CTTB2_HUMAN - dbPTM
CTTB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTTB2_HUMAN
UniProt AC Q8WZ74
Protein Name Cortactin-binding protein 2
Gene Name CTTNBP2
Organism Homo sapiens (Human).
Sequence Length 1663
Subcellular Localization Cytoplasm, cell cortex. Cell projection, dendritic spine. Remains associated with dendritic spines even after glutamate stimulation..
Protein Description Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, thus controls dendritic spinogenesis and dendritic spine maintenance..
Protein Sequence MATDGASCEPDLSRAPEDAAGAAAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNRVINEENLPKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQPACSDSSLVIPTTIAFCSSINPVSASSCRPGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRIPAHGNSFNEEESESSVFDLDGGEESPEGISKPVVPADLINHANREGWTAAHIAASKGFKNCLEILCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIEPSNYGSDDLECENTICALNIRKQTSWDDFSKAVSQALTNHFQAISSDGWWSLEDVTCNNTTDSNIGLSARSIRSITLGNVPWSVGQSFAQSPWDFMRKNKAEHITVLLSGPQEGCLSSVTYASMIPLQMMQNYLRLVEQYHNVIFHGPEGSLQDYIVHQLALCLKHRQMAAGFSCEIVRAEVDAGFSKEQLLDLFISSACLIPVKQSPSKKKIIIILENLEKSSLSELLRDFLAPLENRSTESPCTFQKGNGLSECYYFHENCFLMGTIAKACLQGSDLLVQQHFRWVQLRWDGEPMQGLLQRFLRRKVVNKFKGQAPSPCDPVCKIVDWALSVWRQLNSCLARLGTPEALLGPKYFLSCPVVPGHAQVTVKWMSKLWNGVIAPRVQEAILSRASVKRQPGFGQTTAKRHPSQGQQAVVKAALSILLNKAVLHGCPLPRAELDQHTADFKGGSFPLSIVSSYNTCNKKKGESGAWRKVNTSPRRKSGRFSLPTWNKPDLSTEGMKNKTISQLNCNRNASLSKQKSLENDLSLTLNLDQRLSLGSDDEADLVKELQSMCSSKSESDISKIADSRDDLRMFDSSGNNPVLSATINNLRMPVSQKEVSPLSSHQTTECSNSKSKTELGVSRVKSFLPVPRSKVTQCSQNTKRSSSSSNTRQIEINNNSKEVNWNLHKNEHLEKPNK
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
35PhosphorylationKKEFDVDTLSKSELR
HHHCCHHHCCHHHHH		32.5530177828
37PhosphorylationEFDVDTLSKSELRML
HCCHHHCCHHHHHHH		35.9130177828
39PhosphorylationDVDTLSKSELRMLLS
CHHHCCHHHHHHHHH		38.1930177828
126PhosphorylationKKMQERMSAQLAAAE
HHHHHHHHHHHHHHH		21.0520363803
134PhosphorylationAQLAAAESRQKKLEM
HHHHHHHHHHHHHHH		34.9720363803
214PhosphorylationNELEEELSAEKRRST
HHHHHHHHHHHHHHH		37.3526091039
220PhosphorylationLSAEKRRSTEMEAQM
HHHHHHHHHHHHHHH		32.5218491316
221PhosphorylationSAEKRRSTEMEAQME
HHHHHHHHHHHHHHH		37.2218491316
264AcetylationEEIDKMRKMIEQLKR
HHHHHHHHHHHHHHC		40.517706093
270AcetylationRKMIEQLKRGSDSKP
HHHHHHHHCCCCCCC		55.177706103
273PhosphorylationIEQLKRGSDSKPSLS
HHHHHCCCCCCCCCC		42.62-
278PhosphorylationRGSDSKPSLSLPRKT
CCCCCCCCCCCCCCC		34.0428555341
280PhosphorylationSDSKPSLSLPRKTKD
CCCCCCCCCCCCCCC		40.4424719451
331PhosphorylationLTMPVKPSTGSPLVS
CCCCCCCCCCCCCCC		39.4228555341
332PhosphorylationTMPVKPSTGSPLVSA
CCCCCCCCCCCCCCC		50.6428555341
334PhosphorylationPVKPSTGSPLVSANA
CCCCCCCCCCCCCCC		18.3628555341
361PhosphorylationPGIDRQASYGDLIGA
CCCCCCCCCCCCCCC		22.7026657352
436O-linked_GlycosylationHSPCANTSLHPGLNP
CCCCCCCCCCCCCCH		25.2029351928
468PhosphorylationQNGNTTQSPPSRDVS
CCCCCCCCCCCCCCC		36.3623401153
475PhosphorylationSPPSRDVSPTSRDNL
CCCCCCCCCCCHHHH		27.1022496350
477PhosphorylationPSRDVSPTSRDNLVA
CCCCCCCCCHHHHHH		28.9623312004
478PhosphorylationSRDVSPTSRDNLVAK
CCCCCCCCHHHHHHH		40.8123312004
498MethylationTVTQALSRFTSPQAG
HHHHHHHHHCCCCCC		39.45-
498Asymmetric dimethylarginineTVTQALSRFTSPQAG
HHHHHHHHHCCCCCC		39.45-
500PhosphorylationTQALSRFTSPQAGAP
HHHHHHHCCCCCCCC		38.0928555341
501PhosphorylationQALSRFTSPQAGAPS
HHHHHHCCCCCCCCC		16.5928555341
508PhosphorylationSPQAGAPSRPGVPPT
CCCCCCCCCCCCCCC		51.04-
520PhosphorylationPPTGDVGTHPPVGRT
CCCCCCCCCCCCCCC		30.93-
528PhosphorylationHPPVGRTSLKTHGVA
CCCCCCCCCCCCCCE		26.8924719451
