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O14646

- CHD1_HUMAN

UniProt

O14646 - CHD1_HUMAN

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Protein

Chromodomain-helicase-DNA-binding protein 1

Gene

CHD1

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

Functioni

ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells.By similarity1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi506 – 5138ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent DNA helicase activity Source: ProtInc
  3. DNA binding Source: UniProtKB-KW
  4. methylated histone binding Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. DNA duplex unwinding Source: GOC
  3. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein 1 (EC:3.6.4.12)
Short name:
CHD-1
Alternative name(s):
ATP-dependent helicase CHD1
Gene namesi
Name:CHD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1915. CHD1.

Subcellular locationi

Nucleus. Cytoplasm By similarity
Note: Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26451.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17101710Chromodomain-helicase-DNA-binding protein 1PRO_0000080224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei216 – 2161Phosphoserine1 Publication
Modified residuei237 – 2371Phosphothreonine1 Publication
Modified residuei241 – 2411Phosphoserine1 Publication
Modified residuei250 – 2501Phosphothreonine1 Publication
Modified residuei252 – 2521Phosphoserine1 Publication
Modified residuei1025 – 10251Phosphoserine1 Publication
Modified residuei1040 – 10401Phosphoserine3 Publications
Modified residuei1081 – 10811Phosphoserine1 Publication
Modified residuei1096 – 10961Phosphoserine2 Publications
Modified residuei1098 – 10981Phosphoserine2 Publications
Modified residuei1100 – 11001Phosphoserine2 Publications
Modified residuei1102 – 11021Phosphoserine1 Publication
Modified residuei1353 – 13531Phosphoserine1 Publication
Modified residuei1355 – 13551Phosphoserine1 Publication
Modified residuei1356 – 13561Phosphoserine1 Publication
Modified residuei1360 – 13601Phosphoserine1 Publication
Modified residuei1363 – 13631Phosphoserine1 Publication
Modified residuei1371 – 13711Phosphoserine1 Publication
Modified residuei1677 – 16771Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14646.
PaxDbiO14646.
PRIDEiO14646.

PTM databases

PhosphoSiteiO14646.

Expressioni

Gene expression databases

BgeeiO14646.
CleanExiHS_CHD1.
ExpressionAtlasiO14646. baseline and differential.
GenevestigatoriO14646.

Organism-specific databases

HPAiHPA022236.

Interactioni

Subunit structurei

Component of the SAGA complex (By similarity). Interacts with BCLAF1, NCoR, SRP20 and SAFB (By similarity). Specifically interacts with methylated H3K4me2 and H3K4me3. Interacts with the FACT complex, the PAF complex and the U2 snRNP. Interacts directly with PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and SSRP1.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NS1B2BUF13EBI-1560858,EBI-4291940From a different organism.

Protein-protein interaction databases

BioGridi107530. 19 interactions.
DIPiDIP-38922N.
IntActiO14646. 1 interaction.
STRINGi9606.ENSP00000284049.

Structurei

Secondary structure

1
1710
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi273 – 28412Combined sources
Helixi289 – 2924Combined sources
Helixi294 – 3007Combined sources
Turni303 – 3064Combined sources
Turni309 – 3113Combined sources
Beta strandi314 – 3229Combined sources
Helixi327 – 3293Combined sources
Beta strandi331 – 3333Combined sources
Helixi335 – 3406Combined sources
Helixi347 – 36418Combined sources
Helixi368 – 38720Combined sources
Beta strandi390 – 3978Combined sources
Beta strandi408 – 4136Combined sources
Helixi418 – 4203Combined sources
Beta strandi422 – 4254Combined sources
Helixi426 – 4327Combined sources
Helixi434 – 4418Combined sources
Helixi1128 – 113811Combined sources
Helixi1144 – 11463Combined sources
Helixi1148 – 11547Combined sources
Helixi1162 – 118019Combined sources
Beta strandi1201 – 12044Combined sources
Beta strandi1207 – 12104Combined sources
Helixi1211 – 122717Combined sources
Helixi1232 – 12365Combined sources
Beta strandi1249 – 12513Combined sources
Helixi1255 – 126814Combined sources
Helixi1273 – 12786Combined sources
Beta strandi1280 – 12834Combined sources
Turni1285 – 12873Combined sources
Helixi1299 – 132426Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B2TX-ray2.45A/B268-443[»]
C268-373[»]
2B2UX-ray2.95A/B268-443[»]
C268-373[»]
2B2VX-ray2.65A/B268-443[»]
C268-373[»]
2B2WX-ray2.40A/B268-443[»]
C268-373[»]
2B2YX-ray2.35A/B268-443[»]
C268-373[»]
4B4CX-ray1.62A1119-1327[»]
4NW2X-ray1.90A/C268-443[»]
4O42X-ray1.87A268-443[»]
ProteinModelPortaliO14646.
SMRiO14646. Positions 270-1020, 1124-1327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14646.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini272 – 36493Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini389 – 45264Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini493 – 663171Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini792 – 943152Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Repeati1628 – 163251
Repeati1634 – 163852
Repeati1640 – 164453

