TM1L1_HUMAN - dbPTM
TM1L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM1L1_HUMAN
UniProt AC O75674
Protein Name TOM1-like protein 1
Gene Name TOM1L1
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization Golgi apparatus, Golgi stack. Endosome membrane . Cytoplasm. Membrane
Peripheral membrane protein
Cytoplasmic side. A small proportion is membrane-associated..
Protein Description Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity)..
Protein Sequence MAFGKSHRDPYATSVGHLIEKATFAGVQTEDWGQFMHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLTLSLIDMCVQNCGPSFQSLIVKKEFVKENLVKLLNPRYNLPLDIQNRILNFIKTWSQGFPGGVDVSEVKEVYLDLVKKGVQFPPSEAEAETARQETAQISSNPPTSVPTAPALSSVIAPKNSTVTLVPEQIGKLHSELDMVKMNVRVMSAILMENTPGSENHEDIELLQKLYKTGREMQERIMDLLVVVENEDVTVELIQVNEDLNNAILGYERFTRNQQRILEQNKNQKEATNTTSEPSAPSQDLLDLSPSPRMPRATLGELNTMNNQLSGLNFSLPSSDVTNNLKPSLHPQMNLLALENTEIPPFAQRTSQNLTSSHAYDNFLEHSNSVFLQPVSLQTIAAAPSNQSLPPLPSNHPAMTKSDLQPPNYYEVMEFDPLAPAVTTEAIYEEIDAHQHKGAQNDGD
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---MAFGKSHRDPYA
---CCCCCCCCCCCH		36.3121906983
5Ubiquitination---MAFGKSHRDPYA
---CCCCCCCCCCCH		36.3121890473
5Ubiquitination---MAFGKSHRDPYA
---CCCCCCCCCCCH		36.3121890473
6Phosphorylation--MAFGKSHRDPYAT
--CCCCCCCCCCCHH		24.9220068231
11PhosphorylationGKSHRDPYATSVGHL
CCCCCCCCHHHHHHH		27.1427259358
13PhosphorylationSHRDPYATSVGHLIE
CCCCCCHHHHHHHHH		20.3627251275
14PhosphorylationHRDPYATSVGHLIEK
CCCCCHHHHHHHHHH		20.2329449344
93AcetylationSFQSLIVKKEFVKEN
CHHHHHHCHHHHHHH		39.3219666895
98UbiquitinationIVKKEFVKENLVKLL
HHCHHHHHHHHHHHH		46.32-
103UbiquitinationFVKENLVKLLNPRYN
HHHHHHHHHHCCCCC		50.8821890473
103UbiquitinationFVKENLVKLLNPRYN
HHHHHHHHHHCCCCC		50.8821890473
103UbiquitinationFVKENLVKLLNPRYN
HHHHHHHHHHCCCCC		50.8821906983
109PhosphorylationVKLLNPRYNLPLDIQ
HHHHCCCCCCCHHHH		23.4728152594
114UbiquitinationPRYNLPLDIQNRILN
CCCCCCHHHHHHHHH		38.19-
148UbiquitinationEVYLDLVKKGVQFPP
HHHHHHHHCCCCCCC		51.6221890473
1482-HydroxyisobutyrylationEVYLDLVKKGVQFPP
HHHHHHHHCCCCCCC		51.62-
148UbiquitinationEVYLDLVKKGVQFPP
HHHHHHHHCCCCCCC		51.6221890473
148UbiquitinationEVYLDLVKKGVQFPP
HHHHHHHHCCCCCCC		51.6221906983
149UbiquitinationVYLDLVKKGVQFPPS
HHHHHHHCCCCCCCH		57.76-
156PhosphorylationKGVQFPPSEAEAETA
CCCCCCCHHHHHHHH		50.0728188228
162PhosphorylationPSEAEAETARQETAQ
CHHHHHHHHHHHHHH		33.9028188228
171PhosphorylationRQETAQISSNPPTSV
HHHHHHHCCCCCCCC		16.39-
191UbiquitinationLSSVIAPKNSTVTLV
CCCCCCCCCCEEEEC		55.2821906983
193PhosphorylationSVIAPKNSTVTLVPE
CCCCCCCCEEEECHH		30.3127251275
194PhosphorylationVIAPKNSTVTLVPEQ
CCCCCCCEEEECHHH		27.2327251275
207PhosphorylationEQIGKLHSELDMVKM
HHHCHHHHHHHHHHH		50.7427251275
220PhosphorylationKMNVRVMSAILMENT
