserineCombined sources
Modified residuei1528 – 15281PhosphoserineCombined sources
Modified residuei1530 – 15301PhosphoserineCombined sources
Modified residuei1535 – 15351PhosphothreonineCombined sources
Modified residuei1542 – 15421PhosphothreonineCombined sources
Modified residuei1546 – 15461PhosphothreonineCombined sources
Cross-linki1558 – 1558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1563 – 15631PhosphoserineBy similarity
Cross-linki1565 – 1565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1569 – 15691PhosphoserineBy similarity
Modified residuei1646 – 16461N6-acetyllysine; alternateBy similarity
Cross-linki1646 – 1646Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1650 – 1650Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1656 – 16561PhosphothreonineBy similarity
Cross-linki1673 – 1673Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1682 – 16821PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6PDQ2.
MaxQBiQ6PDQ2.
PaxDbiQ6PDQ2.
PRIDEiQ6PDQ2.

PTM databases

iPTMnetiQ6PDQ2.
PhosphoSiteiQ6PDQ2.

Miscellaneous databases

PMAP-CutDBQ6PDQ2.

Expressioni

Gene expression databases

BgeeiQ6PDQ2.
CleanExiMM_CHD4.
ExpressionAtlasiQ6PDQ2. baseline and differential.
GenevisibleiQ6PDQ2. MM.

Interactioni

Subunit structurei

Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressor complex (PubMed:11003653). Interacts with KLF1; the interaction depends on sumoylation of KLF1, and leads to its transcriptional repression (PubMed:17938210). Interacts with ZGPAT; the interaction is direct. Interacts with BCL6, BRD4 and PCNT. Interacts directly with IKFZ1 in the NuRD complex. Interacts with TRIM27. Part of a complex containing ATR and HDAC2. Interacts with SETX (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Sox2Q60I233EBI-3043852,EBI-6120118
Zfp819Q80V814EBI-3043852,EBI-6394055

GO - Molecular functioni

Protein-protein interaction databases

BioGridi223700. 25 interactions.
DIPiDIP-59651N.
IntActiQ6PDQ2. 12 interactions.
MINTiMINT-1854030.
STRINGi10090.ENSMUSP00000060054.

