LIN41_HUMAN - dbPTM
LIN41_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIN41_HUMAN
UniProt AC Q2Q1W2
Protein Name E3 ubiquitin-protein ligase TRIM71
Gene Name TRIM71
Organism Homo sapiens (Human).
Sequence Length 868
Subcellular Localization Cytoplasm, P-body .
Protein Description E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (Probable). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism. [PubMed: 23125361 Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression]
Protein Sequence MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSGGGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAAGGGAAGEPLKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATADEPPPKNGRAGAPAGAGGHSNHRHHAHHAHPRASASAPPLPQAPQPPAPSRSAPGGPAASPSALLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPGAAAAAQQLGLGPPFPGPPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTMGRHGGHSFIYLQEALQDSRALTIQLLADAQQGRQAIQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLRQNLNKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTVRSLLQPQEDDRVMFTPPDQALYLAIKSFGFVSSGAFAPLTKATGDGLKRALQGKVASFTVIGYDHDGEPRLSGGDLMSAVVLGPDGNLFGAEVSDQQNGTYVVSYRPQLEGEHLVSVTLCNQHIENSPFKVVVKSGRSYVGIGLPGLSFGSEGDSDGKLCRPWGVSVDKEGYIIVADRSNNRIQVFKPCGAFHHKFGTLGSRPGQFDRPAGVACDASRRIVVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGALWKHFDSPRGVAFNHEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFESNGSFLCKFGAQGSGFGQMDRPSGIAITPDGMIVVVDFGNNRILVF
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
2Acetylation------MASFPETDF
------CCCCCCCHH
21.6321406692
3Phosphorylation-----MASFPETDFQ
-----CCCCCCCHHH
39.7821406692
7Phosphorylation-MASFPETDFQICLL
-CCCCCCCHHHHHHH
42.2121406692
88UbiquitinationGAAGEPLKLRCPVCD
CCCCCCCCCCCCCCC
44.60-
187PhosphorylationAPGGPAASPSALLLR
CCCCCCCCHHHEECC
22.8419664995
189PhosphorylationGGPAASPSALLLRRP
CCCCCCHHHEECCCC
29.1119664995
325PhosphorylationLQDSRALTIQLLADA
HHCCCHHHHHHHHHH
12.9927174698
395UbiquitinationKIRQVKAKSLYLQVE
HHHHHCHHHHHHHHH
34.9632142685
396PhosphorylationIRQVKAKSLYLQVEK
HHHHCHHHHHHHHHH
27.4029396449
398PhosphorylationQVKAKSLYLQVEKLR
HHCHHHHHHHHHHHH
11.3729396449
445UbiquitinationLAQVQELKTVRSLLQ
HHHHHHHHHHHHHCC
44.19-
487PhosphorylationSGAFAPLTKATGDGL
CCCCCCCCHHCCHHH
19.99-
495MethylationKATGDGLKRALQGKV
HHCCHHHHHHHCCCE
40.95-
749PhosphorylationALWKHFDSPRGVAFN
CHHHCCCCCCCEEEE
18.6224719451
836PhosphorylationCKFGAQGSGFGQMDR
EEECCCCCCCCCCCC
20.90-

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 LIN41_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIN41_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 LIN41_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LN28B_HUMANLIN28Bphysical
24602972
AGO2_HUMANAGO2physical
24602972
DICER_HUMANDICER1physical
24602972

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 LIN41_HUMAN

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Related Literatures of Post-Translational Modification

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