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1628 – 1644173 X 5 AA repeats of H-S-D-H-RAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi614 – 6174DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 7070Ser-richAdd
BLAST
Compositional biasi117 – 13721Ser-richAdd
BLAST

Domaini

The 2 chromodomains are involved in the binding to the histone H3 methyllysine at position 4 (H3K4me3).1 Publication

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000207917.
HOVERGENiHBG005325.
InParanoidiO14646.
KOiK11367.
OMAiMDHRASS.
OrthoDBiEOG7NPFSB.
PhylomeDBiO14646.
TreeFamiTF313461.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR025260. DUF4208.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00385. Chromo. 2 hits.
PF13907. DUF4208. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14646-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS
60 70 80 90 100
DSDSGSESGS QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA
110 120 130 140 150
ILKKQQQQQQ QQQHQASSNS GSEEDSSSSE DSDDSSSEVK RKKHKDEDWQ
160 170 180 190 200
MSGSGSPSQS GSDSESEEER EKSSCDETES DYEPKNKVKS RKPQNRSKSK
210 220 230 240 250
NGKKILGQKK RQIDSSEEDD DEEDYDNDKR SSRRQATVNV SYKEDEEMKT
260 270 280 290 300
DSDDLLEVCG EDVPQPEEEE FETIERFMDC RIGRKGATGA TTTIYAVEAD
310 320 330 340 350
GDPNAGFEKN KEPGEIQYLI KWKGWSHIHN TWETEETLKQ QNVRGMKKLD
360 370 380 390 400
NYKKKDQETK RWLKNASPED VEYYNCQQEL TDDLHKQYQI VERIIAHSNQ
410 420 430 440 450
KSAAGYPDYY CKWQGLPYSE CSWEDGALIS KKFQACIDEY FSRNQSKTTP
460 470 480 490 500
FKDCKVLKQR PRFVALKKQP SYIGGHEGLE LRDYQLNGLN WLAHSWCKGN
510 520 530 540 550
SCILADEMGL GKTIQTISFL NYLFHEHQLY GPFLLVVPLS TLTSWQREIQ
560 570 580 590 600
TWASQMNAVV YLGDINSRNM IRTHEWTHHQ TKRLKFNILL TTYEILLKDK
610 620 630 640 650
AFLGGLNWAF IGVDEAHRLK NDDSLLYKTL IDFKSNHRLL ITGTPLQNSL
660 670 680 690 700
KELWSLLHFI MPEKFSSWED FEEEHGKGRE YGYASLHKEL EPFLLRRVKK
710 720 730 740 750
DVEKSLPAKV EQILRMEMSA LQKQYYKWIL TRNYKALSKG SKGSTSGFLN
760 770 780 790 800
IMMELKKCCN HCYLIKPPDN NEFYNKQEAL QHLIRSSGKL ILLDKLLIRL
810 820 830 840 850
RERGNRVLIF SQMVRMLDIL AEYLKYRQFP FQRLDGSIKG ELRKQALDHF
860 870 880 890 900
NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN DLQAQARAHR
910 920 930 940 950
IGQKKQVNIY RLVTKGSVEE DILERAKKKM VLDHLVIQRM DTTGKTVLHT
960 970 980 990 1000
GSAPSSSTPF NKEELSAILK FGAEELFKEP EGEEQEPQEM DIDEILKRAE
1010 1020 1030 1040 1050
THENEPGPLT VGDELLSQFK VANFSNMDED DIELEPERNS KNWEEIIPED
1060 1070 1080 1090 1100
QRRRLEEEER QKELEEIYML PRMRNCAKQI SFNGSEGRRS RSRRYSGSDS
1110 1120 1130 1140 1150
DSISEGKRPK KRGRPRTIPR ENIKGFSDAE IRRFIKSYKK FGGPLERLDA
1160 1170 1180 1190 1200
IARDAELVDK SETDLRRLGE LVHNGCIKAL KDSSSGTERT GGRLGKVKGP
1210 1220 1230 1240 1250
TFRISGVQVN AKLVISHEEE LIPLHKSIPS DPEERKQYTI PCHTKAAHFD
1260 1270 1280 1290 1300
IDWGKEDDSN LLIGIYEYGY GSWEMIKMDP DLSLTHKILP DDPDKKPQAK
1310 1320 1330 1340 1350
QLQTRADYLI KLLSRDLAKK EALSGAGSSK RRKARAKKNK AMKSIKVKEE
1360 1370 1380 1390 1400
IKSDSSPLPS EKSDEDDDKL SESKSDGRER SKKSSVSDAP VHITASGEPV
1410 1420 1430 1440 1450
PISEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE REQLEHTRQC
1460 1470 1480 1490 1500
LIKIGDHITE CLKEYTNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA
1510 1520 1530 1540 1550
IKKRQESQQN SDQNSNLNPH VIRNPDVERL KENTNHDDSS RDSYSSDRHL
1560 1570 1580 1590 1600
TQYHDHHKDR HQGDSYKKSD SRKRPYSSFS NGKDHRDWDH YKQDSRYYSD
1610 1620 1630 1640 1650
REKHRKLDDH RSRDHRSNLE GSLKDRSHSD HRSHSDHRLH SDHRSSSEYT
1660 1670 1680 1690 1700
HHKSSRDYRY HSDWQMDHRA SSSGPRSPLD QRSPYGSRSP FEHSVEHKST
1710
PEHTWSSRKT
Length:1,710
Mass (Da):196,688
Last modified:November 24, 2009 - v2
Checksum:iD888AAA46FDA31B1
GO
Isoform 2 (identifier: O14646-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1684-1684: Missing.

