CIP4_HUMAN - dbPTM
CIP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CIP4_HUMAN
UniProt AC Q15642
Protein Name Cdc42-interacting protein 4
Gene Name TRIP10
Organism Homo sapiens (Human).
Sequence Length 601
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection, phagocytic cup. Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity). Loca
Protein Description Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL..
Protein Sequence MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN
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
27MethylationWGLDLLDRYVKFVKE
HHHHHHHHHHHHHHH		37.81115918969
44AcetylationEVEQAYAKQLRSLVK
HHHHHHHHHHHHHHH		36.8723236377
44MalonylationEVEQAYAKQLRSLVK
HHHHHHHHHHHHHHH		36.8726320211
44UbiquitinationEVEQAYAKQLRSLVK
HHHHHHHHHHHHHHH		36.87-
44 (in isoform 5)Ubiquitination-36.8721906983
44 (in isoform 1)Ubiquitination-36.8721906983
44 (in isoform 2)Ubiquitination-36.8721906983
44 (in isoform 4)Ubiquitination-36.8721906983
44 (in isoform 3)Ubiquitination-36.8721906983
66UbiquitinationAKDDPESKFSQQQSF
CCCCCCCCHHHHHHH		47.58-
104AcetylationRVCLELTKYSQEMKQ
HHHHHHHHHHHHHHH		56.3712436413
132AcetylationQQLENGFKQLENSKR
HHHHHHHHHHHHHHH		56.2019823653
132UbiquitinationQQLENGFKQLENSKR
HHHHHHHHHHHHHHH		56.20-
154PhosphorylationEAEKAAQTAERLDQD
HHHHHHHHHHHHHHH		26.2623403867
166 (in isoform 3)Ubiquitination-39.9321906983
166UbiquitinationDQDINATKADVEKAK
HHHHHHHHHHHHHHH		39.9321906983
166 (in isoform 2)Ubiquitination-39.9321906983
166 (in isoform 4)Ubiquitination-39.9321906983
166 (in isoform 5)Ubiquitination-39.9321906983
166 (in isoform 1)Ubiquitination-39.9321906983
187 (in isoform 4)Ubiquitination-58.0121906983
187 (in isoform 5)Ubiquitination-58.0121906983
187UbiquitinationSHMAEESKNEYAAQL
HHHHHHHHHHHHHHH		58.0121906983
187 (in isoform 3)Ubiquitination-58.0121906983
187 (in isoform 1)Ubiquitination-58.0121906983
187 (in isoform 2)Ubiquitination-58.0121906983
190PhosphorylationAEESKNEYAAQLQRF
HHHHHHHHHHHHHHH		19.3429978859
205PhosphorylationNRDQAHFYFSQMPQI
CHHHHHHHHCCCHHH		7.7729978859
207PhosphorylationDQAHFYFSQMPQIFD
HHHHHHHCCCHHHHH		17.7529978859
215 (in isoform 4)Ubiquitination-36.9821906983
215 (in isoform 1)Ubiquitination-36.9821906983
215UbiquitinationQMPQIFDKLQDMDER
CCHHHHHHHHHHHHH		36.982190698
215 (in isoform 2)Ubiquitination-36.9821906983
215 (in isoform 3)Ubiquitination-36.9821906983
215 (in isoform 5)Ubiquitination-36.9821906983
225PhosphorylationDMDERRATRLGAGYG
HHHHHHHHHHHCCCC		25.31-
235PhosphorylationGAGYGLLSEAELEVV
HCCCCCCCHHHHHHH		39.54-
265PhosphorylationAVDPKNDSHVLIELH
CCCCCCCCCEEEEEH		25.5328555341
288PhosphorylationDVEFEDFSQPMNRAP
CCCCCCCCCCCCCCC		45.7727251275
296PhosphorylationQPMNRAPSDSSLGTP
CCCCCCCCCCCCCCC		49.4919664994
298PhosphorylationMNRAPSDSSLGTPSD
CCCCCCCCCCCCCCC		31.6229255136
299PhosphorylationNRAPSDSSLGTPSDG
CCCCCCCCCCCCCCC		35.4929255136
302PhosphorylationPSDSSLGTPSDGRPE
CCCCCCCCCCCCCCC		25.5523927012
304PhosphorylationDSSLGTPSDGRPELR
CCCCCCCCCCCCCCC		53.1623927012
335PhosphorylationKPRPPPLSPLGGPVP
CCCCCCCCCCCCCCC		24.6925159151
343PhosphorylationPLGGPVPSALPNGPP
CCCCCCCCCCCCCCC		42.5528152594
351PhosphorylationALPNGPPSPRSGRDP
CCCCCCCCCCCCCCH		35.7623927012
354PhosphorylationNGPPSPRSGRDPLAI
CCCCCCCCCCCHHHH		41.3827050516
363PhosphorylationRDPLAILSEISKSVK
CCHHHHHHHHHHHCC		27.1122496350
366PhosphorylationLAILSEISKSVKPRL
HHHHHHHHHHCCHHH		18.1521406692
368PhosphorylationILSEISKSVKPRLAS
HHHHHHHHCCHHHHH		28.6921406692
375PhosphorylationSVKPRLASFRSLRGS
HCCHHHHHHHHHCCC		26.2824719451
378PhosphorylationPRLASFRSLRGSRGT
HHHHHHHHHCCCCCE		22.0222617229
437SulfoxidationVYEKTPQMGDPASLE
HHHHCCCCCCHHHCC		7.4730846556
442PhosphorylationPQMGDPASLEPQIAE
CCCCCHHHCCHHHHH		38.3627251275
