TIAM1_HUMAN - dbPTM
TIAM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIAM1_HUMAN
UniProt AC Q13009
Protein Name T-lymphoma invasion and metastasis-inducing protein 1
Gene Name TIAM1
Organism Homo sapiens (Human).
Sequence Length 1591
Subcellular Localization Cell junction. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Detected at the boundary between cells with actin-rich protrusions (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction..
Protein Description Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates RAC1, CDC42, and to a lesser extent RHOA. Required for normal cell adhesion and cell migration..
Protein Sequence MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDSTGPQLATMRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPKQQHSSTLESYLIKPIQRILKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTTVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEDWDPFRFRHMIPTEALQVRALASADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKAVHSILRDKHRRQLLKTESLPSSQQYVPFGGKRLCALKGARPAMSRAVSAPSKSLGRRRRRLARNRFTIDSDAVSASSPEKESQQPPGGGDTDRWVEEQFDLAQYEEQDDIKETDILSDDDEFCESVKGASVDRDLQERLQATSISQRERGRKTLDSHASRMAQLKKQAALSGINGGLESASEEVIWVRREDFAPSRKLNTEI
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
2N-myristoyl glycine------MGNAESQHV
------CCCCCHHCC
54.05-
2Myristoylation------MGNAESQHV
------CCCCCHHCC
54.05-
20PhosphorylationFYGEKHASLGRKHTS
CCCHHHHHCCCCCCH
30.9524719451
26PhosphorylationASLGRKHTSRSLRLS
HHCCCCCCHHHHHHC
28.95-
29PhosphorylationGRKHTSRSLRLSHKT
CCCCCHHHHHHCCCC
20.0123898821
33PhosphorylationTSRSLRLSHKTRRTR
CHHHHHHCCCCCCCC
19.2623898821
43PhosphorylationTRRTRHASSGKVIHR
CCCCCCCCCCCEEEC
33.2324719451
52PhosphorylationGKVIHRNSEVSTRSS
CCEEECCCCCCCCCC
39.0527251275
55PhosphorylationIHRNSEVSTRSSSTP
EECCCCCCCCCCCCC
17.6629449344
56PhosphorylationHRNSEVSTRSSSTPS
ECCCCCCCCCCCCCC
39.4829449344
58PhosphorylationNSEVSTRSSSTPSIP
CCCCCCCCCCCCCCC
28.8228348404
59PhosphorylationSEVSTRSSSTPSIPQ
CCCCCCCCCCCCCCH
34.6328348404
60PhosphorylationEVSTRSSSTPSIPQS
CCCCCCCCCCCCCHH
45.6527251275
61PhosphorylationVSTRSSSTPSIPQSL
CCCCCCCCCCCCHHH
24.0128348404
63PhosphorylationTRSSSTPSIPQSLAE
CCCCCCCCCCHHHHH
47.1728348404
102PhosphorylationDMGLRPVSYTDSSVT
ECCCEECCCCCCCCC
25.6228348404
104PhosphorylationGLRPVSYTDSSVTPS
CCEECCCCCCCCCCC
23.1528348404
106PhosphorylationRPVSYTDSSVTPSVD
EECCCCCCCCCCCCC
20.9328348404
107PhosphorylationPVSYTDSSVTPSVDS
ECCCCCCCCCCCCCC
32.5928348404
135PhosphorylationDTEESRLYGDDATYL
CCCHHHHHCCCCCCE
19.8729978859
140PhosphorylationRLYGDDATYLAEGGR
HHHCCCCCCEECCCC
26.5129978859
141PhosphorylationLYGDDATYLAEGGRR
HHCCCCCCEECCCCC
12.9729978859
152PhosphorylationGGRRQHSYTSNGPTF
CCCCCCCCCCCCCCH
16.44-
158PhosphorylationSYTSNGPTFMETASF
CCCCCCCCHHHHHCC
36.6928348404
