CSR2B_HUMAN - dbPTM
CSR2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSR2B_HUMAN
UniProt AC Q9H8E8
Protein Name Cysteine-rich protein 2-binding protein
Gene Name KAT14 {ECO:0000312|HGNC:HGNC:15904}
Organism Homo sapiens (Human).
Sequence Length 782
Subcellular Localization Nucleus. Cytoplasm. Mainly nuclear.
Protein Description Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle..
Protein Sequence MDSSIHLSSLISRHDDEATRTSTSEGLEEGEVEGETLLIVESEDQASVDLSHDQSGDSLNSDEGDVSWMEEQLSYFCDKCQKWIPASQLREQLSYLKGDNFFRFTCSDCSADGKEQYERLKLTWQQVVMLAMYNLSLEGSGRQGYFRWKEDICAFIEKHWTFLLGNRKKTSTWWSTVAGCLSVGSPMYFRSGAQEFGEPGWWKLVHNKPPTMKPEGEKLSASTLKIKAASKPTLDPIITVEGLRKRASRNPVESAMELKEKRSRTQEAKDIRRAQKEAAGFLDRSTSSTPVKFISRGRRPDVILEKGEVIDFSSLSSSDRTPLTSPSPSPSLDFSAPGTPASHSATPSLLSEADLIPDVMPPQALFHDDDEMEGDGVIDPGMEYVPPPAGSVASGPVVGVRKKVRGPEQIKQEVESEEEKPDRMDIDSEDTDSNTSLQTRAREKRKPQLEKDTKPKEPRYTPVSIYEEKLLLKRLEACPGAVAMTPEARRLKRKLIVRQAKRDRGLPLFDLDQVVNAALLLVDGIYGAKEGGISRLPAGQATYRTTCQDFRILDRYQTSLPSRKGFRHQTTKFLYRLVGSEDMAVDQSIVSPYTSRILKPYIRRDYETKPPKLQLLSQIRSHLHRSDPHWTPEPDAPLDYCYVRPNHIPTINSMCQEFFWPGIDLSECLQYPDFSVVVLYKKVIIAFGFMVPDVKYNEAYISFLFVHPEWRRAGIATFMIYHLIQTCMGKDVTLHVSASNPAMLLYQKFGFKTEEYVLDFYDKYYPLESTECKHAFFLRLRR
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
3Phosphorylation-----MDSSIHLSSL
-----CCCCEEHHHH		29.8723186163
4Phosphorylation----MDSSIHLSSLI
----CCCCEEHHHHH		15.1227174698
8PhosphorylationMDSSIHLSSLISRHD
CCCCEEHHHHHHHCC		14.6727174698
9PhosphorylationDSSIHLSSLISRHDD
CCCEEHHHHHHHCCC		35.7627174698
12PhosphorylationIHLSSLISRHDDEAT
EEHHHHHHHCCCCCC		28.9327174698
19PhosphorylationSRHDDEATRTSTSEG
HHCCCCCCCCCCCCC		32.2227174698
97UbiquitinationREQLSYLKGDNFFRF
HHHHHHHCCCCEEEE		56.86-
105PhosphorylationGDNFFRFTCSDCSAD
CCCEEEEEECCCCCC		13.5729052541
107PhosphorylationNFFRFTCSDCSADGK
CEEEEEECCCCCCCH		38.3029052541
110PhosphorylationRFTCSDCSADGKEQY
EEEECCCCCCCHHHH		34.0929052541
117PhosphorylationSADGKEQYERLKLTW
CCCCHHHHHHHCCHH		12.24-
123PhosphorylationQYERLKLTWQQVVML
HHHHHCCHHHHHHHH		21.46-
185PhosphorylationAGCLSVGSPMYFRSG
HHHCCCCCCEEECCC		12.3528555341
218"N6,N6-dimethyllysine"TMKPEGEKLSASTLK
CCCCCCCCCCHHHEE		59.61-
218MethylationTMKPEGEKLSASTLK
CCCCCCCCCCHHHEE		59.61-
220PhosphorylationKPEGEKLSASTLKIK
CCCCCCCCHHHEEEE		31.1023312004
222PhosphorylationEGEKLSASTLKIKAA
CCCCCCHHHEEEEEC		30.7823312004
223PhosphorylationGEKLSASTLKIKAAS
CCCCCHHHEEEEECC		31.6123312004
231AcetylationLKIKAASKPTLDPII
EEEEECCCCCCCCEE		36.9826051181
248PhosphorylationEGLRKRASRNPVESA
HHHHHHHHCCHHHHH		36.3028555341
265PhosphorylationLKEKRSRTQEAKDIR
HHHHHHHHHHHHHHH		31.8225106551
269AcetylationRSRTQEAKDIRRAQK
HHHHHHHHHHHHHHH		53.5923749302
276AcetylationKDIRRAQKEAAGFLD
HHHHHHHHHHCCCCC		48.6225953088
285PhosphorylationAAGFLDRSTSSTPVK
