DCR1C_HUMAN - dbPTM
DCR1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCR1C_HUMAN
UniProt AC Q96SD1
Protein Name Protein artemis
Gene Name DCLRE1C
Organism Homo sapiens (Human).
Sequence Length 692
Subcellular Localization Nucleus .
Protein Description Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ..
Protein Sequence MSSFEGQMAEYPTISIDRFDRENLRARAYFLSHCHKDHMKGLRAPTLKRRLECSLKVYLYCSPVTKELLLTSPKYRFWKKRIISIEIETPTQISLVDEASGEKEEIVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAQGEAARMELLHSGGRVKDIQSVYLDTTFCDPRFYQIPSREECLSGVLELVRSWITRSPYHVVWLNCKAAYGYEYLFTNLSEELGVQVHVNKLDMFRNMPEILHHLTTDRNTQIHACRHPKAEEYFQWSKLPCGITSRNRIPLHIISIKPSTMWFGERSRKTNVIVRTGESSYRACFSFHSSYSEIKDFLSYLCPVNAYPNVIPVGTTMDKVVEILKPLCRSSQSTEPKYKPLGKLKRARTVHRDSEEEDDYLFDDPLPIPLRHKVPYPETFHPEVFSMTAVSEKQPEKLRQTPGCCRAECMQSSRFTNFVDCEESNSESEEEVGIPASLQGDLGSVLHLQKADGDVPQWEVFFKRNDEITDESLENFPSSTVAGGSQSPKLFSDSDGESTHISSQNSSQSTHITEQGSQGWDSQSDTVLLSSQERNSGDITSLDKADYRPTIKENIPASLMEQNVICPKDTYSDLKSRDKDVTIVPSTGEPTTLSSETHIPEEKSLLNLSTNADSQSSSDFEVPSTPEAELPKREHLQYLYEKLATGESIAVKKRKCSLLDT
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
2Phosphorylation------MSSFEGQMA
------CCCCCCCCC		43.6723401153
3Phosphorylation-----MSSFEGQMAE
-----CCCCCCCCCC		26.4723663014
11PhosphorylationFEGQMAEYPTISIDR
CCCCCCCCCEEEEEC		8.9923663014
13PhosphorylationGQMAEYPTISIDRFD
CCCCCCCEEEEECCC		26.8423401153
15PhosphorylationMAEYPTISIDRFDRE
CCCCCEEEEECCCHH		22.4023401153
18 (in isoform 3)Phosphorylation-33.4222468782
19 (in isoform 3)Phosphorylation-10.3522468782
58PhosphorylationLECSLKVYLYCSPVT
HHEEEEEEEEECCCC		7.1426074081
60PhosphorylationCSLKVYLYCSPVTKE
EEEEEEEEECCCCHH		3.5326074081
62PhosphorylationLKVYLYCSPVTKELL
EEEEEEECCCCHHHH		14.6226074081
65PhosphorylationYLYCSPVTKELLLTS
EEEECCCCHHHHHCC		23.3726074081
71PhosphorylationVTKELLLTSPKYRFW
CCHHHHHCCCCCCCE		42.8426074081
71O-linked_GlycosylationVTKELLLTSPKYRFW
CCHHHHHCCCCCCCE		42.8430059200
72PhosphorylationTKELLLTSPKYRFWK
CHHHHHCCCCCCCEE		21.2626074081
91PhosphorylationSIEIETPTQISLVDE
EEEECCCCEEEEEEC		46.0515723659
157UbiquitinationLHSGGRVKDIQSVYL
HHCCCCCCCCEEEEE		47.99-
251PhosphorylationHLTTDRNTQIHACRH
HHHCCCCCCEEECCC		29.7815723659
260UbiquitinationIHACRHPKAEEYFQW
EEECCCCCHHHHHHH		63.40-
264PhosphorylationRHPKAEEYFQWSKLP
CCCCHHHHHHHCCCC		7.8023071622
286PhosphorylationRIPLHIISIKPSTMW
CCEEEEEEECCCCCC		24.7724719451
290PhosphorylationHIISIKPSTMWFGER
EEEEECCCCCCCCCC		26.3724719451
291PhosphorylationIISIKPSTMWFGERS
EEEECCCCCCCCCCC		27.2724719451
298PhosphorylationTMWFGERSRKTNVIV
CCCCCCCCCCCEEEE		33.5529083192
307PhosphorylationKTNVIVRTGESSYRA
CCEEEEECCCCCHHH		34.1122210691
310PhosphorylationVIVRTGESSYRACFS
EEEECCCCCHHHHHH		33.7322210691
311PhosphorylationIVRTGESSYRACFSF
EEECCCCCHHHHHHC		17.8422210691
312PhosphorylationVRTGESSYRACFSFH
EECCCCCHHHHHHCC		16.1227762562
317PhosphorylationSSYRACFSFHSSYSE
CCHHHHHHCCCCHHH		23.18-
322PhosphorylationCFSFHSSYSEIKDFL
HHHCCCCHHHHHHHH		17.21-
380PhosphorylationGKLKRARTVHRDSEE
HHHCCCEECCCCCCC		21.4922115753
385 (in isoform 4)Phosphorylation-47.0326552605
385PhosphorylationARTVHRDSEEEDDYL
CEECCCCCCCCCCCC		47.0322115753
387 (in isoform 4)Phosphorylation-71.3426552605
389 (in isoform 4)Phosphorylation-53.8126552605
