CMIP_HUMAN - dbPTM
CMIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMIP_HUMAN
UniProt AC Q8IY22
Protein Name C-Maf-inducing protein
Gene Name CMIP
Organism Homo sapiens (Human).
Sequence Length 773
Subcellular Localization Nucleus . Cytoplasm . Isoform 2 is translocated to the nucleus and is specifically recruited during minimal change nephrotic syndrome (MCNS) (PubMed:12939343) (PubMed:15616553). Detected in nuclear and cytoplasmic compartments during MCNS relapse (Pu
Protein Description Plays a role in T-cell signaling pathway. Isoform 2 may play a role in T-helper 2 (Th2) signaling pathway and seems to represent the first proximal signaling protein that links T-cell receptor-mediated signal to the activation of c-Maf Th2 specific factor..
Protein Sequence MDVTSSSGGGGDPRQIEETKPLLGGDVSAPEGTKMGAVPCRRALLLCNGMRYKLLQEGDIQVCVIRHPRTFLSKILTSKFLRRWEPHHLTLADNSLASATPTGYMENSVSYSAIEDVQLLSWENAPKYCLQLTIPGGTVLLQAANSYLRDQWFHSLQWKKKIYKYKKVLSNPSRWEVVLKEIRTLVDMALTSPLQDDSINQAPLEIVSKLLSENTNLTTQEHENIIVAIAPLLENNHPPPDLCEFFCKHCRERPRSMVVIEVFTPVVQRILKHNMDFGKCPRLRLFTQEYILALNELNAGMEVVKKFIQSMHGPTGHCPHPRVLPNLVAVCLAAIYSCYEEFINSRDNSPSLKEIRNGCQQPCDRKPTLPLRLLHPSPDLVSQEATLSEARLKSVVVASSEIHVEVERTSTAKPALTASAGNDSEPNLIDCLMVSPACSTMSIELGPQADRTLGCYVEILKLLSDYDDWRPSLASLLQPIPFPKEALAHEKFTKELKYVIQRFAEDPRQEVHSCLLSVRAGKDGWFQLYSPGGVACDDDGELFASMVHILMGSCYKTKKFLLSLAENKLGPCMLLALRGNQTMVEILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLENLSLAFTNVTSACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSMKSLCSLNMNSTKLSADTYEDLKAKLPNLKEVDVRYTEAW
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
7Phosphorylation-MDVTSSSGGGGDPR
-CCCCCCCCCCCCHH		41.0222210691
8 (in isoform 2)Phosphorylation-40.4924719451
20SumoylationPRQIEETKPLLGGDV
HHHHCCCCCCCCCCC		36.63-
20SumoylationPRQIEETKPLLGGDV
HHHHCCCCCCCCCCC		36.63-
20UbiquitinationPRQIEETKPLLGGDV
HHHHCCCCCCCCCCC		36.63-
20 (in isoform 1)Ubiquitination-36.6321890473
27 (in isoform 2)Phosphorylation-6.2624719451
34UbiquitinationVSAPEGTKMGAVPCR
CCCCCCCCCCCCCCH		46.31-
73PhosphorylationRHPRTFLSKILTSKF
ECCHHHHHHHHHHHH		17.29-
74UbiquitinationHPRTFLSKILTSKFL
CCHHHHHHHHHHHHH		43.8321890473
74 (in isoform 1)Ubiquitination-43.8321890473
77PhosphorylationTFLSKILTSKFLRRW
HHHHHHHHHHHHHHC		33.09-
78PhosphorylationFLSKILTSKFLRRWE
HHHHHHHHHHHHHCC		20.26-
79UbiquitinationLSKILTSKFLRRWEP
HHHHHHHHHHHHCCC		43.0921890473
79 (in isoform 1)Ubiquitination-43.0921890473
121PhosphorylationIEDVQLLSWENAPKY
HCCEEEECCCCCCCE		40.72-
146PhosphorylationVLLQAANSYLRDQWF
HHHHHHHHHHHHHHH		22.33-
147PhosphorylationLLQAANSYLRDQWFH
HHHHHHHHHHHHHHH		12.93-
155PhosphorylationLRDQWFHSLQWKKKI
HHHHHHHHHHHHHHH		16.8720873877
167UbiquitinationKKIYKYKKVLSNPSR
HHHHHHHHHHCCHHH		45.37-
170PhosphorylationYKYKKVLSNPSRWEV
HHHHHHHCCHHHHHH		50.08-
173PhosphorylationKKVLSNPSRWEVVLK
HHHHCCHHHHHHHHH		55.03-
180UbiquitinationSRWEVVLKEIRTLVD
HHHHHHHHHHHHHHH		39.21-
191PhosphorylationTLVDMALTSPLQDDS
HHHHHHHCCCCCCCC		20.8228270605
192PhosphorylationLVDMALTSPLQDDSI
HHHHHHCCCCCCCCC		25.1828270605
198PhosphorylationTSPLQDDSINQAPLE
CCCCCCCCCCHHHHH		31.5628270605
211 (in isoform 3)Ubiquitination-7.4921906983
255 (in isoform 2)Phosphorylation-43.5424719451
256PhosphorylationHCRERPRSMVVIEVF
HHHHCCCCEEEEEEC		20.7228270605
259 (in isoform 2)Ubiquitination-2.0121906983
272UbiquitinationPVVQRILKHNMDFGK
HHHHHHHHCCCCCCC		30.48-
