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Protein Page:
CHD-3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
CHD-3 Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressive complex. Interacts with TRIM28 and SERBP1. Interacts (via its C-terminal) with HABP4. Interacts with PCNT; the interaction regulates centrosome integrity. Widely expressed. Belongs to the SNF2/RAD54 helicase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; EC 3.6.1.-; EC 3.6.4.12; Helicase
Cellular Component: centrosome; intermediate filament cytoskeleton; cytoplasm; nucleolus; NuRD complex; nucleus
Molecular Function: ATP-dependent DNA helicase activity; protein binding; DNA binding; zinc ion binding; helicase activity; ATP binding
Biological Process: regulation of transcription from RNA polymerase II promoter; regulation of transcription, DNA-dependent; transcription, DNA-dependent; centrosome organization and biogenesis; chromatin modification; spindle organization and biogenesis
Reference #:  NP_001005271 (RefSeq)
Alt. Names/Synonyms: ATP-dependent helicase CHD3; CHD-3; CHD3; chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3; hZFH; Mi-2 autoantigen 240 kDa protein; Mi-2a; Mi2-alpha; ZFH; Zinc finger helicase; zinc-finger helicase (Snf2-like)
Gene Symbols: CHD3
Molecular weight: 233,037 Da
Basal Isoelectric point: 5.88  Predict pI for various phosphorylation states
CST Pathways:  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CHD-3
Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

► Hide Isoforms 		 
0 3 S66-p DRGRDRHsPPGCHLF
0 5 S102-p DDIRLLPsALGVKKR
0 1 K115-m1 KRKRGPKkQkENKPG
0 1 K117-m1 KRGPKkQkENKPGkP
0 2 K123-m1 QkENKPGkPRKRKKR
0 11 S132-p RKRKKRDsEEEFGsE
0 8 S138-p DsEEEFGsERDEYRE
0 3 S147-p RDEYREKsEsGGsEy
0 3 S149-p EYREKsEsGGsEyGT
0 3 S152-p EKsEsGGsEyGTGPG
0 1 Y154-p sEsGGsEyGTGPGRK
0 7 K234-a FMRPLIAkkNPKIPM
0 7 K235-a MRPLIAkkNPKIPMs
0 1 S242-p kNPKIPMsKMMTILG
0 1 K320-a PIRRAKTkEGkGPGH
0 1 K323-a RAKTkEGkGPGHkRR
0 1 K328-a EGkGPGHkRRSKSPR
0 1 K361 KLGLLGGKRKKGGSY
0 4 S372-p GGSYVFQsDEGPEPE
0 7 S383-p PEPEAEEsDLDsGSV
0 1 S387-p AEEsDLDsGSVHsAs
0 1 S392-p LDsGSVHsAsGRPDG
0 1 S394-p sGSVHsAsGRPDGPV
0 1 Y654-p DEPPPLDyGsGEDDG
0 2 S656-p PPPLDyGsGEDDGKS
0 1 T691 GIKPEWMTVHRIINH
0 2 S771-p LQGDGPPssPTNDPT
0 10 S772-p QGDGPPssPTNDPTV