458UbiquitinationLSNIERLKLEVQKYE
HHHHHHHHHHHHHHH		49.15-
464PhosphorylationLKLEVQKYEAWLAEA
HHHHHHHHHHHHHHH		8.1927642862
477PhosphorylationEAESRVLSNRGDSLS
HHHHHHHHCCCCCHH		22.9425159151
482PhosphorylationVLSNRGDSLSRHARP
HHHCCCCCHHHCCCC		30.9423927012
484PhosphorylationSNRGDSLSRHARPPD
HCCCCCHHHCCCCCC		26.4423927012
495PhosphorylationRPPDPPASAPPDSSS
CCCCCCCCCCCCCCC		47.2728985074
500PhosphorylationPASAPPDSSSNSASQ
CCCCCCCCCCCCCCC		41.2523663014
501PhosphorylationASAPPDSSSNSASQD
CCCCCCCCCCCCCCC		40.7023663014
502PhosphorylationSAPPDSSSNSASQDT
CCCCCCCCCCCCCCC		38.4623663014
504PhosphorylationPPDSSSNSASQDTKE
CCCCCCCCCCCCCCC		31.1123663014
506PhosphorylationDSSSNSASQDTKESS
CCCCCCCCCCCCCCC		28.5425159151
509PhosphorylationSNSASQDTKESSEEP
CCCCCCCCCCCCCCC		29.1323663014
527PhosphorylationESQDTPIYTEFDEDF
CCCCCCCCCCCCCCC		11.0412456510
539PhosphorylationEDFEEEPTSPIGHCV
CCCCCCCCCCCCEEE		50.8726657352
540PhosphorylationDFEEEPTSPIGHCVA
CCCCCCCCCCCEEEE		25.8226657352
544 (in isoform 3)Phosphorylation-12.00-
579PhosphorylationEDKGDGWTRVRRKEG
CCCCCCCEEEEECCC		25.47-
590PhosphorylationRKEGGEGYVPTSYLR
ECCCCCCCCCCCCEE		10.0427642862
595PhosphorylationEGYVPTSYLRVTLN-
CCCCCCCCEEEEEC-		10.8727642862
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
471YPhosphorylationKinaseSRCP12931
PSP
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CIP4_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 CIP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC42_HUMANCDC42physical
9210375
HD_HUMANHTTphysical
12604778
WASP_HUMANWASphysical
10713100
WBP11_HUMANWBP11physical
16189514
STAT3_HUMANSTAT3physical
15163742
AKAP9_HUMANAKAP9physical
15047863
RHG17_HUMANARHGAP17physical
11431473
CDC42_HUMANCDC42physical
10713100
ASAP1_HUMANASAP1physical
19041431
DYN2_HUMANDNM2physical
19041431
SHIP1_HUMANINPP5Dphysical
19041431
SBK1_HUMANSBK1physical
19041431
DYN2_HUMANDNM2physical
16418535
WASL_HUMANWASLphysical
16418535
INT9_HUMANINTS9physical
22863883
OSB11_HUMANOSBPL11physical
22863883
DPOD1_HUMANPOLD1physical
22863883
TBD2A_HUMANTBC1D2physical
22863883
WDR44_HUMANWDR44physical
22863883
CIP4_HUMANTRIP10physical
25416956
RHG44_HUMANARHGAP44physical
25416956
3BP1_HUMANSH3BP1physical
25416956
RHG17_HUMANARHGAP17physical
25416956
RHOJ_HUMANRHOJphysical
25416956
RHG12_HUMANARHGAP12physical
25416956
COPA_HUMANCOPAphysical
26344197
COPB2_HUMANCOPB2physical
26344197
COPE_HUMANCOPEphysical
26344197
HNRPU_HUMANHNRNPUphysical
26344197
SF3A1_HUMANSF3A1physical
26344197
RENT2_HUMANUPF2physical
26344197
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 CIP4_HUMAN

loading...

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-296 AND SER-299, ANDMASS SPECTROMETRY.
"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-296; SER-299; SER-335AND SER-351, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-299, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-299, ANDMASS SPECTROMETRY.
"Felic (CIP4b), a novel binding partner with the Src kinase Lyn andCdc42, localizes to the phagocytic cup.";
Dombrosky-Ferlan P., Grishin A., Botelho R.J., Sampson M., Wang L.,Rudert W.A., Grinstein S., Corey S.J.;
Blood 101:2804-2809(2003).
Cited for: INTERACTION WITH CDC42; LYN AND SRC, SUBCELLULAR LOCATION, TISSUESPECIFICITY, AND PHOSPHORYLATION AT TYROSINE RESIDUES.
"Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell-cell adhesion: expression and function in renalcell carcinoma.";
Tsuji E., Tsuji Y., Fujiwara T., Ogata S., Tsukamoto K., Saku K.;
Biochem. Biophys. Res. Commun. 339:1083-1088(2006).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH CTNNB1,SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYROSINE RESIDUES.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory
Application loaded.