CC88B_HUMAN - dbPTM
CC88B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC88B_HUMAN
UniProt AC A6NC98
Protein Name Coiled-coil domain-containing protein 88B
Gene Name CCDC88B
Organism Homo sapiens (Human).
Sequence Length 1476
Subcellular Localization Membrane
Peripheral membrane protein . Cytoplasm, cytoskeleton, microtubule organizing center . Endoplasmic reticulum . Golgi apparatus . Cytoplasm .
Protein Description Acts as a positive regulator of T-cell maturation and inflammatory function. Required for several functions of T-cells, in both the CD4(+) and the CD8(+) compartments and this includes expression of cell surface markers of activation, proliferation, and cytokine production in response to specific or non-specific stimulation (By similarity). Enhances NK cell cytotoxicity by positively regulating polarization of microtubule-organizing center (MTOC) to cytotoxic synapse, lytic granule transport along microtubules, and dynein-mediated clustering to MTOC. [PubMed: 25762780 Interacts with HSPA5 and stabilizes the interaction between HSPA5 and ERN1, leading to suppression of ERN1-induced JNK activation and endoplasmic reticulum stress-induced apoptosis]
Protein Sequence MEGGKGPRLRDFLSGSLATWALGLAGLVGEAEDSEGEEEEEEEEPPLWLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQASDWSPQESGSPVETQESPEKAGRRSSLQSPASVAPPQGPGTKIQAPQLLGGETEGREAPQGELVPEAWGLRQEGPEHKPGPSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQKPQQKSEGALEVQVWEGPIPGESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPVPLPRTKKGSWLADKVKRLMRPRREGGPPGGLRLGADGAGSTESLGGPPETELPEGREADGTGSPSPAPMRRAQSSLCLRDETLAGGQRRKLSSRFPVGRSSESFSPGDTPRQRFRQRHPGPLGAPVSHSKGPGVGWENSAETLQEHETDANREGPEVQEPEKRPLTPSLSQ
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
5Ubiquitination---MEGGKGPRLRDF
---CCCCCCCCHHHH		76.29-
57PhosphorylationEKRFLRLSDGALLLR
HHHHHHHCHHHHHHH		27.80-
310UbiquitinationQALSGQAKRAELYRE
HHHHHHHHHHHHHHH		44.23-
429PhosphorylationLELELQRSLEPPPGS
HHHHHHHHCCCCCCC		24.9128450419
436PhosphorylationSLEPPPGSPGEAPLA
HCCCCCCCCCCCCCC		35.1928348404
448PhosphorylationPLAGAAPSLQDEVRE
CCCCCCCCHHHHHHH		33.6626074081
489 (in isoform 5)Phosphorylation-6.59-
507PhosphorylationVLEEAPQTPVAFDHS
CCCCCCCCCCCCCCC		20.7627080861
514PhosphorylationTPVAFDHSPQGLVQK
CCCCCCCCCCHHHHH		22.2927080861
539PhosphorylationLAPPALDSVLEASAE
HCCHHHHHHHHHHHC		29.4726074081
544PhosphorylationLDSVLEASAECPQAP
HHHHHHHHHCCCCCC		18.4126074081
553PhosphorylationECPQAPDSDPQEAES
CCCCCCCCCHHHCCC		50.5626074081
559 (in isoform 5)Phosphorylation-52.7328450419
560PhosphorylationSDPQEAESPLQAAAM
CCHHHCCCHHHHHHC		37.6526074081
563 (in isoform 5)Phosphorylation-32.1328450419
565 (in isoform 5)Phosphorylation-7.1428450419
567 (in isoform 5)Phosphorylation-7.1028450419