162PhosphorylationNGPTFMETASFKKKR
CCCCHHHHHCCCCCC
18.8028348404
164PhosphorylationPTFMETASFKKKRSK
CCHHHHHCCCCCCCC
45.0524719451
170PhosphorylationASFKKKRSKSADIWR
HCCCCCCCCCCCCCC
39.5827732954
172PhosphorylationFKKKRSKSADIWRED
CCCCCCCCCCCCCCC
32.2128188228
216PhosphorylationEEARGMETRASPRQL
HHHCCCCCCCCHHHH
23.7329083192
219PhosphorylationRGMETRASPRQLSTC
CCCCCCCCHHHHHHH
19.8228348404
224PhosphorylationRASPRQLSTCQRANS
CCCHHHHHHHHHHHH
20.8523312004
225PhosphorylationASPRQLSTCQRANSL
CCHHHHHHHHHHHHH
22.6523312004
231PhosphorylationSTCQRANSLGDLYAQ
HHHHHHHHHHHHHHH
32.5119664994
236PhosphorylationANSLGDLYAQKNSGV
HHHHHHHHHHHCCCC
16.2430266825
241PhosphorylationDLYAQKNSGVTANGG
HHHHHHCCCCCCCCC
41.4928111955
244PhosphorylationAQKNSGVTANGGPGS
HHHCCCCCCCCCCCH
20.2428111955
251PhosphorylationTANGGPGSKFAGYCR
CCCCCCCHHHHHHHH
27.9428111955
283PhosphorylationAAEETPPYSNYNTLP
HCCCCCCCCCCCCCC
15.6827642862
286PhosphorylationETPPYSNYNTLPCRK
CCCCCCCCCCCCCCH
12.0027642862
288PhosphorylationPPYSNYNTLPCRKSH
CCCCCCCCCCCCHHH
23.0127050516
294PhosphorylationNTLPCRKSHCLSEGA
CCCCCCHHHHCCCCC
10.4829978859
298PhosphorylationCRKSHCLSEGATNPQ
CCHHHHCCCCCCCCC
39.1029978859
302PhosphorylationHCLSEGATNPQISHS
HHCCCCCCCCCCCCC
59.2829978859
307PhosphorylationGATNPQISHSNSMQG
CCCCCCCCCCCCCCC
18.6729507054
309PhosphorylationTNPQISHSNSMQGRR
CCCCCCCCCCCCCCC
24.6529978859
311PhosphorylationPQISHSNSMQGRRAK
CCCCCCCCCCCCCCC
18.5929978859
319PhosphorylationMQGRRAKTTQDVNAG
CCCCCCCCCCCCCCC
28.8027273156
320PhosphorylationQGRRAKTTQDVNAGE
CCCCCCCCCCCCCCC
23.2825850435
329PhosphorylationDVNAGEGSEFADSGI
CCCCCCCCCCCCCCC
25.8230624053
334PhosphorylationEGSEFADSGIEGATT
CCCCCCCCCCCCCCC
37.9430624053
340PhosphorylationDSGIEGATTDTDLLS
CCCCCCCCCCHHHHH
35.74-
350PhosphorylationTDLLSRRSNATNSSY
HHHHHHHCCCCCCCC
29.7023312004
353PhosphorylationLSRRSNATNSSYSPT
HHHHCCCCCCCCCCC
39.6223312004
355PhosphorylationRRSNATNSSYSPTTG
HHCCCCCCCCCCCCC
26.7128450419
356PhosphorylationRSNATNSSYSPTTGR
HCCCCCCCCCCCCCC
31.5322617229
357PhosphorylationSNATNSSYSPTTGRA
CCCCCCCCCCCCCCC
20.6320363803
358PhosphorylationNATNSSYSPTTGRAF
CCCCCCCCCCCCCCE
20.0919664994
360PhosphorylationTNSSYSPTTGRAFVG
CCCCCCCCCCCCEEC
35.6228450419
361PhosphorylationNSSYSPTTGRAFVGS
CCCCCCCCCCCEECC
28.2328450419
368PhosphorylationTGRAFVGSDSGSSST
CCCCEECCCCCCCCH
24.2527732954
370PhosphorylationRAFVGSDSGSSSTGD
CCEECCCCCCCCHHH
42.1227732954
372PhosphorylationFVGSDSGSSSTGDAA
EECCCCCCCCHHHHH
25.6827732954
373PhosphorylationVGSDSGSSSTGDAAR
ECCCCCCCCHHHHHH
35.1327732954
374PhosphorylationGSDSGSSSTGDAARQ
CCCCCCCCHHHHHHH
37.8027732954
375PhosphorylationSDSGSSSTGDAARQG
CCCCCCCHHHHHHHH
40.8227732954
384PhosphorylationDAARQGVYENFRREL
HHHHHHHHHHHHHHH
16.3925884760
456PhosphorylationKKNKKVESATRRKWK
ECCCCCCHHHHHCCC
37.62-
458PhosphorylationNKKVESATRRKWKHY