Show »
Length:1,709
Mass (Da):196,590
Checksum:i8B2C96C7597E55B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti392 – 3921E → G in AAB87381. (PubMed:9326634)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti264 – 2641P → T.
Corresponds to variant rs10062803 [ dbSNP | Ensembl ].
VAR_055652

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1684 – 16841Missing in isoform 2. 2 PublicationsVSP_038432

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006513 mRNA. Translation: AAB87381.1.
AC022121 Genomic DNA. No translation available.
BC117134 mRNA. Translation: AAI17135.1.
CCDSiCCDS34204.1. [O14646-1]
RefSeqiNP_001261.2. NM_001270.2. [O14646-1]
XP_005271924.1. XM_005271867.2. [O14646-1]
UniGeneiHs.643465.

Genome annotation databases

EnsembliENST00000284049; ENSP00000284049; ENSG00000153922. [O14646-1]
ENST00000614616; ENSP00000483667; ENSG00000153922. [O14646-1]
GeneIDi1105.
KEGGihsa:1105.
UCSCiuc003knf.3. human. [O14646-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006513 mRNA. Translation: AAB87381.1 .
AC022121 Genomic DNA. No translation available.
BC117134 mRNA. Translation: AAI17135.1 .
CCDSi CCDS34204.1. [O14646-1 ]
RefSeqi NP_001261.2. NM_001270.2. [O14646-1 ]
XP_005271924.1. XM_005271867.2. [O14646-1 ]
UniGenei Hs.643465.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B2T X-ray 2.45 A/B 268-443 [» ]
C 268-373 [» ]
2B2U X-ray 2.95 A/B 268-443 [» ]
C 268-373 [» ]
2B2V X-ray 2.65 A/B 268-443 [» ]
C 268-373 [» ]
2B2W X-ray 2.40 A/B 268-443 [» ]
C 268-373 [» ]
2B2Y X-ray 2.35 A/B 268-443 [» ]
C 268-373 [» ]
4B4C X-ray 1.62 A 1119-1327 [» ]
4NW2 X-ray 1.90 A/C 268-443 [» ]
4O42 X-ray 1.87 A 268-443 [» ]
ProteinModelPortali O14646.
SMRi O14646. Positions 270-1020, 1124-1327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107530. 19 interactions.
DIPi DIP-38922N.
IntActi O14646. 1 interaction.
STRINGi 9606.ENSP00000284049.

