MTL5_HUMAN - dbPTM
MTL5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTL5_HUMAN
UniProt AC Q9Y4I5
Protein Name Tesmin {ECO:0000303|PubMed:10191092}
Gene Name TESMIN {ECO:0000312|HGNC:HGNC:7446}
Organism Homo sapiens (Human).
Sequence Length 508
Subcellular Localization Cytoplasm . Nucleus . Predominantly localized to the cytoplasm. Translocates from the cytoplasm to the nucleus in the G2/M transition upon treatment with cadmium, cobalt or zinc.
Protein Description May have a role in spermatogenesis..
Protein Sequence MEEGPLPGGLPSPEDAMVTELLSPEGPFASENIGLKAPVKYEEDEFHVFKEAYLGPADPKEPVLHAFNPALGADCKGQVKAKLAGGDSDGGELLGEYPGIPELSALEDVALLQAPQPPACNVHFLSSLLPAHRSPAVLPLGAWVLEGASHPGVRMIPVEIKEAGGTTTSNNPEEATLQNLLAQESCCKFPSSQELEDASCCSLKKDSNPMVICQLKGGTQMLCIDNSRTRELKALHLVPQYQDQNNYLQSDVPKPMTALVGRFLPASTKLNLITQQLEGALPSVVNGSAFPSGSTLPGPPKITLAGYCDCFASGDFCNNCNCNNCCNNLHHDIERFKAIKACLGRNPEAFQPKIGKGQLGNVKPQHNKGCNCRRSGCLKNYCECYEAQIMCSSICKCIGCKNYEESPERKTLMSMPNYMQTGGLEGSHYLPPTKFSGLPRFSHDRRPSSCISWEVVEATCACLLAQGEEAEKEHCSKCLAEQMILEEFGRCLSQILHTEFKSKGLKME
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
12PhosphorylationPLPGGLPSPEDAMVT
CCCCCCCCHHHHHHH
46.0628348404
19PhosphorylationSPEDAMVTELLSPEG
CHHHHHHHHHCCCCC
14.0828348404
23PhosphorylationAMVTELLSPEGPFAS
HHHHHHCCCCCCCCC
33.2628348404
40AcetylationIGLKAPVKYEEDEFH
CCCCCCCCCCCCCEE
45.9819608861
134PhosphorylationSLLPAHRSPAVLPLG
HCCCCCCCCCEEECC
13.8221712546
166PhosphorylationEIKEAGGTTTSNNPE
EEEECCCCCCCCCHH
26.4419690332
167PhosphorylationIKEAGGTTTSNNPEE
EEECCCCCCCCCHHH
31.3419690332
185PhosphorylationQNLLAQESCCKFPSS
HHHHHHHHHCCCCCC
16.8522817900
283PhosphorylationQLEGALPSVVNGSAF
HHHCCCCCCCCCCCC
39.2828387310
292PhosphorylationVNGSAFPSGSTLPGP
CCCCCCCCCCCCCCC
38.6328387310
340UbiquitinationIERFKAIKACLGRNP
HHHHHHHHHHHCCCH
37.6029967540
381PhosphorylationRSGCLKNYCECYEAQ
CCCCHHHHHHHHHHH
6.5022210691
385PhosphorylationLKNYCECYEAQIMCS
HHHHHHHHHHHHHHH
7.6322210691
403PhosphorylationKCIGCKNYEESPERK
HHHCCCCCCCCCCHH
13.4322210691
406PhosphorylationGCKNYEESPERKTLM
CCCCCCCCCCHHHHH
21.8122210691
414PhosphorylationPERKTLMSMPNYMQT
CCHHHHHCCCCHHHC
33.9128985074
418PhosphorylationTLMSMPNYMQTGGLE
HHHCCCCHHHCCCCC
5.68-
433PhosphorylationGSHYLPPTKFSGLPR
CCCCCCCCCCCCCCC
42.6628985074

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 MTL5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTL5_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 MTL5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MTL5_HUMAN !!

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 MTL5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND MASS SPECTROMETRY.
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-185, AND MASSSPECTROMETRY.

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