391 (in isoform 4)Phosphorylation-22.9126552605
391PhosphorylationDSEEEDDYLFDDPLP
CCCCCCCCCCCCCCC		22.9126657352
494AcetylationPQWEVFFKRNDEITD
CCEEEEEECCCCCCH		38.5411921477
500PhosphorylationFKRNDEITDESLENF
EECCCCCCHHHHHHC		31.5030576142
503PhosphorylationNDEITDESLENFPSS
CCCCCHHHHHHCCCC		43.7423927012
509PhosphorylationESLENFPSSTVAGGS
HHHHHCCCCCCCCCC		34.2123663014
510PhosphorylationSLENFPSSTVAGGSQ
HHHHCCCCCCCCCCC		27.4323663014
511PhosphorylationLENFPSSTVAGGSQS
HHHCCCCCCCCCCCC		20.7923663014
516PhosphorylationSSTVAGGSQSPKLFS
CCCCCCCCCCCCCCC		26.9423401153
518PhosphorylationTVAGGSQSPKLFSDS
CCCCCCCCCCCCCCC		26.2130266825
525PhosphorylationSPKLFSDSDGESTHI
CCCCCCCCCCCCCEE		46.4415723659
534PhosphorylationGESTHISSQNSSQST
CCCCEECCCCCCCCE		32.5522817900
538PhosphorylationHISSQNSSQSTHITE
EECCCCCCCCEEEEE		35.3822817900
548PhosphorylationTHITEQGSQGWDSQS
EEEEECCCCCCCCCC		25.8022817900
553PhosphorylationQGSQGWDSQSDTVLL
CCCCCCCCCCCEEEE		25.6922817900
562PhosphorylationSDTVLLSSQERNSGD
CCEEEECCCCCCCCC		35.7115723659
567PhosphorylationLSSQERNSGDITSLD
ECCCCCCCCCCCCCC		44.0221815630
589PhosphorylationIKENIPASLMEQNVI
HHHCCCHHHHHCCCC		23.9330576142
601PhosphorylationNVICPKDTYSDLKSR
CCCCCCCCHHHHHHC		30.9324719451
607PhosphorylationDTYSDLKSRDKDVTI
CCHHHHHHCCCCEEE		53.67-
613PhosphorylationKSRDKDVTIVPSTGE
HHCCCCEEEECCCCC		26.7924043423
617PhosphorylationKDVTIVPSTGEPTTL
CCEEEECCCCCCCCC		37.8424043423
618PhosphorylationDVTIVPSTGEPTTLS
CEEEECCCCCCCCCC		39.2224043423
622PhosphorylationVPSTGEPTTLSSETH
ECCCCCCCCCCCCCC		35.7524043423
623PhosphorylationPSTGEPTTLSSETHI
CCCCCCCCCCCCCCC		35.0424043423
625PhosphorylationTGEPTTLSSETHIPE
CCCCCCCCCCCCCCC		24.8424043423
626PhosphorylationGEPTTLSSETHIPEE
CCCCCCCCCCCCCCH		50.0224043423
628PhosphorylationPTTLSSETHIPEEKS
CCCCCCCCCCCCHHH		27.3624043423
645PhosphorylationNLSTNADSQSSSDFE
CCCCCCCCCCCCCCC		29.5615731174
647PhosphorylationSTNADSQSSSDFEVP
CCCCCCCCCCCCCCC		35.44-
648PhosphorylationTNADSQSSSDFEVPS
CCCCCCCCCCCCCCC		26.70-
649PhosphorylationNADSQSSSDFEVPST
CCCCCCCCCCCCCCC		52.12-
655PhosphorylationSSDFEVPSTPEAELP
CCCCCCCCCCCCCCC		62.87-
656PhosphorylationSDFEVPSTPEAELPK
CCCCCCCCCCCCCCC		21.05-
676PhosphorylationYLYEKLATGESIAVK
HHHHHHHCCCCCEEE		52.50-
683AcetylationTGESIAVKKRKCSLL
CCCCCEEEEECCCCC		37.5320167786
688PhosphorylationAVKKRKCSLLDT---
EEEEECCCCCCC---		34.6921815630
692PhosphorylationRKCSLLDT-------
ECCCCCCC-------		40.2421712546
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
503SPhosphorylationKinaseATMQ13315
PSP
503SPhosphorylationKinasePRKDCP78527
GPS
516SPhosphorylationKinasePRKDCP78527
GPS
516SPhosphorylationKinaseATMQ13315
PSP
516SPhosphorylationKinaseATRQ13535
PSP
534SPhosphorylationKinasePRKDCP78527
GPS
534SPhosphorylationKinaseATMQ13315
GPS
538SPhosphorylationKinasePRKDCP78527
GPS
538SPhosphorylationKinaseATMQ13315
GPS
548SPhosphorylationKinasePRKDCP78527
GPS
553SPhosphorylationKinasePRKDCP78527
GPS
645SPhosphorylationKinaseATRQ13535
PSP
645SPhosphorylationKinasePRKDCP78527
GPS
645SPhosphorylationKinaseATMQ13315
Uniprot
647SPhosphorylationKinaseATMQ13315
PSP
648SPhosphorylationKinaseATMQ13315
PSP
649SPhosphorylationKinaseATMQ13315
PSP
656TPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCR1C_HUMAN !!
