ARP21_HUMAN - dbPTM
ARP21_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARP21_HUMAN
UniProt AC Q9UBL0
Protein Name cAMP-regulated phosphoprotein 21
Gene Name ARPP21
Organism Homo sapiens (Human).
Sequence Length 812
Subcellular Localization Cytoplasm.
Protein Description Isoform 2 may act as a competitive inhibitor of calmodulin-dependent enzymes such as calcineurin in neurons..
Protein Sequence MSEQGDLNQAIAEEGGTEQETATPENGIVKSESLDEEEKLELQRRLEAQNQERRKSKSGAGKGKLTRSLAVCEESSARPGGESLQDQESIHLQLSSFSSLQEEDKSRKDDSEREKEKDKNKDKTSEKPKIRMLSKDCSQEYTDSTGIDLHEFLINTLKNNSRDRMILLKMEQEIIDFIADNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTGKSVIINKTSSTRIPEQRFCEHLKDEKGEESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDSVCSQESLFVENSRLLEDSNICNETYKKRQLFRGNRDGSGRTSGSRQSSSENELKWSDHQRAWSSTDSDSSNRNLKPAMTKTASFGGITVLTRGDSTSSTRSTGKLSKAGSESSSSAGSSGSLSRTHPPLQSTPLVSGVAAGSPGCVPYPENGIGGQVAPSSTSYILLPLEAATGIPPGSILLNPHTGQPFVNPDGTPAIYNPPTSQQPLRSAMVGQSQQQPPQQQPSPQPQQQVQPPQPQMAGPLVTQRDDVATQFGQMTLSRQSSGETPEPPSGPVYPSSLMPQPAQQPSYVIASTGQQLPTGGFSGSGPPISQQVLQPPPSPQGFVQQPPPAQMPVYYYPSGQYPTSTTQQYRPMAPVQYNAQRSQQMPQAAQQAGYQPVLSGQQGFQGLIGVQQPPQSQNVINNQQGTPVQSVMVSYPTMSSYQVPMTQGSQGLPQQSYQQPIMLPNQAGQGSLPATGMPVYCNVTPPTPQNNLRLIGPHCPSSTVPVMSASCRTNCASMSNAGWQVKF
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
2Acetylation------MSEQGDLNQ
------CCCCCCHHH		38.33-
31PhosphorylationPENGIVKSESLDEEE
CCCCCCCCCCCCHHH		22.8629691806
33PhosphorylationNGIVKSESLDEEEKL
CCCCCCCCCCHHHHH		48.4928787133
39UbiquitinationESLDEEEKLELQRRL
CCCCHHHHHHHHHHH		51.01-
56PhosphorylationQNQERRKSKSGAGKG
HHHHHHHCCCCCCCC		30.18-
57AcetylationNQERRKSKSGAGKGK
HHHHHHCCCCCCCCC		56.816570387
58PhosphorylationQERRKSKSGAGKGKL
HHHHHCCCCCCCCCH		40.75-
62AcetylationKSKSGAGKGKLTRSL
HCCCCCCCCCHHHHE		52.956570317
64AcetylationKSGAGKGKLTRSLAV
CCCCCCCCHHHHEEE		50.616570313
68PhosphorylationGKGKLTRSLAVCEES
CCCCHHHHEEEHHCC		18.55-
83 (in isoform 2)Phosphorylation-34.31-
88 (in isoform 2)Phosphorylation-61.01-
134PhosphorylationKPKIRMLSKDCSQEY
CHHHHHCCCCCCCCC		19.6628122231
138PhosphorylationRMLSKDCSQEYTDST
HHCCCCCCCCCCCCC		35.8628796482
141PhosphorylationSKDCSQEYTDSTGID
CCCCCCCCCCCCCCC		14.2828796482
142PhosphorylationKDCSQEYTDSTGIDL
CCCCCCCCCCCCCCH		23.7928796482
144PhosphorylationCSQEYTDSTGIDLHE
CCCCCCCCCCCCHHH		22.2727690223
145PhosphorylationSQEYTDSTGIDLHEF
CCCCCCCCCCCHHHH		40.7527690223
156PhosphorylationLHEFLINTLKNNSRD
HHHHHHHHHCCCCCC		31.92-
158UbiquitinationEFLINTLKNNSRDRM
HHHHHHHCCCCCCCE		52.63-
186UbiquitinationADNNNHYKKFPQMSS
HCCCCCHHCCCCCHH		40.15-
187UbiquitinationDNNNHYKKFPQMSSY
CCCCCHHCCCCCHHH		55.93-
187 (in isoform 3)Ubiquitination-55.93-
215PhosphorylationLDHNVDQTGKSVIIN
CCCCCCCCCCEEEEE		41.96-
217 (in isoform 3)Ubiquitination-44.96-
217UbiquitinationHNVDQTGKSVIINKT
CCCCCCCCEEEEECC		44.96-
218PhosphorylationNVDQTGKSVIINKTS
CCCCCCCEEEEECCC		21.64-
223 (in isoform 3)Ubiquitination-39.10-
223UbiquitinationGKSVIINKTSSTRIP
CCEEEEECCCCCCCC		39.10-
257PhosphorylationFILKRDNSSIDKEDN
EEEECCCCCCCCCCC		32.7228787133
258PhosphorylationILKRDNSSIDKEDNQ
EEECCCCCCCCCCCC		40.8528787133
278PhosphorylationPFRDDRRSKSIEERE
CCCCCHHHCCHHHHH		31.4821955146
280PhosphorylationRDDRRSKSIEEREEE