0 1 T783-p DPTVKYEtQPRFITA
0 1 Y798-p TGGTLHMyQLEGLNW
0 1 T925-p LTSYELItIDQAALG
0 1 S933-p IDQAALGsIRWACLV
0 1 K1033-u RLKADVFkNMPAkTE
0 1 K1038-u VFkNMPAkTELIVRV
0 1 Y1054-p LSPMQKKyYKYILTR
0 1 K1126-u GKLMLLQkMLRKLKE
0 1 K1281-a SKAGSMSkQELDDIL
0 1 T1333-p NQDATEDtDVQNMNE
0 1 Y1341-p DVQNMNEyLssFKVA
0 1 S1343-p QNMNEyLssFKVAQY
0 1 S1344-p NMNEyLssFKVAQYV
0 1 S1420 QEDQDNQSEYsVGsE
0 1 Y1422 DQDNQSEYsVGsEEE
0 5 S1423-p QDNQSEYsVGsEEED
0 6 S1426-p QSEYsVGsEEEDEDF
0 6 S1591-p SKRSSRAssPtktSP
0 1 S1592-p KRSSRAssPtktSPt
0 2 T1594-p SSRAssPtktSPttP
0 1 K1595-u SRAssPtktSPttPE
0 1 T1596-p RAssPtktSPttPEA
0 1 S1597 AssPtktSPttPEAs
0 2 T1599-p sPtktSPttPEAsAt
0 14 T1600-p PtktSPttPEAsAtN
0 4 S1604-p SPttPEAsAtNsPCt
0 1 A1605 PttPEAsAtNsPCts
0 2 T1606-p ttPEAsAtNsPCtsk
0 8 S1608-p PEAsAtNsPCtskPA
0 4 T1611-p sAtNsPCtskPAtPA
0 1 S1612-p AtNsPCtskPAtPAP
0 1 K1613-u tNsPCtskPAtPAPS
0 16 T1616-p PCtskPAtPAPSEKG
0 1 T1628-p EKGEGIRtPLEKEEA
0 8 A1658 KMETEADAPsPAPsL
0 18 S1660-p ETEADAPsPAPsLGE
0 15 S1664-p DAPsPAPsLGERLEP
0 1 S1704-p REKSATEstPGERGE
0 11 T1705-p EKSATEstPGERGEE
0 1 R1818-m1 IVLHGYArWQDIQND
0 1 K1836 AIINEPFKTEANKGN
0 1 K1841 PFKTEANKGNFLEMK
0 5 K1935-u EELLSDMkADVTRLP
0 1 - gap
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R87 IVLHGYARWQDIQND
K105 AIINEPFKTEANKGN
K110 PFKTEANKGNFLEMK
- gap
S371-p QALGPAAsPPPsPPL
S375-p PAAsPPPsPPLGPSL
  mouse

 
S65-p DRSRDRHsPPSCHLF
S95-p DDIRLLPsALGVKKR
K108 KRKRGPKKQKENKPG
K110 KRGPKKQKENKPGKP
K116 QKENKPGKPRKRKKL
S125-p RKRKKLDsEEEFGsE
S131-p DsEEEFGsERDEYRE
S140 RDEYREKSESGGSEY
S142 EYREKSESGGSEYGT
S145 EKSESGGSEYGTGPG
Y147 SESGGSEYGTGPGRK
K227 FMRPLIAKKNPKIPM
K228 MRPLIAKKNPKIPMS
S235 KNPKIPMSKMMTILG
K314 PIRRAKTKEGKGPGH
K317 RAKTKEGKGPGHKRR
K322 EGKGPGHKRRNKSPR
K355-a KLGLLGGkRKKAGSC
S366 AGSCAFQSEEGHEPE
S377 HEPEAEESDLDSGSV
S381 AEESDLDSGSVHSAS
S386 LDSGSVHSASGWPDG
S388 SGSVHSASGWPDGPV
Y647 DEPPPLDYGsGEDDG
S649-p PPPLDYGsGEDDGKS
T684-p GIKPEWMtVHRIINH
S764-p LQGDGPPssPTNDPT
S765-p QGDGPPssPTNDPTV
T776 DPTVKYETQPRFITA
Y791 TGGTLHMYQLEGLNW
T918 LTSYELITIDQAALG
S926 IDQAALGSIRWACLV
K1026 RLKADVFKNMPAKTE
K1031 VFKNMPAKTELIVRV
Y1047-p LSPMQKKyYKYILTR
K1119 GKLLLLQKMLRKLKE
K1274 SKAGSMSKQELDDIL
T1326 NQDATEDTDVQNMNE
Y1334 DVQNMNEYLSSFKVA
S1336 QNMNEYLSSFKVAQY
S1337 NMNEYLSSFKVAQYV
S1413-p QEDQDNQsEysVGsE