Structurei

3D structure databases

ProteinModelPortaliQ6PDQ2.
SMRiQ6PDQ2. Positions 358-413, 439-670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini522 – 57958Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini615 – 67662Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini731 – 915185Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1047 – 1196150Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1570 – 1915346Required for interaction with PCNTBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi866 – 8694DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi50 – 12677Lys-richAdd
BLAST
Compositional biasi471 – 53262Pro-richAdd
BLAST
Compositional biasi1560 – 1671112Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 2 chromo domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri363 – 41048PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri442 – 48948PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ6PDQ2.
KOiK11643.
OrthoDBiEOG7C8GG7.
PhylomeDBiQ6PDQ2.
TreeFamiTF106448.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028725. CHD4.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10799:SF554. PTHR10799:SF554. 5 hits.
PfamiPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 1 hit.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PDQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPD EDLSEAETPK
60 70 80 90 100
LKKKKKPKKP RDPKIPKSKR QKKELGDSSG EGPEFVEEEE EVALRSDSEG
110 120 130 140 150
SDYTPGKKKK KKLGPKKEKK SKSKRKEEEE EEDEDDDSKE PKSSAQLLED
160 170 180 190 200
WGMEDIDHVF SEEDYRTLTN YKAFSQFVRP LIAAKNPKIA VSKMMMVLGA
210 220 230 240 250
KWREFSTNNP FKGSSGASVA AAAAAAVAVV ESMVTATEVA PPPPPVEVPI
260 270 280 290 300
RKAKTKEGKG PNARRKPKGS PRVPDAKKPK PKKVAPLKIK LGGFGSKRKR
310 320 330 340 350
SSSEDDDLDV ESDFDDASIN SYSVSDGSTS RSSRSRKKLR TAKKKKKGEE
360 370 380 390 400
EVTAVDGYET DHQDYCEVCQ QGGEIILCDT CPRAYHMVCL DPDMEKAPEG
410 420 430 440 450
KWSCPHCEKE GIQWEAKEDN SEGEEILEEV GGDPEEEDDH HMEFCRVCKD
460 470 480 490 500
GGELLCCDTC PSSYHIHCLN PPLPEIPNGE WLCPRCTCPA LKGKVQKILI
510 520 530 540 550
WKWGQPPSPT PVPRPPDADP NTPSPKPLEG RPERQFFVKW QGMSYWHCSW
560 570 580 590 600
VSELQLELHC QVMFRNYQRK NDMDEPPSGD FGGDEEKSRK RKNKDPKFAE
610 620 630 640 650
MEERFYRYGI KPEWMMIHRI LNHSVDKKGH VHYLIKWRDL PYDQASWESE
660 670 680 690 700
DVEIQDYDLF KQSYWNHREL MRGEEGRPGK KLKKVKLRKL ERPPETPTVD
710 720 730 740 750
PTVKYERQPE YLDATGGTLH PYQMEGLNWL RFSWAQGTDT ILADEMGLGK
760 770 780 790 800
TVQTAVFLYS LYKEGHSKGP FLVSAPLSTI INWEREFEMW APDMYVVTYV
810 820 830 840 850
GDKDSRAIIR ENEFSFEDNA IRGGKKASRM KKEASVKFHV LLTSYELITI
860 870 880 890 900
DMAILGSIDW ACLIVDEAHR LKNNQSKFFR VLNGYSLQHK LLLTGTPLQN
910 920 930 940 950
NLEELFHLLN FLTPERFHNL EGFLEEFADI AKEDQIKKLH DMLGPHMLRR
960 970 980 990 1000
LKADVFKNMP SKTELIVRVE LSPMQKKYYK YILTRNFEAL NARGGGNQVS
1010 1020 1030 1040 1050
LLNVVMDLKK CCNHPYLFPV AAMEAPKMPN GMYDGSALIR ASGKLLLLQK
1060 1070 1080 1090 1100
MLKNLKEGGH RVLIFSQMTK MLDLLEDFLE HEGYKYERID GGITGNMRQE
1110 1120 1130 1140 1150
AIDRFNAPGA QQFCFLLSTR AGGLGINLAT ADTVIIYDSD WNPHNDIQAF
1160 1170 1180 1190 1200
SRAHRIGQNK KVMIYRFVTR ASVEERITQV AKKKMMLTHL VVRPGLGSKT
1210 1220 1230 1240 1250
GSMSKQELDD ILKFGTEELF KDEATDGGGD NKEGEDSSVI HYDDKAIERL
1260 1270 1280 1290 1300
LDRNQDETED TELQGMNEYL SSFKVAQYVV REEEMGEEEE VEREIIKQEE
1310 1320 1330 1340 1350
SVDPDYWEKL LRHHYEQQQE DLARNLGKGK RIRKQVNYND GSQEDRDWQD
1360 1370 1380 1390 1400
DQSDNQSDYS VASEEGDEDF DERSEAPRRP SRKGLRNDKD KPLPPLLARV
1410 1420 1430 1440 1450
GGNIEVLGFN ARQRKAFLNA IMRYGMPPQD AFTTQWLVRD LRGKSEKEFK
1460 1470 1480 1490 1500
AYVSLFMRHL CEPGADGAET FADGVPREGL SRQHVLTRIG VMSLIRKKVQ
1510 1520 1530 1540 1550
EFEHVNGRWS MPELAEVEEN KKMSQPGSPS PKTPTPSTPG DTQPNTPAPV
1560 1570 1580 1590 1600
PPAEDGIKIE ENSLKEEEST EGEKEVKSTA PEATVECAQP PAPAPATAPA
1610 1620 1630 1640 1650
TATAPEDDKA PAEPPEGEEK VEKAEVKERT EEPMETEAKG TTEVEKVEEK
1660 1670 1680 1690 1700
SAVDLTPIVV EDKEEKKEEE EKKDVMLQNG ETPKDLSDEK QKKNSKQRFM
1710 1720 1730 1740 1750
FNIADGGFTE LHSLWQNEER AATVTKKTYE IWHRRHDYWL LAGIINHGYA
1760 1770 1780 1790 1800
RWQDIQNDPR YAILNEPFKG EMNRGNFLEI KNKFLARRFK LLEQALVIEE
1810 1820 1830 1840 1850
QLRRAAYLNM SEDPSHPSMA LNTRFAEVEC LAESHQHLSK ESMAGNKPAN
1860 1870 1880 1890 1900
AVLHKVLKQL EELLSDMKAD VTRLPATIAR IPPVAVRLQM SERNILSRLA
1910
NRAPEPPPQQ VAQQQ
Length:1,915
Mass (Da):217,751
Last modified:July 5, 2004 - v1
Checksum:iCFCB83B419AE6B5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC058578 mRNA. Translation: AAH58578.1.
CCDSiCCDS20543.1.
RefSeqiNP_666091.1. NM_145979.2.
UniGeneiMm.333388.