279UbiquitinationKHNMDFGKCPRLRLF
HCCCCCCCCCHHHHH		40.85-
283 (in isoform 2)Phosphorylation-3.1824719451
337O-linked_GlycosylationVCLAAIYSCYEEFIN
HHHHHHHHHHHHHHH		12.2429485866
349PhosphorylationFINSRDNSPSLKEIR
HHHCCCCCCCHHHHH		21.8322167270
351PhosphorylationNSRDNSPSLKEIRNG
HCCCCCCCHHHHHCC		52.4722167270
353 (in isoform 1)Ubiquitination-56.2721890473
353UbiquitinationRDNSPSLKEIRNGCQ
CCCCCCHHHHHCCCC		56.27-
366UbiquitinationCQQPCDRKPTLPLRL
CCCCCCCCCCCCCCC		29.15-
368PhosphorylationQPCDRKPTLPLRLLH
CCCCCCCCCCCCCCC		44.0023312004
377PhosphorylationPLRLLHPSPDLVSQE
CCCCCCCCCCCCCCC		21.9429255136
382PhosphorylationHPSPDLVSQEATLSE
CCCCCCCCCCCCCCH		29.6023403867
386PhosphorylationDLVSQEATLSEARLK
CCCCCCCCCCHHHHH		30.0223403867
388PhosphorylationVSQEATLSEARLKSV
CCCCCCCCHHHHHEE		25.5123403867
409PhosphorylationIHVEVERTSTAKPAL
EEEEEEECCCCCCCE		19.54-
410PhosphorylationHVEVERTSTAKPALT
EEEEEECCCCCCCEE		32.37-
411PhosphorylationVEVERTSTAKPALTA
EEEEECCCCCCCEEC		37.78-
419PhosphorylationAKPALTASAGNDSEP
CCCCEECCCCCCCCC		31.3228102081
424PhosphorylationTASAGNDSEPNLIDC
ECCCCCCCCCCCHHH		59.9828348404
435PhosphorylationLIDCLMVSPACSTMS
CHHHEEECCCCCEEE		7.8828102081
439PhosphorylationLMVSPACSTMSIELG
EEECCCCCEEEEECC		29.2928102081
440PhosphorylationMVSPACSTMSIELGP
EECCCCCEEEEECCC		18.1528102081
442PhosphorylationSPACSTMSIELGPQA
CCCCCEEEEECCCCC		17.0128102081
456PhosphorylationADRTLGCYVEILKLL
CCHHHHHHHHHHHHH		10.1829396449
491UbiquitinationKEALAHEKFTKELKY
HHHHHCHHHHHHHHH		48.76-
593 (in isoform 2)Phosphorylation-14.0124719451
614 (in isoform 3)Ubiquitination-11.1721906983
645PhosphorylationPTRLTLPSKSTDADL
CCCEECCCCCCHHHH		42.2124719451
646UbiquitinationTRLTLPSKSTDADLA
CCEECCCCCCHHHHH		56.27-
647PhosphorylationRLTLPSKSTDADLAR
CEECCCCCCHHHHHH		35.54-
648PhosphorylationLTLPSKSTDADLARL
EECCCCCCHHHHHHH		38.65-
657PhosphorylationADLARLLSSGSFGNL
HHHHHHHHCCCCCCC		36.9328060719
658PhosphorylationDLARLLSSGSFGNLE
HHHHHHHCCCCCCCC		38.1228060719
658 (in isoform 2)Phosphorylation-38.1227642862
660PhosphorylationARLLSSGSFGNLENL
HHHHHCCCCCCCCHH		31.7428450419
662 (in isoform 2)Ubiquitination-39.2421906983
668PhosphorylationFGNLENLSLAFTNVT
CCCCCHHHHHEECHH		29.2728060719
672PhosphorylationENLSLAFTNVTSACA
CHHHHHEECHHHHHH		24.1528060719
687PhosphorylationEHLIKLPSLKQLNLW
HHHHCCCCHHHHCCC		59.6524719451
707PhosphorylationDAGLRLLSEHLTMLQ
HHHHHHHHHHHHHHH		27.80-
736PhosphorylationLALSSMKSLCSLNMN
HHHHHHHHHHCCCCC		26.43-
739PhosphorylationSSMKSLCSLNMNSTK
HHHHHHHCCCCCCCC		28.24-
746UbiquitinationSLNMNSTKLSADTYE
CCCCCCCCCCCCCHH		40.02-
751PhosphorylationSTKLSADTYEDLKAK
CCCCCCCCHHHHHHH		28.6428796482
752PhosphorylationTKLSADTYEDLKAKL
CCCCCCCHHHHHHHC		14.1628796482
756 (in isoform 1)Ubiquitination-56.6621890473
756UbiquitinationADTYEDLKAKLPNLK
CCCHHHHHHHCCCCC		56.66-
769PhosphorylationLKEVDVRYTEAW---
CCCCCCCEECCC---		14.58-
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 CMIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMIP_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 CMIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLNA_HUMANFLNAphysical
15128042
P85A_HUMANPIK3R1physical
20018188
MIB1_HUMANMIB1physical
20018188
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 CMIP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASSSPECTROMETRY.

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