Y1415-p DQDNQsEysVGsEEE
S1416-p QDNQsEysVGsEEED
S1419-p QsEysVGsEEEDEDF
S1584-p SKRSSRAsSPtKTsP
S1585 KRSSRAsSPtKTsPt
T1587-p SSRAsSPtKTsPttP
K1588 SRAsSPtKTsPttPE
T1589 RAsSPtKTsPttPEA
S1590-p AsSPtKTsPttPEAs
T1592-p SPtKTsPttPEAstt
T1593-p PtKTsPttPEAsttN
S1597-p sPttPEAsttNsPCt
T1598-p PttPEAsttNsPCts
T1599-p ttPEAsttNsPCtsK
S1601-p PEAsttNsPCtsKPA
T1604-p sttNsPCtsKPAtPA
S1605-p ttNsPCtsKPAtPAP
K1606 tNsPCtsKPAtPAPS
T1609-p PCtsKPAtPAPSEKG
T1621 EKGDGVRTPLDKDDT
S1651-p KMEAEVDsPsPAPsL
S1653-p EAEVDsPsPAPsLGE
S1657-p DsPsPAPsLGERLEH
P1697 REKSASEPTPGERGE
T1698 EKSASEPTPGERGEE
R1812 IVLHGYARWQDIQND
K1830-a AIINEPFkTEANkGN
K1835-a PFkTEANkGNFLEMK
K1929-u EELLSDMkADVTRLP
- gap
- gap
  rat

 
- under review  
- under review  
K12 KRKRGPKKQKENKPG
K14 KRGPKKQKENKPGKP
K20 QKENKPGKPRKRKKL
S29 RKRKKLDSEEEFGSE
S35 DSEEEFGSERDEYRE
S44 RDEYREKSESGGSEY
S46 EYREKSESGGSEYGT
S49 EKSESGGSEYGTGPG
Y51 SESGGSEYGTGPGRK
K131 FMRPLIAKKNPKIPM
K132 MRPLIAKKNPKIPMS
S139 KNPKIPMSKMMTILG
K218 PIRRAKTKEGKGPGH
K221 RAKTKEGKGPGHKRR
K226 EGKGPGHKRRGKSAR
R259 KLGLLGGRRRKAGSC
G270 AGSCVFQGDEGPEPE
S281 PEPEAEESDLDSGSV
S285 AEESDLDSGSVHSAS
S290 LDSGSVHSASGRPDG
S292 SGSVHSASGRPDGPV
Y551 DEPPPLDYGSGEDDG
S553 PPPLDYGSGEDDGKS
T588 GIKPEWMTVHRIINH
S668 IQGDGPPSSPTNDPT
S669 QGDGPPSSPTNDPTV
T680 DPTVKYETQPRFITA
Y695 TGGTLHMYQLEGLNW
T822 LTSYELITIDQAALG
S830 IDQAALGSIRWACLV
K930 RLKADVFKNMPAKTE
K935 VFKNMPAKTELIVRV
Y951 LSPMQKKYYKYILTR
K1023 GKLLLLQKMLRKLKE
K1178 SKAGSMSKQELDDIL
T1230 NQDATDDTDVQNMNE
Y1238 DVQNMNEYLSSFKVA
S1240 QNMNEYLSSFKVAQY
S1241 NMNEYLSSFKVAQYV
S1317 QEDQDNQSEYSVGSE
Y1319 DQDNQSEYSVGSEEE
S1320 QDNQSEYSVGSEEED
S1323 QSEYSVGSEEEDEDF
S1488 SKRSSRASSPTKTSP
S1489 KRSSRASSPTKTSPT
T1491 SSRASSPTKTSPTTP
K1492 SRASSPTKTSPTTPE
T1493 RASSPTKTSPTTPEA
S1494 ASSPTKTSPTTPEAS
T1496 SPTKTSPTTPEASTT
T1497 PTKTSPTTPEASTTN
S1501 SPTTPEASTTNSPCT
T1502 PTTPEASTTNSPCTS
T1503 TTPEASTTNSPCTSK
S1505 PEASTTNSPCTSKPA
T1508 STTNSPCTSKPATPA
S1509 TTNSPCTSKPATPAP
K1510 TNSPCTSKPATPAPS
T1513 PCTSKPATPAPSEKG
T1525 EKGDGVRTLLEKDDT
S1555 KMETEIDSPSPAPSL
S1557 ETEIDSPSPAPSLGE
S1561 DSPSPAPSLGERLEH
P1601 REKSASEPTPGERGE
T1602 EKSASEPTPGERGEE
R1716 IVLHGYARWQDIQND
K1734 AIINEPFKTEANKGN
K1739 PFKTEANKGNFLEMK
K1833 EELLSDMKADVTRLP
- under review  
- under review  
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