CCCCCHHHHHCCCEE
40.04-
483PhosphorylationFYESDGRSGIDHNSI
EEECCCCCCCCCCCC
45.7026270265
489PhosphorylationRSGIDHNSIPKHAVW
CCCCCCCCCCCCEEE
36.5326270265
592PhosphorylationEMQLSSVTDSKKKKT
CCCHHCCCCCHHHHH
36.1830576142
594PhosphorylationQLSSVTDSKKKKTIL
CHHCCCCCHHHHHHH
36.6930576142
596AcetylationSSVTDSKKKKTILDQ
HCCCCCHHHHHHHHH
64.557679253
599PhosphorylationTDSKKKKTILDQIFV
CCCHHHHHHHHHHHH
35.33-
679PhosphorylationETGVRRRTQAMSRSA
CCHHHHHHHHHHHHH
20.9022210691
687PhosphorylationQAMSRSASKRRSRFS
HHHHHHHHHHHHHHH
28.1322210691
694PhosphorylationSKRRSRFSSLWGLDT
HHHHHHHHHHHCCCC
24.3430576142
695PhosphorylationKRRSRFSSLWGLDTT
HHHHHHHHHHCCCCC
25.9828348404
701PhosphorylationSSLWGLDTTSKKKQG
HHHHCCCCCCCCCCC
37.7030576142
702PhosphorylationSLWGLDTTSKKKQGR
HHHCCCCCCCCCCCC
37.9129083192
703PhosphorylationLWGLDTTSKKKQGRP
HHCCCCCCCCCCCCC
44.5729083192
726PhosphorylationGTEAVKKSLEGIFDD
CHHHHHHHHCHHHCC
26.4029507054
820PhosphorylationIENKMQLYVPQPEED
HHCCCEEECCCCHHH
8.00-
829PhosphorylationPQPEEDIYELLYKEI
CCCHHHHHHHHHHHH
16.91-
887MethylationETGLASKKGLKAGDE
HHCCCCCCCCCCCHH
67.96-
989PhosphorylationEGPDLESSDETDHSS
CCCCCCCCCCCCCCC
30.05-
992PhosphorylationDLESSDETDHSSKST
CCCCCCCCCCCCCCH
43.96-
998PhosphorylationETDHSSKSTEQVAAF
CCCCCCCCHHHHHHH
38.84-
1008PhosphorylationQVAAFCRSLHEMNPS
HHHHHHHHHHHCCCC
34.9527732954
1015PhosphorylationSLHEMNPSDQSPSPQ
HHHHCCCCCCCCCCC
43.1929978859
1018PhosphorylationEMNPSDQSPSPQDST
HCCCCCCCCCCCCCC
32.1322199227
1020PhosphorylationNPSDQSPSPQDSTGP
CCCCCCCCCCCCCCH
40.2022199227
1024PhosphorylationQSPSPQDSTGPQLAT
CCCCCCCCCCHHHHH
29.9827732954
1025PhosphorylationSPSPQDSTGPQLATM
CCCCCCCCCHHHHHH
62.2627732954
1031PhosphorylationSTGPQLATMRQLSDA
CCCHHHHHHHHHCCH
22.8328122231
1036PhosphorylationLATMRQLSDADKLRK
HHHHHHHCCHHHHHH
23.5529496963
1040AcetylationRQLSDADKLRKVICE
HHHCCHHHHHHHHHH
52.4925953088
1142PhosphorylationYADRFKLYSAFCASH
HHHHHHHHHHHHHHC
9.8820166139
1143PhosphorylationADRFKLYSAFCASHT
HHHHHHHHHHHHHCC
25.8820166139
1317PhosphorylationQKKKLVGSHRLSIYE
HHEEEECCEEEECCC
9.65-
1321PhosphorylationLVGSHRLSIYEDWDP
EECCEEEECCCCCCC
24.0729978859
1323PhosphorylationGSHRLSIYEDWDPFR
CCEEEECCCCCCCHH
12.4025884760
1337PhosphorylationRFRHMIPTEALQVRA
HCCCCCCCHHHHHHH
23.98-
1397TrimethylationVHSILRDKHRRQLLK
HHHHHCHHHHHHHHH
32.36-
1397MethylationVHSILRDKHRRQLLK
HHHHHCHHHHHHHHH
32.36-
1405PhosphorylationHRRQLLKTESLPSSQ
HHHHHHHCCCCCCCC
30.6729978859
1407PhosphorylationRQLLKTESLPSSQQY
HHHHHCCCCCCCCCC
51.3023401153
1410PhosphorylationLKTESLPSSQQYVPF
HHCCCCCCCCCCCCC
46.1829978859
1411PhosphorylationKTESLPSSQQYVPFG
HCCCCCCCCCCCCCC
21.2623684312
1414PhosphorylationSLPSSQQYVPFGGKR
CCCCCCCCCCCCCEE
11.4921406692
1420AcetylationQYVPFGGKRLCALKG
CCCCCCCEEHHHHCC
42.4424468117
1433PhosphorylationKGARPAMSRAVSAPS
