LIN37_HUMAN - dbPTM
LIN37_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIN37_HUMAN
UniProt AC Q96GY3
Protein Name Protein lin-37 homolog
Gene Name LIN37
Organism Homo sapiens (Human).
Sequence Length 246
Subcellular Localization
Protein Description
Protein Sequence MFPVKVKVEKSELEMAKARNQLDAVLQCLLEKSHMDRERLDEEAGKTPSDTHNKDCSIAATGKRPSARFPHQRRKKRREMDDGLAEGGPQRSNTYVIKLFDRSVDLAQFSENTPLYPICRAWMRNSPSVRERECSPSSPLPPLPEDEEGSEVTNSKSRDVYKLPPPTPPGPPGDACRSRIPSPLQPEMQGTPDDEPSEPEPSPSTLIYRNMQRWKRIRQRWKEASHRNQLRYSESMKILREMYERQ
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
1Acetylation-------MFPVKVKV
-------CCCCEEEE		8.4822814378
5Sumoylation---MFPVKVKVEKSE
---CCCCEEEEEHHH		36.2528112733
5Acetylation---MFPVKVKVEKSE
---CCCCEEEEEHHH		36.2525953088
7Sumoylation-MFPVKVKVEKSELE
-CCCCEEEEEHHHHH		38.6728112733
17UbiquitinationKSELEMAKARNQLDA
HHHHHHHHHHHHHHH		46.7132015554
18UbiquitinationSELEMAKARNQLDAV
HHHHHHHHHHHHHHH		13.2032015554
28GlutathionylationQLDAVLQCLLEKSHM
HHHHHHHHHHHHHHH		4.0222555962
32UbiquitinationVLQCLLEKSHMDRER
HHHHHHHHHHHCHHH		45.7032015554
33PhosphorylationLQCLLEKSHMDRERL
HHHHHHHHHHCHHHH		18.0526074081
47PhosphorylationLDEEAGKTPSDTHNK
HHHHHCCCCCCCCCC		27.4025159151
49PhosphorylationEEAGKTPSDTHNKDC
HHHCCCCCCCCCCCC		61.4426074081
51PhosphorylationAGKTPSDTHNKDCSI
HCCCCCCCCCCCCCC		31.5226074081
63AcetylationCSIAATGKRPSARFP
CCCEECCCCCCCCCC		57.7025953088
94PhosphorylationGGPQRSNTYVIKLFD
CCCCCCCEEEEEECC		22.03-
98UbiquitinationRSNTYVIKLFDRSVD
CCCEEEEEECCCCCC		32.8122817900
123PhosphorylationYPICRAWMRNSPSVR
HHHHHHHHHCCCCCC		2.5833259812
124PhosphorylationPICRAWMRNSPSVRE
HHHHHHHHCCCCCCC		29.7632142685
135PhosphorylationSVRERECSPSSPLPP
CCCCCCCCCCCCCCC		24.0629255136
137PhosphorylationRERECSPSSPLPPLP
CCCCCCCCCCCCCCC		28.4429255136
138PhosphorylationERECSPSSPLPPLPE
CCCCCCCCCCCCCCC		33.5629255136
150PhosphorylationLPEDEEGSEVTNSKS
CCCCCCCCCCCCCCC		31.9723927012
153PhosphorylationDEEGSEVTNSKSRDV
CCCCCCCCCCCCCCC		29.7123927012
155PhosphorylationEGSEVTNSKSRDVYK
CCCCCCCCCCCCCCC		23.7323927012
157PhosphorylationSEVTNSKSRDVYKLP
CCCCCCCCCCCCCCC		33.27-
161PhosphorylationNSKSRDVYKLPPPTP
CCCCCCCCCCCCCCC		15.8826074081
167PhosphorylationVYKLPPPTPPGPPGD
CCCCCCCCCCCCCCH		48.1425159151
168PhosphorylationYKLPPPTPPGPPGDA
CCCCCCCCCCCCCHH		37.3132645325
178PhosphorylationPPGDACRSRIPSPLQ
CCCHHHHCCCCCCCC		34.1521955146
182PhosphorylationACRSRIPSPLQPEMQ
HHHCCCCCCCCHHHC		35.5525159151
191PhosphorylationLQPEMQGTPDDEPSE
CCHHHCCCCCCCCCC		13.4721955146
197PhosphorylationGTPDDEPSEPEPSPS
CCCCCCCCCCCCCCC		64.8325022875
202PhosphorylationEPSEPEPSPSTLIYR
CCCCCCCCCCHHHHH		29.8025159151
204PhosphorylationSEPEPSPSTLIYRNM
CCCCCCCCHHHHHHH		39.9425022875
205PhosphorylationEPEPSPSTLIYRNMQ
CCCCCCCHHHHHHHH		22.1321712546
208PhosphorylationPSPSTLIYRNMQRWK
CCCCHHHHHHHHHHH		10.0725022875
237AcetylationLRYSESMKILREMYE
HHHHHHHHHHHHHHH		48.1125953088
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 LIN37_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIN37_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 LIN37_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TEX11_HUMANTEX11physical
16189514
LIN9_HUMANLIN9physical
17531812
LIN52_HUMANLIN52physical
17531812
LIN54_HUMANLIN54physical
17531812
MYBB_HUMANMYBL2physical
17531812
E2F4_HUMANE2F4physical
17531812
RBL2_HUMANRBL2physical
17531812
TFDP1_HUMANTFDP1physical
17531812
TFDP2_HUMANTFDP2physical
17531812
RBBP4_HUMANRBBP4physical
17531812
MYBA_HUMANMYBL1physical
17531812
LIN9_HUMANLIN9physical
17671431
MYBB_HUMANMYBL2physical
17671431
RBL1_HUMANRBL1physical
17671431
LIN54_HUMANLIN54physical
17671431
RBBP4_HUMANRBBP4physical
17671431
HSP74_HUMANHSPA4physical
17671431
TBB3_HUMANTUBB3physical
17671431
RBL2_HUMANRBL2physical
17671431
E2F4_HUMANE2F4physical
17671431
TRI54_HUMANTRIM54physical
25416956
CEP70_HUMANCEP70physical
25416956
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
LIN54_HUMANLIN54physical
26186194
MYBB_HUMANMYBL2physical
26186194
MYBA_HUMANMYBL1physical
26186194
RBBP4_HUMANRBBP4physical
26186194
LIN9_HUMANLIN9physical
26186194
PYGB_HUMANPYGBphysical
26186194
LIN52_HUMANLIN52physical
26186194
LIN9_HUMANLIN9physical
28514442
MYBA_HUMANMYBL1physical
28514442
MYBB_HUMANMYBL2physical
28514442
LIN52_HUMANLIN52physical
28514442
LIN54_HUMANLIN54physical
28514442
SG1D2_HUMANSCGB1D2physical
28514442
RBBP4_HUMANRBBP4physical
28514442
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 LIN37_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-138; SER-182 ANDSER-202, AND MASS 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-178 AND THR-205, 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-138; SER-182 ANDSER-202, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167; SER-182 ANDSER-202, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.

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