Genome annotation databases

EnsembliENSMUST00000056889; ENSMUSP00000060054; ENSMUSG00000063870.
GeneIDi107932.
KEGGimmu:107932.
UCSCiuc009dtk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC058578 mRNA. Translation: AAH58578.1.
CCDSiCCDS20543.1.
RefSeqiNP_666091.1. NM_145979.2.
UniGeneiMm.333388.

3D structure databases

ProteinModelPortaliQ6PDQ2.
SMRiQ6PDQ2. Positions 358-413, 439-670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223700. 25 interactions.
DIPiDIP-59651N.
IntActiQ6PDQ2. 12 interactions.
MINTiMINT-1854030.
STRINGi10090.ENSMUSP00000060054.

PTM databases

iPTMnetiQ6PDQ2.
PhosphoSiteiQ6PDQ2.

Proteomic databases

EPDiQ6PDQ2.
MaxQBiQ6PDQ2.
PaxDbiQ6PDQ2.
PRIDEiQ6PDQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056889; ENSMUSP00000060054; ENSMUSG00000063870.
GeneIDi107932.
KEGGimmu:107932.
UCSCiuc009dtk.1. mouse.

Organism-specific databases

CTDi1108.
MGIiMGI:1344380. Chd4.

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ6PDQ2.
KOiK11643.
OrthoDBiEOG7C8GG7.
PhylomeDBiQ6PDQ2.
TreeFamiTF106448.

Enzyme and pathway databases

ReactomeiR-MMU-6804758. Regulation of TP53 Activity through Acetylation.
R-MMU-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiChd4. mouse.
PMAP-CutDBQ6PDQ2.
PROiQ6PDQ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PDQ2.
CleanExiMM_CHD4.
ExpressionAtlasiQ6PDQ2. baseline and differential.
GenevisibleiQ6PDQ2. MM.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028725. CHD4.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10799:SF554. PTHR10799:SF554. 5 hits.
PfamiPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 1 hit.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: INTERACTION WITH IKFZ1 IN THE NURD COMPLEX.
  3. "Sumoylation of EKLF promotes transcriptional repression and is involved in inhibition of megakaryopoiesis."
    Siatecka M., Xue L., Bieker J.J.
    Mol. Cell. Biol. 27:8547-8560(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLF1, FUNCTION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-1528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-302; SER-303; SER-312; SER-421; SER-508; THR-522; SER-524; SER-1202; SER-1301; SER-1524; SER-1528; SER-1530; THR-1535; THR-1542 AND THR-1546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCHD4_MOUSE
AccessioniPrimary (citable) accession number: Q6PDQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.