CCCHHHHHHHHCCCC
21.1329449344
1437PhosphorylationPAMSRAVSAPSKSLG
HHHHHHHCCCCCHHH
33.2126657352
1440PhosphorylationSRAVSAPSKSLGRRR
HHHHCCCCCHHHHHH
34.2929449344
1442PhosphorylationAVSAPSKSLGRRRRR
HHCCCCCHHHHHHHH
40.1524719451
1456PhosphorylationRLARNRFTIDSDAVS
HHHHCCEECCCCCCC
22.1923401153
1459PhosphorylationRNRFTIDSDAVSASS
HCCEECCCCCCCCCC
24.5023401153
1463PhosphorylationTIDSDAVSASSPEKE
ECCCCCCCCCCCCCH
24.9330266825
1465PhosphorylationDSDAVSASSPEKESQ
CCCCCCCCCCCCHHC
38.6325849741
1466PhosphorylationSDAVSASSPEKESQQ
CCCCCCCCCCCHHCC
36.4719664994
1471PhosphorylationASSPEKESQQPPGGG
CCCCCCHHCCCCCCC
45.2230624053
1502PhosphorylationEQDDIKETDILSDDD
CCCCCCCCCCCCCCH
24.2829514088
1506PhosphorylationIKETDILSDDDEFCE
CCCCCCCCCCHHHHH
39.0519664994
1519PhosphorylationCESVKGASVDRDLQE
HHHCCCCCCCHHHHH
32.9723401153
1531PhosphorylationLQERLQATSISQRER
HHHHHHHHCHHHHHH
17.4023312004
1532PhosphorylationQERLQATSISQRERG
HHHHHHHCHHHHHHH
24.2123312004
1534PhosphorylationRLQATSISQRERGRK
HHHHHCHHHHHHHHH
23.9729978859
1542PhosphorylationQRERGRKTLDSHASR
HHHHHHHHHHHHHHH
34.1417322306
1560PhosphorylationLKKQAALSGINGGLE
HHHHHHHCCCCCCCC
32.66-

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
231SPhosphorylationKinaseAKT1P31749
PSP
329SPhosphorylationKinaseCK1AP48729
PSP
384YPhosphorylationKinaseSRCP12931
GPS
829YPhosphorylationKinaseNTRK2Q16620
Uniprot
1466SPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:25124033

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIAM1_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 TIAM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEB2_HUMANPPP1R9Bphysical
12531897
JIP2_HUMANMAPK8IP2physical
12024021
JIP1_HUMANMAPK8IP1physical
12024021
RAC1_HUMANRAC1physical
11130063
RAC1_HUMANRAC1physical
11595749
ANK1_HUMANANK1physical
10893266
ANK3_HUMANANK3physical
10893266
FBW1A_HUMANBTRCphysical
25124033
KC1A_HUMANCSNK1A1physical
25124033
KC1E_HUMANCSNK1Ephysical
25124033
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
CING_HUMANCGNphysical
27173435
MAST3_HUMANMAST3physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NF1_HUMANNF1physical
27173435
F110B_HUMANFAM110Bphysical
27173435
UBP21_HUMANUSP21physical
27173435
CBY1_HUMANCBY1physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
FA53C_HUMANFAM53Cphysical
27173435
NADK_HUMANNADKphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
NGAP_HUMANRASAL2physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435

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 TIAM1_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-231, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
"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-356 AND SER-358, ANDMASS SPECTROMETRY.

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