TMM51_HUMAN - dbPTM
TMM51_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMM51_HUMAN
UniProt AC Q9NW97
Protein Name Transmembrane protein 51
Gene Name TMEM51
Organism Homo sapiens (Human).
Sequence Length 253
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MMAQSKANGSHYALTAIGLGMLVLGVIMAMWNLVPGFSAAEKPTAQGSNKTEVGGGILKSKTFSVAYVLVGAGVMLLLLSICLSIRDKRKQRQGEDLAHVQHPTGAGPHAQEEDSQEEEEEDEEAASRYYVPSYEEVMNTNYSEARGEEQNPRLSISLPSYESLTGLDETTPTSTRADVEASPGNPPDRQNSKLAKRLKPLKVRRIKSEKLHLKDFRINLPDKNVPPPSIEPLTPPPQYDEVQEKAPDTRPPD
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
48PhosphorylationEKPTAQGSNKTEVGG
HCCCCCCCCCCEECC
24.07-
62PhosphorylationGGILKSKTFSVAYVL
CCCCCCCCCCHHHHH
28.38-
104PhosphorylationLAHVQHPTGAGPHAQ
CCCCCCCCCCCCCCC
37.2223927012
115PhosphorylationPHAQEEDSQEEEEED
CCCCCCCCHHHHHHH
42.6530266825
127PhosphorylationEEDEEAASRYYVPSY
HHHHHHHHHHCCCCH
28.0623927012
129PhosphorylationDEEAASRYYVPSYEE
HHHHHHHHCCCCHHH
13.3022817900
130PhosphorylationEEAASRYYVPSYEEV
HHHHHHHCCCCHHHH
12.5529449344
133PhosphorylationASRYYVPSYEEVMNT
HHHHCCCCHHHHHCC
34.8225849741
134PhosphorylationSRYYVPSYEEVMNTN
HHHCCCCHHHHHCCC
15.2725849741
140PhosphorylationSYEEVMNTNYSEARG
CHHHHHCCCHHHHCC
19.8927642862
142PhosphorylationEEVMNTNYSEARGEE
HHHHCCCHHHHCCCC
13.0727259358
143PhosphorylationEVMNTNYSEARGEEQ
HHHCCCHHHHCCCCC
27.1829978859
155PhosphorylationEEQNPRLSISLPSYE
CCCCCCEEEECCCHH
16.0624300666
157PhosphorylationQNPRLSISLPSYESL
CCCCEEEECCCHHHH
30.7428387310
160PhosphorylationRLSISLPSYESLTGL
CEEEECCCHHHHCCC
46.9926657352
161PhosphorylationLSISLPSYESLTGLD
EEEECCCHHHHCCCC
13.9626657352
163PhosphorylationISLPSYESLTGLDET
EECCCHHHHCCCCCC
24.0125137130
165PhosphorylationLPSYESLTGLDETTP
CCCHHHHCCCCCCCC
45.0027251275
170PhosphorylationSLTGLDETTPTSTRA
HHCCCCCCCCCCCHH
37.4324300666
171PhosphorylationLTGLDETTPTSTRAD
HCCCCCCCCCCCHHH
23.6324300666
173PhosphorylationGLDETTPTSTRADVE
CCCCCCCCCCHHHHH
40.4124300666
174PhosphorylationLDETTPTSTRADVEA
CCCCCCCCCHHHHHC
19.6624300666
175PhosphorylationDETTPTSTRADVEAS
CCCCCCCCHHHHHCC
32.1424300666
182PhosphorylationTRADVEASPGNPPDR
CHHHHHCCCCCCCCH
21.6019664994
192PhosphorylationNPPDRQNSKLAKRLK
CCCCHHHCHHHHHHC
22.2525159151
193UbiquitinationPPDRQNSKLAKRLKP
CCCHHHCHHHHHHCC
61.07-
202UbiquitinationAKRLKPLKVRRIKSE
HHHHCCCEEEEECCC
42.07-
208PhosphorylationLKVRRIKSEKLHLKD
CEEEEECCCCCCCCC
37.2828857561
210UbiquitinationVRRIKSEKLHLKDFR
EEEECCCCCCCCCCE
48.58-
214UbiquitinationKSEKLHLKDFRINLP
CCCCCCCCCCEECCC
44.03-
223UbiquitinationFRINLPDKNVPPPSI
CEECCCCCCCCCCCC
58.88-
229PhosphorylationDKNVPPPSIEPLTPP
CCCCCCCCCCCCCCC
45.4130206219
234PhosphorylationPPSIEPLTPPPQYDE
CCCCCCCCCCCCCHH
44.4523401153
239PhosphorylationPLTPPPQYDEVQEKA
CCCCCCCCHHHHHHC
21.6125884760
245UbiquitinationQYDEVQEKAPDTRPP
CCHHHHHHCCCCCCC
48.40-
249PhosphorylationVQEKAPDTRPPD---
HHHHCCCCCCCC---
43.9723312004

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 TMM51_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMM51_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 TMM51_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN5_HUMANPTPN5physical
25416956
S39AB_HUMANSLC39A11physical
26186194
HS12A_HUMANHSPA12Aphysical
26186194
NEDD4_HUMANNEDD4physical
26186194
ITCH_HUMANITCHphysical
26186194
NED4L_HUMANNEDD4Lphysical
26186194
WWP1_HUMANWWP1physical
26186194
TTI1_HUMANTTI1physical
26186194
PTER_HUMANPTERphysical
26186194
CT024_HUMANC20orf24physical
26186194
AN13A_HUMANANKRD13Aphysical
26186194
FND3A_HUMANFNDC3Aphysical
26186194
KBTB7_HUMANKBTBD7physical
26186194
ZCCHL_HUMANZC3HAV1Lphysical
26186194
GALC_HUMANGALCphysical
26186194
F1142_HUMANFAM114A2physical
26186194
PDCD4_HUMANPDCD4physical
26186194
CUED1_HUMANCUEDC1physical
26186194
HECW2_HUMANHECW2physical
26186194
F1142_HUMANFAM114A2physical
28514442
PDCD4_HUMANPDCD4physical
28514442
NED4L_HUMANNEDD4Lphysical
28514442
CT024_HUMANC20orf24physical
28514442
NEDD4_HUMANNEDD4physical
28514442
HS12A_HUMANHSPA12Aphysical
28514442
PTER_HUMANPTERphysical
28514442
WWP1_HUMANWWP1physical
28514442
TTI1_HUMANTTI1physical
28514442
CUED1_HUMANCUEDC1physical
28514442
ITCH_HUMANITCHphysical
28514442
HECW2_HUMANHECW2physical
28514442
GALC_HUMANGALCphysical
28514442
FND3A_HUMANFNDC3Aphysical
28514442
S39AB_HUMANSLC39A11physical
28514442
WWP2_HUMANWWP2physical
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 TMM51_HUMAN

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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 THR-234, AND MASSSPECTROMETRY.

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