CHD1_DROME - dbPTM
CHD1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHD1_DROME
UniProt AC Q7KU24
Protein Name Chromodomain-helicase-DNA-binding protein 1
Gene Name Chd1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1883
Subcellular Localization Nucleus . Chromosome . Colocalizes with elongating RNA polymerase II (Pol II) on polytene chromosomes (PubMed:18202396).
Protein Description 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 (By similarity). Involved in assembly of active chromatin. Required for maintaining open chromatin and pluripotency in embryonic stem cells and is important for wing development and fertility. Is essential for the incorporation of histone H3.3 and assembly of paternal chromatin. Required for replication-independent nucleosome assembly in the decondensing male pronucleus..
Protein Sequence MSQALNESANSIGSDEQDDTREEANGTDHSGSGSGSGSSGSDSDSDSSSGNSSDGRSSPEPEDKSLSVAGFPPTAAAAQADSKTNGFTDDQEDSSSDGSSGSDSDSDAEGPSDQRNQSINNANTSSSLPKPEQNEEEDNETEAGQQQPASDASADESSDSSANVSPTSSSSSSEEEEEDYRPKRTRQARKPPTAAEKSKKAPAPKNKKKTWDSDESDESEDSDDEVSTAQKRKPAATTSRSKLAQQQQRRRVKPFSSEDSDDDDASKRCATRRKGAAVSYKEASEDEATDSEDLLEFEYDESQAATTAATAEEEEKCETIERILAQRAGKRGCTGNQTTIYAIEENGFDPHAGFDEKQTPDAETEAQFLIKWKGWSYIHNTWESEATLRDMKAKGMKKLDNFIKKEKEQAYWRRYAGPEDIDYFECQLELQHELLKSYNNVDRIIAKGSKPDDGTEEYLCKWQSLPYAESTWEDAALVLRKWQRCAEQFNDRESSKCTPSRHCRVIKYRPKFSRIKNQPEFLSSGLTLRDYQMDGLNWLLHSWCKENSVILADEMGLGKTIQTICFLYSLFKIHHLYGPFLCVVPLSTMTAWQREFDLWAPDMNVVTYLGDIKSRELIQQYEWQFESSKRLKFNCILTTYEIVLKDKQFLGTLQWAALLVDEAHRLKNDDSLLYKSLKEFDTNHRLLITGTPLQNSLKELWALLHFIMPDKFDTWENFEVQHGNAEDKGYTRLHQQLEPYILRRVKKDVEKSLPAKVEQILRVEMTSLQKQYYKWILTKNFDALRKGKRGSTSTFLNIVIELKKCCNHAALIRPSEFELMGLQQDEALQTLLKGSGKLVLLDKLLCRLKETGHRVLIFSQMVRMLDVLADYLQKRHFPFQRLDGSIKGEMRRQALDHFNAEGSQDFCFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAQARAHRIGQKNQVNIYRLVTARSVEEQIVERAKQKMVLDHLVIQRMDTTGRTVLDKSGNGHSSNSNPFNKDDLSAILKFGAEELFKDEQEHDDDLVCDIDEILRRAETRNEDPEMPADDLLSAFKVASIAAFEEEPSDSVSKQDQNAAGEEDDSKDWDDIIPEGFRKAIDDQERAKEMEDLYLPPRRKTAANQNEGKRGAGKGGKGKQQADDSGGDSDYELGSDGSGDDGRPRKRGRPTMKEKITGFTDAELRRFIRSYKKFPAPLHRMEAIACDAELQEKPLAELKRLGEMLHDRCVQFLHEHKEEESKTAATDETPGAKQRRARATFSVKLGGVSFNAKKLLACEQELQPLNEIMPSMPEERQQWSFNIKTRAPVFDVDWGIEEDTKLLCGIYQYGIGSWEQMKLDPTLKLTDKILLNDTRKPQAKQLQTRAEYLLKIIKKNVELTKGGQRRQRRPRASRANDAKAASQSASSTIDAKPHDGEDAAGDARTVAESSNSQVDPSTASPHNAPATEQHGDPAKKAKKSKARSKKTSASDNNGNKPMHFTANNEPRALEVLGDLDPSIFNECKEKMRPVKKALKALDQPDVSLSDQDQLQHTRDCLLQIGKQIDVCLNPYAETEKKEWRSNLWYFVSKFTELDAKRLFKIYKHALKQKAGGDGEAKGKDKGSSGSPAKSKPNGVTTEEKEKERDRSGGKKKKKDKDKERSGQARYPETGIPTSGRYADPPLKRKRDENDADASSGLAGAPGGGIGDNLKSMSFKRLNMDRHEDRKKHHRGPDYYGGSGPPMGSGSYEGGSNSRRQGPTSPSTPRTGRGGYDPPPAPSGYTPEMERWQSRDRYSQDYKRDRYDGYGRSGGGQGSYHRERDRRPEKRRYPSGLPPHPYSSHYLPPNYYGLPNGAVPGLPPPSSVYRSDPRGYPVMPRDYPADYRRSDYERRTQT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
65PhosphorylationSPEPEDKSLSVAGFP
CCCCCCCCCCCCCCC
37.8922817900
67PhosphorylationEPEDKSLSVAGFPPT
CCCCCCCCCCCCCCC
19.6022817900
256PhosphorylationRRRVKPFSSEDSDDD
HHCCCCCCCCCCCCC
41.1519429919
257PhosphorylationRRVKPFSSEDSDDDD
HCCCCCCCCCCCCCH
45.8919429919
260PhosphorylationKPFSSEDSDDDDASK
CCCCCCCCCCCHHHH
38.6019429919
266PhosphorylationDSDDDDASKRCATRR
CCCCCHHHHHHHHHH
27.8518327897
1096PhosphorylationAAGEEDDSKDWDDII
CCCCCCCCCCHHHHC
44.8519429919
1155PhosphorylationGKQQADDSGGDSDYE
CCCCCCCCCCCCCCC
45.2718327897
1159PhosphorylationADDSGGDSDYELGSD
CCCCCCCCCCCCCCC
45.4218327897
1165PhosphorylationDSDYELGSDGSGDDG
CCCCCCCCCCCCCCC
51.9618327897
1168PhosphorylationYELGSDGSGDDGRPR
CCCCCCCCCCCCCCC
44.0018327897
1749PhosphorylationNSRRQGPTSPSTPRT
CCCCCCCCCCCCCCC
61.1625749252
1750PhosphorylationSRRQGPTSPSTPRTG
CCCCCCCCCCCCCCC
21.7122817900
1784PhosphorylationWQSRDRYSQDYKRDR
HHCCCCCCHHHHCCC
19.9219429919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CHD1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHD1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CHD1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSRP1_HUMANSSRP1physical
10199952

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHD1_DROME

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Related Literatures of Post-Translational Modification

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