570 (in isoform 5)Phosphorylation-49.5928450419
572PhosphorylationAAMDPQASDWSPQES
HHCCCCCCCCCCCCC		34.0726074081
596PhosphorylationPEKAGRRSSLQSPAS
HHHCCCCCCCCCCCC		33.7623401153
597PhosphorylationEKAGRRSSLQSPASV
HHCCCCCCCCCCCCC		28.7228674151
600PhosphorylationGRRSSLQSPASVAPP
CCCCCCCCCCCCCCC		27.9423882029
603PhosphorylationSSLQSPASVAPPQGP
CCCCCCCCCCCCCCC		23.3830108239
612PhosphorylationAPPQGPGTKIQAPQL
CCCCCCCCCCCCCHH		28.2723684312
833PhosphorylationRQWEREGSRLRAQSE
HHHHHHHHHHHHHHH		24.3223403867
839PhosphorylationGSRLRAQSEAAEERM
HHHHHHHHHHHHHHH		28.3723403867
986PhosphorylationRLIEVERSNAMLVAE
EEEEEEHHHHHHHHH		18.5528796482
988 (in isoform 2)Phosphorylation-8.2424670416
1253PhosphorylationLAEVQALSRENRELL
HHHHHHHHHHHHHHH		40.3325159151
1277PhosphorylationLHREQREYLDQLNAL
HHHHHHHHHHHHHHH		20.12-
1345PhosphorylationLGADGAGSTESLGGP
CCCCCCCCCCCCCCC		28.5928450419
1346PhosphorylationGADGAGSTESLGGPP
CCCCCCCCCCCCCCC		28.7728450419
1348PhosphorylationDGAGSTESLGGPPET
CCCCCCCCCCCCCCC		32.1928450419
1355PhosphorylationSLGGPPETELPEGRE
CCCCCCCCCCCCCCC		48.9027080861
1366PhosphorylationEGREADGTGSPSPAP
CCCCCCCCCCCCCHH		34.7328450419
1368PhosphorylationREADGTGSPSPAPMR
CCCCCCCCCCCHHHH		23.2623401153
1370PhosphorylationADGTGSPSPAPMRRA
CCCCCCCCCHHHHHH		35.0828450419
1379PhosphorylationAPMRRAQSSLCLRDE
HHHHHHHHCEECCCC		25.0523401153
1380PhosphorylationPMRRAQSSLCLRDET
HHHHHHHCEECCCCC		15.8323401153
1387PhosphorylationSLCLRDETLAGGQRR
CEECCCCCCCCCCCC		26.6329978859
1397PhosphorylationGGQRRKLSSRFPVGR
CCCCCCCHHCCCCCC		23.6226074081
1398PhosphorylationGQRRKLSSRFPVGRS
CCCCCCHHCCCCCCC		48.6726074081
1405PhosphorylationSRFPVGRSSESFSPG
HCCCCCCCCCCCCCC		32.3128450419
1406PhosphorylationRFPVGRSSESFSPGD
CCCCCCCCCCCCCCC		35.5826657352
1408PhosphorylationPVGRSSESFSPGDTP
CCCCCCCCCCCCCCH		32.7323401153
1410PhosphorylationGRSSESFSPGDTPRQ
CCCCCCCCCCCCHHH		36.9328450419
1414PhosphorylationESFSPGDTPRQRFRQ
CCCCCCCCHHHHHHH		26.7028450419
1444PhosphorylationPGVGWENSAETLQEH
CCCCCCCHHHHHHHH		18.9029978859
1447PhosphorylationGWENSAETLQEHETD
CCCCHHHHHHHHCCC		33.2029978859
1453PhosphorylationETLQEHETDANREGP
HHHHHHCCCCCCCCC		42.1729978859
1471PhosphorylationEPEKRPLTPSLSQ--
CCCCCCCCCCCCC--		17.3223401153
1473PhosphorylationEKRPLTPSLSQ----
CCCCCCCCCCC----		35.1028450419
1475PhosphorylationRPLTPSLSQ------
CCCCCCCCC------		37.8823401153
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 CC88B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC88B_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 CC88B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CC88B_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 CC88B_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-436 AND SER-1408, ANDMASS SPECTROMETRY.

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