CD2AP_MOUSE - dbPTM
CD2AP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD2AP_MOUSE
UniProt AC Q9JLQ0
Protein Name CD2-associated protein
Gene Name Cd2ap
Organism Mus musculus (Mouse).
Sequence Length 637
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, ruffle . Cell junction . Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (By similarity). Located at podocyte slit diaphragm between podocyte foot processes (PubMed:10514378, PubMed:11733379).
Protein Description Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (By similarity). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. [PubMed: 9741631 May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus]
Protein Sequence MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKRETEPKDDNLPIKRERQGNVASLVQRISTYGLPAGGIQPHPQTKAIKKKTKKRQCKVLFDYSPQNEDELELIVGDVIDVIEEVEEGWWSGTLNNKLGLFPSNFVKELESTEDGETHNAQEESEVPLTGPTSPLPSPGNGSEPAPGSVAQPKKIRGIGFGDIFKEGSVKLRTRTSSSETEEKKTEKPLILQPLGSRTQNVEVTKPDVDGKIKAKEYCRTLFPYTGTNEDELTFREGEIIHLISKETGEAGWWKGELNGKEGVFPDNFAVQISELDKDFPKPKKPPPPAKGPAPKPDLSAAEKKAFPLKAEEKDEKSLLEQKPSKPAAPQVPPKKPTAPTKASNLLRSPGAVYPKRPEKPVPPPPPAAKINGEVSIISSKIDTEPVSKPKLDPEQLPVRPKSVDLDAFVARNSKETDDVNFDDIASSENLLHLTANRPKMPGRRLPGRFNGGHSPTQSPEKTLKLPKEDDSGNLKPLEFKKDASYSSKSSLSTPSSASKVNTAAFLTPLELKAKAEADDGKRNSVDELRAQIIELLCIVDALKKDHGKELEKLRKELEEEKAMRSNLEVEIAKLKKAVLLS
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
71UbiquitinationKDDNLPIKRERQGNV
CCCCCCCCHHHCCCH
46.3922790023
80PhosphorylationERQGNVASLVQRIST
HHCCCHHHHHHHHHH
25.4529176673
86PhosphorylationASLVQRISTYGLPAG
HHHHHHHHHHCCCCC
20.1227087446
87PhosphorylationSLVQRISTYGLPAGG
HHHHHHHHHCCCCCC
21.1627600695
88PhosphorylationLVQRISTYGLPAGGI
HHHHHHHHCCCCCCC
15.1821183079
102UbiquitinationIQPHPQTKAIKKKTK
CCCCHHCHHHHHHCC
42.7522790023
167PhosphorylationNFVKELESTEDGETH
HHHHHHHCCCCCCCC
50.1223649490
168PhosphorylationFVKELESTEDGETHN
HHHHHHCCCCCCCCC
28.8125777480
173PhosphorylationESTEDGETHNAQEES
HCCCCCCCCCCCCCC
26.4225777480
180PhosphorylationTHNAQEESEVPLTGP
CCCCCCCCCCCCCCC
43.0426239621
185PhosphorylationEESEVPLTGPTSPLP
CCCCCCCCCCCCCCC
34.7425777480
188PhosphorylationEVPLTGPTSPLPSPG
CCCCCCCCCCCCCCC
44.3025777480
189PhosphorylationVPLTGPTSPLPSPGN
CCCCCCCCCCCCCCC
27.8021659605
193PhosphorylationGPTSPLPSPGNGSEP
CCCCCCCCCCCCCCC
53.7921659605
198PhosphorylationLPSPGNGSEPAPGSV
CCCCCCCCCCCCCCC
44.3925777480
204PhosphorylationGSEPAPGSVAQPKKI
CCCCCCCCCCCCCEE
17.1425777480
214UbiquitinationQPKKIRGIGFGDIFK
CCCEECCCCCCHHHC
2.7227667366
221UbiquitinationIGFGDIFKEGSVKLR
CCCCHHHCCCEEEEE
62.5922790023