Chemistry

DrugBanki DB00445. Epirubicin.

PTM databases

PhosphoSitei O14646.

Proteomic databases

MaxQBi O14646.
PaxDbi O14646.
PRIDEi O14646.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284049 ; ENSP00000284049 ; ENSG00000153922 . [O14646-1 ]
ENST00000614616 ; ENSP00000483667 ; ENSG00000153922 . [O14646-1 ]
GeneIDi 1105.
KEGGi hsa:1105.
UCSCi uc003knf.3. human. [O14646-1 ]

Organism-specific databases

CTDi 1105.
GeneCardsi GC05M098190.
H-InvDB HIX0005061.
HGNCi HGNC:1915. CHD1.
HPAi HPA022236.
MIMi 602118. gene.
neXtProti NX_O14646.
PharmGKBi PA26451.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00760000119067.
HOGENOMi HOG000207917.
HOVERGENi HBG005325.
InParanoidi O14646.
KOi K11367.
OMAi MDHRASS.
OrthoDBi EOG7NPFSB.
PhylomeDBi O14646.
TreeFami TF313461.

Miscellaneous databases

ChiTaRSi CHD1. human.
EvolutionaryTracei O14646.
GeneWikii CHD1.
GenomeRNAii 1105.
NextBioi 4580.
PROi O14646.
SOURCEi Search...

Gene expression databases

Bgeei O14646.
CleanExi HS_CHD1.
ExpressionAtlasi O14646. baseline and differential.
Genevestigatori O14646.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR025260. DUF4208.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF00385. Chromo. 2 hits.
PF13907. DUF4208. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEi PS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 2).
    Tissue: Cerebellum.
  4. "Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains."
    Sims R.J. III, Chen C.-F., Santos-Rosa H., Kouzarides T., Patel S.S., Reinberg D.
    J. Biol. Chem. 280:41789-41792(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH H3K4ME2 AND H3K4ME3.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Molecular implications of evolutionary differences in CHD double chromodomains."
    Flanagan J.F., Blus B.J., Kim D., Clines K.L., Rastinejad F., Khorasanizadeh S.
    J. Mol. Biol. 369:334-342(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, INTERACTION WITH HISTONE H3K4ME3.
  8. "Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing."
    Sims R.J. III, Millhouse S., Chen C.-F., Lewis B.A., Erdjument-Bromage H., Tempst P., Manley J.L., Reinberg D.
    Mol. Cell 28:665-676(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH H3K4ME3; PAF1; SFA3A1; SFA3A2; SFA3A3; SNF2 AND SSRP1.
  9. "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-1040; SER-1081 AND SER-1677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237; SER-241; SER-1040; SER-1096; SER-1098; SER-1100 AND SER-1677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-250; SER-252; SER-1025; SER-1040 AND SER-1677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-215; SER-216; SER-1096; SER-1098; SER-1100; SER-1102; SER-1353; SER-1355; SER-1356; SER-1360; SER-1363 AND SER-1371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Double chromodomains cooperate to recognize the methylated histone H3 tail."
    Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L., Kim Y., Minor W., Rastinejad F., Khorasanizadeh S.
    Nature 438:1181-1185(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 268-443, INTERACTION WITH HISTONE H3K4ME3.

Entry informationi

Entry nameiCHD1_HUMAN
AccessioniPrimary (citable) accession number: O14646
Secondary accession number(s): Q17RZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 24, 2009
Last modified: November 26, 2014
This is version 139 of the entry and version 2 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3