HHHHHHHHHHHHCCC		14.8628122231
241UbiquitinationEDIELLQKLYKTGRE
HHHHHHHHHHHHCHH		54.47-
298MethylationQRILEQNKNQKEATN
HHHHHHCCCHHHHCC		61.5223644510
298UbiquitinationQRILEQNKNQKEATN
HHHHHHCCCHHHHCC		61.5221906983
298"N6,N6-dimethyllysine"QRILEQNKNQKEATN
HHHHHHCCCHHHHCC		61.52-
301UbiquitinationLEQNKNQKEATNTTS
HHHCCCHHHHCCCCC		59.7221906983
304PhosphorylationNKNQKEATNTTSEPS
CCCHHHHCCCCCCCC		33.9023403867
306PhosphorylationNQKEATNTTSEPSAP
CHHHHCCCCCCCCCC		27.6123403867
307PhosphorylationQKEATNTTSEPSAPS
HHHHCCCCCCCCCCC		32.9123403867
308PhosphorylationKEATNTTSEPSAPSQ
HHHCCCCCCCCCCCC		45.5323403867
311PhosphorylationTNTTSEPSAPSQDLL
CCCCCCCCCCCCCCC		49.0823927012
314PhosphorylationTSEPSAPSQDLLDLS
CCCCCCCCCCCCCCC		35.7217525332
321PhosphorylationSQDLLDLSPSPRMPR
CCCCCCCCCCCCCCC		24.0129255136
323PhosphorylationDLLDLSPSPRMPRAT
CCCCCCCCCCCCCCC		23.0529255136
330PhosphorylationSPRMPRATLGELNTM
CCCCCCCCHHHHHHH		36.2526074081
342PhosphorylationNTMNNQLSGLNFSLP
HHHHHCCCCCCCCCC		31.32-
392PhosphorylationNLTSSHAYDNFLEHS
CCCCCHHHHHHHHHC		13.1419798056
441PhosphorylationSDLQPPNYYEVMEFD
HHCCCCCEEEEEECC		13.5326356563
442PhosphorylationDLQPPNYYEVMEFDP
HCCCCCEEEEEECCC		14.5326356563
455PhosphorylationDPLAPAVTTEAIYEE
CCCCCCCCHHHHHHH		22.4826356563
456PhosphorylationPLAPAVTTEAIYEEI
CCCCCCCHHHHHHHH		19.4726356563
460PhosphorylationAVTTEAIYEEIDAHQ
CCCHHHHHHHHHHHH		17.9819798056
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 TM1L1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM1L1_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 TM1L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TS101_HUMANTSG101physical
15611048
HGS_HUMANHGSphysical
15611048
TOLIP_HUMANTOLLIPphysical
16412388
CLH1_HUMANCLTCphysical
16412388
FYN_HUMANFYNphysical
20182632
EGFR_HUMANEGFRphysical
19798056
CLH1_HUMANCLTCphysical
19798056
CLH1_HUMANCLTCphysical
17785434
SRC_HUMANSRCphysical
17785434
UBC_BOVINUBCphysical
20150893
SYAC_HUMANAARSphysical
22863883
ARC1B_HUMANARPC1Bphysical
22863883
ARPC2_HUMANARPC2physical
22863883
ARPC5_HUMANARPC5physical
22863883
NIF3L_HUMANNIF3L1physical
22863883
OGT1_HUMANOGTphysical
22863883
RPR1B_HUMANRPRD1Bphysical
22863883
TOLIP_HUMANTOLLIPphysical
15047686
TOLIP_HUMANTOLLIPphysical
26899482
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 TM1L1_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-321 AND SER-323, ANDMASS SPECTROMETRY.
"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-323, AND MASSSPECTROMETRY.
"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-323, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-323, ANDMASS SPECTROMETRY.

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