224PhosphorylationGDIFKEGSVKLRTRT
CHHHCCCEEEEEECC
19.7126824392
229PhosphorylationEGSVKLRTRTSSSET
CCEEEEEECCCCCCC
49.0527087446
231PhosphorylationSVKLRTRTSSSETEE
EEEEEECCCCCCCCC
32.1420139300
232PhosphorylationVKLRTRTSSSETEEK
EEEEECCCCCCCCCH
28.6927087446
233PhosphorylationKLRTRTSSSETEEKK
EEEECCCCCCCCCHH
31.4220139300
234PhosphorylationLRTRTSSSETEEKKT
EEECCCCCCCCCHHC
48.5927087446
236PhosphorylationTRTSSSETEEKKTEK
ECCCCCCCCCHHCCC
51.9329514104
252PhosphorylationLILQPLGSRTQNVEV
EEEEECCCCCCCEEE
39.5825338131
254PhosphorylationLQPLGSRTQNVEVTK
EEECCCCCCCEEECC
26.6221454597
355PhosphorylationPAPKPDLSAAEKKAF
CCCCCCCCHHHHHHC
32.5827149854
380PhosphorylationSLLEQKPSKPAAPQV
HHHHCCCCCCCCCCC
59.3022067460
399PhosphorylationPTAPTKASNLLRSPG
CCCCCCHHHHCCCCC
29.5726239621
404PhosphorylationKASNLLRSPGAVYPK
CHHHHCCCCCCCCCC
27.8827087446
431PhosphorylationAKINGEVSIISSKID
CEECCEEEEEEEECC
15.2027841257
432UbiquitinationKINGEVSIISSKIDT
EECCEEEEEEEECCC
4.2327667366
439PhosphorylationIISSKIDTEPVSKPK
EEEEECCCCCCCCCC
45.7419854140
444UbiquitinationIDTEPVSKPKLDPEQ
CCCCCCCCCCCCHHH
46.5427667366
457UbiquitinationEQLPVRPKSVDLDAF
HHCCCCCCEECHHHH
53.1722790023
458PhosphorylationQLPVRPKSVDLDAFV
HCCCCCCEECHHHHH
24.4427087446
469PhosphorylationDAFVARNSKETDDVN
HHHHHCCCCCCCCCC
26.7330352176
482PhosphorylationVNFDDIASSENLLHL
CCHHHHHCCCCCHHH
38.2219367708
510PhosphorylationGRFNGGHSPTQSPEK
CCCCCCCCCCCCHHH
32.6825521595
512PhosphorylationFNGGHSPTQSPEKTL
CCCCCCCCCCHHHCC
44.7027087446
514PhosphorylationGGHSPTQSPEKTLKL
CCCCCCCCHHHCCCC
37.1925521595
527PhosphorylationKLPKEDDSGNLKPLE
CCCCCCCCCCCCCCE
41.7322067460
541PhosphorylationEFKKDASYSSKSSLS
EEECCCCCCCCCCCC
20.77-
545PhosphorylationDASYSSKSSLSTPSS
CCCCCCCCCCCCCCC
38.1630635358
546PhosphorylationASYSSKSSLSTPSSA
CCCCCCCCCCCCCCC
30.0330635358
548PhosphorylationYSSKSSLSTPSSASK
CCCCCCCCCCCCCCC
39.9722942356
549PhosphorylationSSKSSLSTPSSASKV
CCCCCCCCCCCCCCC
32.2722942356
551PhosphorylationKSSLSTPSSASKVNT
CCCCCCCCCCCCCCH
38.3322942356
552PhosphorylationSSLSTPSSASKVNTA
CCCCCCCCCCCCCHH
37.4522942356
554PhosphorylationLSTPSSASKVNTAAF
CCCCCCCCCCCHHHC
38.8030635358
558PhosphorylationSSASKVNTAAFLTPL
CCCCCCCHHHCCCHH
23.5023984901
563PhosphorylationVNTAAFLTPLELKAK
CCHHHCCCHHHHHHH
21.2626643407
568UbiquitinationFLTPLELKAKAEADD
CCCHHHHHHHHHCCC
38.1722790023
580PhosphorylationADDGKRNSVDELRAQ
CCCCCCCCHHHHHHH
34.6726824392
629UbiquitinationNLEVEIAKLKKAVLL
CHHHHHHHHHHHHHC
67.5122790023

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 CD2AP_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD2AP_MOUSE !!