553PhosphorylationPPKKPGLSQTPSPPH
CCCCCCCCCCCCCCC		37.6121712546
555PhosphorylationKKPGLSQTPSPPHPQ
CCCCCCCCCCCCCCC		23.5123312004
557PhosphorylationPGLSQTPSPPHPQLK
CCCCCCCCCCCCCEE		55.2228985074
587PhosphorylationDNKTVASTPSSLPQG
CCCCCCCCCCCCCCC		19.9028555341
873PhosphorylationRIPAHGNSFNEEESE
CCCCCCCCCCHHHCC		33.7626471730
879PhosphorylationNSFNEEESESSVFDL
CCCCHHHCCCCCEEC		46.1626471730
881PhosphorylationFNEEESESSVFDLDG
CCHHHCCCCCEECCC		40.8726471730
882PhosphorylationNEEESESSVFDLDGG
CHHHCCCCCEECCCC		23.8126471730
1167PhosphorylationAEVDAGFSKEQLLDL
EECCCCCCHHHHHHH		34.0721815630
1178PhosphorylationLLDLFISSACLIPVK
HHHHHHHHHCCCEEC		20.41-
1187PhosphorylationCLIPVKQSPSKKKII
CCCEECCCCCCCEEE		25.9822817900
1189PhosphorylationIPVKQSPSKKKIIII
CEECCCCCCCEEEEE		63.4522817900
1234PhosphorylationFQKGNGLSECYYFHE
EECCCCCCEEEEEEC		27.3325278378
1237PhosphorylationGNGLSECYYFHENCF
CCCCCEEEEEECCCC		12.7125278378
1238PhosphorylationNGLSECYYFHENCFL
CCCCEEEEEECCCCH		15.3225278378
1248PhosphorylationENCFLMGTIAKACLQ
CCCCHHHHHHHHHHH		12.0925278378
1327PhosphorylationSCLARLGTPEALLGP
HHHHHHCCHHHHHCC		23.6523612710
1404PhosphorylationAVVKAALSILLNKAV
HHHHHHHHHHHHHHH		13.3828857561
1466PhosphorylationNTSPRRKSGRFSLPT
CCCCCCCCCCCCCCC		33.1327251275
1470PhosphorylationRRKSGRFSLPTWNKP
CCCCCCCCCCCCCCC		31.8827251275
1481O-linked_GlycosylationWNKPDLSTEGMKNKT
CCCCCCCCCCCCCCC		43.8029351928
1505PhosphorylationASLSKQKSLENDLSL
CCCCCCHHCCCCHHH		38.1230624053
1521PhosphorylationLNLDQRLSLGSDDEA
EEHHHCCCCCCCCHH		32.6430266825
1524PhosphorylationDQRLSLGSDDEADLV
HHCCCCCCCCHHHHH		47.3719664994
1536PhosphorylationDLVKELQSMCSSKSE
HHHHHHHHHHCCCCH		34.0927251275
1539PhosphorylationKELQSMCSSKSESDI
HHHHHHHCCCCHHHH		31.9627251275
1540PhosphorylationELQSMCSSKSESDIS
HHHHHHCCCCHHHHH		34.9627251275
1542PhosphorylationQSMCSSKSESDISKI
HHHHCCCCHHHHHHH		44.2628985074
1544PhosphorylationMCSSKSESDISKIAD
HHCCCCHHHHHHHCC		47.5427251275
1547PhosphorylationSKSESDISKIADSRD
CCCHHHHHHHCCCHH		24.0127251275
1552PhosphorylationDISKIADSRDDLRMF
HHHHHCCCHHHHHCC		28.7029978859
1561PhosphorylationDDLRMFDSSGNNPVL
HHHHCCCCCCCCCCE		28.9629978859
1562PhosphorylationDLRMFDSSGNNPVLS
HHHCCCCCCCCCCEE		47.5929978859
1569PhosphorylationSGNNPVLSATINNLR
CCCCCCEEEEECCCC		24.4924732914
1571PhosphorylationNNPVLSATINNLRMP
CCCCEEEEECCCCCC		22.3624732914
1585PhosphorylationPVSQKEVSPLSSHQT
CCCHHCCCCCCCCCC		22.6328555341
1611PhosphorylationLGVSRVKSFLPVPRS
CCCCHHHHCCCCCHH		29.2028555341
1621PhosphorylationPVPRSKVTQCSQNTK
CCCHHHCEECCCCCC		27.8229460479
1632PhosphorylationQNTKRSSSSSNTRQI
CCCCCCCCCCCCEEE		38.7523403867
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 CTTB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTTB2_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 CTTB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRN_HUMANSTRNphysical
18782753
STRP1_HUMANSTRIP1physical
18782753
STRN3_HUMANSTRN3physical
18782753
STK26_HUMANSTK26physical
18782753
STRN4_HUMANSTRN4physical
18782753
PHOCN_HUMANMOB4physical
18782753
PDC10_HUMANPDCD10physical
18782753
CT2NL_HUMANCTTNBP2NLphysical
18782753
STRP2_HUMANSTRIP2physical
18782753
TCPB_HUMANCCT2physical
18782753
TCPQ_HUMANCCT8physical
18782753
TCPG_HUMANCCT3physical
18782753
TCPA_HUMANTCP1physical
18782753
TCPE_HUMANCCT5physical
18782753
TCPZ_HUMANCCT6Aphysical
18782753
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 CTTB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1524, AND MASSSPECTROMETRY.

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