HCCCCCCCCCCCCEE		32.1025159151
286PhosphorylationAGFLDRSTSSTPVKF
CCCCCCCCCCCCEEE		27.8228450419
287PhosphorylationGFLDRSTSSTPVKFI
CCCCCCCCCCCEEEC		33.2028450419
288PhosphorylationFLDRSTSSTPVKFIS
CCCCCCCCCCEEECC		36.5028450419
289PhosphorylationLDRSTSSTPVKFISR
CCCCCCCCCEEECCC		31.6925159151
292AcetylationSTSSTPVKFISRGRR
CCCCCCEEECCCCCC		37.8819608861
295PhosphorylationSTPVKFISRGRRPDV
CCCEEECCCCCCCCE		31.6423312004
324PhosphorylationSSDRTPLTSPSPSPS
CCCCCCCCCCCCCCC		39.5326074081
325PhosphorylationSDRTPLTSPSPSPSL
CCCCCCCCCCCCCCC		30.9426074081
327PhosphorylationRTPLTSPSPSPSLDF
CCCCCCCCCCCCCCC		37.4626074081
329PhosphorylationPLTSPSPSPSLDFSA
CCCCCCCCCCCCCCC		31.3026074081
335PhosphorylationPSPSLDFSAPGTPAS
CCCCCCCCCCCCCCC		32.9726074081
339PhosphorylationLDFSAPGTPASHSAT
CCCCCCCCCCCCCCC		18.0226074081
342PhosphorylationSAPGTPASHSATPSL
CCCCCCCCCCCCHHH		21.1226074081
344PhosphorylationPGTPASHSATPSLLS
CCCCCCCCCCHHHHC		31.2026074081
394PhosphorylationPPAGSVASGPVVGVR
CCCCCCCCCCEEEEE		41.28-
416PhosphorylationQIKQEVESEEEKPDR
HHHHHHHCCCCCCCC		56.3223401153
428PhosphorylationPDRMDIDSEDTDSNT
CCCCCCCCCCCCCCH		37.3923663014
431PhosphorylationMDIDSEDTDSNTSLQ
CCCCCCCCCCCHHHH		36.9623663014
433PhosphorylationIDSEDTDSNTSLQTR
CCCCCCCCCHHHHHH		44.0623663014
435PhosphorylationSEDTDSNTSLQTRAR
CCCCCCCHHHHHHHH		34.4627732954
436PhosphorylationEDTDSNTSLQTRARE
CCCCCCHHHHHHHHH		23.8025849741
439PhosphorylationDSNTSLQTRAREKRK
CCCHHHHHHHHHHCC		31.4318669648
444AcetylationLQTRAREKRKPQLEK
HHHHHHHHCCCCCCC		61.23-
461PhosphorylationKPKEPRYTPVSIYEE
CCCCCCCCCCCHHHH		20.6321815630
485PhosphorylationCPGAVAMTPEARRLK
CCCCCCCCHHHHHHH		14.2928450419
526PhosphorylationLLLVDGIYGAKEGGI
HHHHHHCCCCCCCCC		19.29-
572AcetylationGFRHQTTKFLYRLVG
CCCHHHHHHHHHHHC		36.4423954790
599UbiquitinationPYTSRILKPYIRRDY
HHHHHCCHHHHCCCC		33.14-
606PhosphorylationKPYIRRDYETKPPKL
HHHHCCCCCCCCCHH		24.5625002506
608PhosphorylationYIRRDYETKPPKLQL
HHCCCCCCCCCHHHH		42.4925002506
717PhosphorylationWRRAGIATFMIYHLI
HHHHHHHHHHHHHHH		16.3023401153
721PhosphorylationGIATFMIYHLIQTCM
HHHHHHHHHHHHHHC		4.4523401153
726PhosphorylationMIYHLIQTCMGKDVT
HHHHHHHHHCCCCEE		9.4723401153
763AcetylationYVLDFYDKYYPLEST
EEHHHHHHHCCCCCC		34.9926051181
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 CSR2B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSR2B_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 CSR2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MBIP1_HUMANMBIPphysical
19060904
H31_HUMANHIST1H3Aphysical
19103755
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSR2B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-292 AND LYS-572, AND MASSSPECTROMETRY.

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