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 CD2AP_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPN4_HUMANCLINT1physical
20360068
RGAP1_HUMANRACGAP1physical
20360068
SHCBP_HUMANSHCBP1physical
20360068
SH3K1_HUMANSH3KBP1physical
20360068
SYNJ2_HUMANSYNJ2physical
20360068
CLH1_HUMANCLTCphysical
20360068
ARAP1_HUMANARAP1physical
20360068
SH319_HUMANSH3D19physical
20360068
RTKN2_HUMANRTKN2physical
20360068
CD2AP_HUMANCD2APphysical
20360068
BACD3_HUMANKCTD10physical
20360068
KIF23_HUMANKIF23physical
20360068
CSKP_RATCaskphysical
15331416
NPHN_RATNphs1physical
15331416
VGFR1_MOUSEFlt1physical
15001553
CBL_MOUSECblphysical
15001553
PKD2_MOUSEPkd2physical
10913159
AP2A1_HUMANAP2A1physical
26496610
VATA_HUMANATP6V1Aphysical
26496610
VATB2_HUMANATP6V1B2physical
26496610
VPP1_HUMANATP6V0A1physical
26496610
CAZA1_HUMANCAPZA1physical
26496610
CAZA2_HUMANCAPZA2physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
CAV1_HUMANCAV1physical
26496610
CLCN7_HUMANCLCN7physical
26496610
CLCA_HUMANCLTAphysical
26496610
CLCB_HUMANCLTBphysical
26496610
CLH1_HUMANCLTCphysical
26496610
DAPK3_HUMANDAPK3physical
26496610
STOM_HUMANSTOMphysical
26496610
FLOT2_HUMANFLOT2physical
26496610
GELS_HUMANGSNphysical
26496610
ITPR3_HUMANITPR3physical
26496610
MYO1C_HUMANMYO1Cphysical
26496610
MYO6_HUMANMYO6physical
26496610
NDUS5_HUMANNDUFS5physical
26496610
CHM1A_HUMANCHMP1Aphysical
26496610
PEX10_HUMANPEX10physical
26496610
TRI27_HUMANTRIM27physical
26496610
RL6_HUMANRPL6physical
26496610
RM23_HUMANMRPL23physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
BACD2_HUMANTNFAIP1physical
26496610
TPD52_HUMANTPD52physical
26496610
TS101_HUMANTSG101physical
26496610
IFRD2_HUMANIFRD2physical
26496610
UBP7_HUMANUSP7physical
26496610
TOP3B_HUMANTOP3Bphysical
26496610
UBP8_HUMANUSP8physical
26496610
VA0D1_HUMANATP6V0D1physical
26496610
KIF23_HUMANKIF23physical
26496610
IST1_HUMANIST1physical
26496610
KEAP1_HUMANKEAP1physical
26496610
RNF10_HUMANRNF10physical
26496610
PDC6I_HUMANPDCD6IPphysical
26496610
FLOT1_HUMANFLOT1physical
26496610
TM9S1_HUMANTM9SF1physical
26496610
ERLN1_HUMANERLIN1physical
26496610
PRDX3_HUMANPRDX3physical
26496610
RB6I2_HUMANERC1physical
26496610
PHLB1_HUMANPHLDB1physical
26496610
DNMBP_HUMANDNMBPphysical
26496610
CHM2B_HUMANCHMP2Bphysical
26496610
ERC2_HUMANERC2physical
26496610
MYOF_HUMANMYOFphysical
26496610
CHM2A_HUMANCHMP2Aphysical
26496610
RGAP1_HUMANRACGAP1physical
26496610
SH3K1_HUMANSH3KBP1physical
26496610
CHMP5_HUMANCHMP5physical
26496610
VP37C_HUMANVPS37Cphysical
26496610
LRC59_HUMANLRRC59physical
26496610
MICA3_HUMANMICAL3physical
26496610
PHAR4_HUMANPHACTR4physical
26496610
SHCBP_HUMANSHCBP1physical
26496610
BACD3_HUMANKCTD10physical
26496610
PHLB2_HUMANPHLDB2physical
26496610
KLH13_HUMANKLHL13physical
26496610
TM263_HUMANTMEM263physical
26496610
MB12A_HUMANMVB12Aphysical
26496610
OSBL5_HUMANOSBPL5physical
26496610
ARAP1_HUMANARAP1physical
26496610
CHM4B_HUMANCHMP4Bphysical
26496610
MITD1_HUMANMITD1physical
26496610
RBM45_HUMANRBM45physical
26496610
SH319_HUMANSH3D19physical
26496610
PGAM5_HUMANPGAM5physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD2AP_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASSSPECTROMETRY.

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