CCCHHHCCHHHHHHH		36.1623401153
284MethylationRSKSIEEREEEYQRV
HHCCHHHHHHHHHHH		43.78-
288PhosphorylationIEEREEEYQRVRERI
HHHHHHHHHHHHHHH		12.6128796482
300PhosphorylationERIFAHDSVCSQESL
HHHHCCCCCCCCHHH		18.37-
318PhosphorylationNSRLLEDSNICNETY
CHHHHCCCCCCCHHH		20.7929083192
324PhosphorylationDSNICNETYKKRQLF
CCCCCCHHHHHHHCC		27.0129083192
325PhosphorylationSNICNETYKKRQLFR
CCCCCHHHHHHHCCC		14.3429083192
326UbiquitinationNICNETYKKRQLFRG
CCCCHHHHHHHCCCC		49.23-
338PhosphorylationFRGNRDGSGRTSGSR
CCCCCCCCCCCCCCC		29.4124719451
344PhosphorylationGSGRTSGSRQSSSEN
CCCCCCCCCCCCCCC		27.2424719451
363PhosphorylationSDHQRAWSSTDSDSS
CCCCHHHHCCCCCCC		23.5230576142
364PhosphorylationDHQRAWSSTDSDSSN
CCCHHHHCCCCCCCC		26.0730576142
365PhosphorylationHQRAWSSTDSDSSNR
CCHHHHCCCCCCCCC		33.7230576142
367PhosphorylationRAWSSTDSDSSNRNL
HHHHCCCCCCCCCCC		39.2126546556
369PhosphorylationWSSTDSDSSNRNLKP
HHCCCCCCCCCCCCH		33.2028634298
370PhosphorylationSSTDSDSSNRNLKPA
HCCCCCCCCCCCCHH		44.8128634298
375UbiquitinationDSSNRNLKPAMTKTA
CCCCCCCCHHHEEEE		33.99-
381PhosphorylationLKPAMTKTASFGGIT
CCHHHEEEECCCCEE		20.5428787133
383PhosphorylationPAMTKTASFGGITVL
HHHEEEECCCCEEEE		29.6528787133
388PhosphorylationTASFGGITVLTRGDS
EECCCCEEEEECCCC		16.8530576142
391PhosphorylationFGGITVLTRGDSTSS
CCCEEEEECCCCCCC		28.4126074081
395PhosphorylationTVLTRGDSTSSTRST
EEEECCCCCCCCCCC		32.7726074081
396PhosphorylationVLTRGDSTSSTRSTG
EEECCCCCCCCCCCC		31.2826074081
397PhosphorylationLTRGDSTSSTRSTGK
EECCCCCCCCCCCCC		33.3926074081
398PhosphorylationTRGDSTSSTRSTGKL
ECCCCCCCCCCCCCE		28.1126074081
399PhosphorylationRGDSTSSTRSTGKLS
CCCCCCCCCCCCCEE		28.5426074081
401PhosphorylationDSTSSTRSTGKLSKA
CCCCCCCCCCCEECC		41.4226074081
402PhosphorylationSTSSTRSTGKLSKAG
CCCCCCCCCCEECCC		34.7426074081
410PhosphorylationGKLSKAGSESSSSAG
CCEECCCCCCCCCCC		38.8830576142
412PhosphorylationLSKAGSESSSSAGSS
EECCCCCCCCCCCCC		36.9024245541
414PhosphorylationKAGSESSSSAGSSGS
CCCCCCCCCCCCCCC		33.22-
415PhosphorylationAGSESSSSAGSSGSL
CCCCCCCCCCCCCCC		38.3028111955
418PhosphorylationESSSSAGSSGSLSRT
CCCCCCCCCCCCCCC		31.1028111955
419PhosphorylationSSSSAGSSGSLSRTH
CCCCCCCCCCCCCCC		31.3328111955
421PhosphorylationSSAGSSGSLSRTHPP
CCCCCCCCCCCCCCC		25.7230576142
560PhosphorylationATQFGQMTLSRQSSG
HHHHHCEEECCCCCC		17.4428122231
562PhosphorylationQFGQMTLSRQSSGET
HHHCEEECCCCCCCC		21.0726074081
565PhosphorylationQMTLSRQSSGETPEP
CEEECCCCCCCCCCC		38.9226074081
566PhosphorylationMTLSRQSSGETPEPP
EEECCCCCCCCCCCC		32.1026074081
569PhosphorylationSRQSSGETPEPPSGP
CCCCCCCCCCCCCCC		36.1626074081
655MethylationTSTTQQYRPMAPVQY
CCCCCCCCCCCCHHH		15.3515096520
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 ARP21_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
56SPhosphorylation

19690332
655RMethylation

15096520
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 ARP21_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARP21_HUMAN !!
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 ARP21_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-383 AND SER-562,AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASSSPECTROMETRY.

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