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 DCR1C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRKDC_HUMANPRKDCphysical
11955432
FBXW7_HUMANFBXW7physical
19423708
DDB1_HUMANDDB1physical
22134138
DDB2_HUMANDDB2physical
22134138
ATM_HUMANATMphysical
15456891
BRCA1_HUMANBRCA1physical
15456891
RAD50_HUMANRAD50physical
15456891
NBN_HUMANNBNphysical
15456891
MRE11_HUMANMRE11Aphysical
15456891
PRKDC_HUMANPRKDCphysical
15936993
XRCC5_HUMANXRCC5physical
16857680
PRKDC_HUMANPRKDCphysical
16857680
CDN1B_HUMANCDKN1Bphysical
22134138
AKA11_HUMANAKAP11physical
26186194
ANR52_HUMANANKRD52physical
26186194
ZSWM8_HUMANZSWIM8physical
26186194
AAKG2_HUMANPRKAG2physical
26186194
AAKG1_HUMANPRKAG1physical
26186194
PP6R2_HUMANPPP6R2physical
26186194
AAKB1_HUMANPRKAB1physical
26186194
AAKB2_HUMANPRKAB2physical
26186194
TRI26_HUMANTRIM26physical
26186194
KAPCB_HUMANPRKACBphysical
26186194
AAPK1_HUMANPRKAA1physical
26186194
AAPK2_HUMANPRKAA2physical
26186194
PASK_HUMANPASKphysical
26186194
ANR28_HUMANANKRD28physical
26186194
DDX20_HUMANDDX20physical
26186194
PP6R1_HUMANPPP6R1physical
26186194
GOGA2_HUMANGOLGA2physical
26186194
SPT20_HUMANSPATA20physical
26186194
CDC27_HUMANCDC27physical
26186194
KAP1_HUMANPRKAR1Bphysical
26186194
2A5E_HUMANPPP2R5Ephysical
26186194
ZSWM8_HUMANZSWIM8physical
28514442
AAKB1_HUMANPRKAB1physical
28514442
TRI26_HUMANTRIM26physical
28514442
AAKG2_HUMANPRKAG2physical
28514442
AAPK2_HUMANPRKAA2physical
28514442
ANR52_HUMANANKRD52physical
28514442
AAKB2_HUMANPRKAB2physical
28514442
AAPK1_HUMANPRKAA1physical
28514442
AAKG1_HUMANPRKAG1physical
28514442
SPT20_HUMANSPATA20physical
28514442
AKA11_HUMANAKAP11physical
28514442
ANR28_HUMANANKRD28physical
28514442
PP6R1_HUMANPPP6R1physical
28514442
2A5E_HUMANPPP2R5Ephysical
28514442
CDC27_HUMANCDC27physical
28514442
PP6R2_HUMANPPP6R2physical
28514442
KAPCB_HUMANPRKACBphysical
28514442
MTHR_HUMANMTHFRphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602450Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID)
602450Severe combined immunodeficiency Athabaskan type (SCIDA)
603554Omenn syndrome (OS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCR1C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis inresponse to DNA damage.";
Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K.,Chessa L., Villa A., Lecis D., Delia D., Mizutani S.;
Cancer Sci. 96:134-141(2005).
Cited for: INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, ANDPHOSPHORYLATION AT SER-645.
"Phosphorylation of Artemis following irradiation-induced DNAdamage.";
Poinsignon C., de Chasseval R., Soubeyrand S., Moshous D., Fischer A.,Hache R.J.G., de Villartay J.-P.;
Eur. J. Immunol. 34:3146-3155(2004).
Cited for: FUNCTION, MUTAGENESIS OF SER-516; SER-534; SER-538; SER-548; SER-553;SER-561 AND SER-562, PHOSPHORYLATION BY ATM, AND PHOSPHORYLATION ATSER-645.

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