TRI44_HUMAN - dbPTM
TRI44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI44_HUMAN
UniProt AC Q96DX7
Protein Name Tripartite motif-containing protein 44
Gene Name TRIM44
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization
Protein Description May play a role in the process of differentiation and maturation of neuronal cells (By similarity). May regulate the activity of TRIM17. Is a negative regulator of PAX6 expression. [PubMed: 26394807]
Protein Sequence MASGVGAAFEELPHDGTCDECEPDEAPGAEEVCRECGFCYCRRHAEAHRQKFLSHHLAEYVHGSQAWTPPADGEGAGKEEAEVKVEQEREIESEAGEESESEEESESEEESETEEESEDESDEESEEDSEEEMEDEQESEAEEDNQEEGESEAEGETEAESEFDPEIEMEAERVAKRKCPDHGLDLSTYCQEDRQLICVLCPVIGAHQGHQLSTLDEAFEELRSKDSGGLKAAMIELVERLKFKSSDPKVTRDQMKMFIQQEFKKVQKVIADEEQKALHLVDIQEAMATAHVTEILADIQSHMDRLMTQMAQAKEQLDTSNESAEPKAEGDEEGPSGASEEEDT
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
3Phosphorylation-----MASGVGAAFE
-----CCCCCCHHHH
32.4824043423
17PhosphorylationEELPHDGTCDECEPD
HCCCCCCCCCCCCCC
23.8824043423
40PhosphorylationCRECGFCYCRRHAEA
HHHCCCEEHHHHHHH
6.1724043423
64PhosphorylationLAEYVHGSQAWTPPA
HHHHHHCCCCCCCCC
11.2229523821
68PhosphorylationVHGSQAWTPPADGEG
HHCCCCCCCCCCCCC
23.5529523821
178UbiquitinationAERVAKRKCPDHGLD
HHHHHHHHCCCCCCC
49.7933845483
225UbiquitinationAFEELRSKDSGGLKA
HHHHHHCCCCCCHHH
49.8623000965
231UbiquitinationSKDSGGLKAAMIELV
CCCCCCHHHHHHHHH
37.0623000965
244UbiquitinationLVERLKFKSSDPKVT
HHHHHCCCCCCCCCC
47.6833845483
249UbiquitinationKFKSSDPKVTRDQMK
CCCCCCCCCCHHHHH
62.3229967540
256UbiquitinationKVTRDQMKMFIQQEF
CCCHHHHHHHHHHHH
25.6523000965
264UbiquitinationMFIQQEFKKVQKVIA
HHHHHHHHHHHHHHC
51.8123000965
265UbiquitinationFIQQEFKKVQKVIAD
HHHHHHHHHHHHHCC
56.0423000965
268UbiquitinationQEFKKVQKVIADEEQ
HHHHHHHHHHCCHHH
38.3023000965
314UbiquitinationMTQMAQAKEQLDTSN
HHHHHHHHHHHHCCC
33.6323000965
319PhosphorylationQAKEQLDTSNESAEP
HHHHHHHCCCCCCCC
41.8825159151
320PhosphorylationAKEQLDTSNESAEPK
HHHHHHCCCCCCCCC
37.9625159151
323PhosphorylationQLDTSNESAEPKAEG
HHHCCCCCCCCCCCC
42.0325159151
327UbiquitinationSNESAEPKAEGDEEG
CCCCCCCCCCCCCCC
51.0423503661
336PhosphorylationEGDEEGPSGASEEED
CCCCCCCCCCCCCCC
58.8225159151
339PhosphorylationEEGPSGASEEEDT--
CCCCCCCCCCCCC--
49.4125159151
344PhosphorylationGASEEEDT-------
CCCCCCCC-------
43.7322199227

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 TRI44_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI44_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 TRI44_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI17_HUMANTRIM17physical
19358823
A4_HUMANAPPphysical
21832049
TRI69_HUMANTRIM69physical
25416956
ZN254_HUMANZNF254physical
28514442
DACH1_HUMANDACH1physical
28514442
RN187_HUMANRNF187physical
28514442
TRI47_HUMANTRIM47physical
28514442
BOREA_HUMANCDCA8physical
28514442
SPS2L_HUMANSPATS2Lphysical
28514442
CCD15_HUMANCCDC15physical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
TRI11_HUMANTRIM11physical
28514442
FGRL1_HUMANFGFRL1physical
28514442
ZNF91_HUMANZNF91physical
28514442
ACD11_HUMANACAD11physical
28514442
CC112_HUMANCCDC112physical
28514442
TAF1B_HUMANTAF1Bphysical
28514442
TAF1A_HUMANTAF1Aphysical
28514442
SPAS2_HUMANSPATS2physical
28514442
CC151_HUMANCCDC151physical
28514442
GOGA2_HUMANGOLGA2physical
28514442
MCRS1_HUMANMCRS1physical
28514442
KANL2_HUMANKANSL2physical
28514442
PTHB1_HUMANBBS9physical
28514442
TAF1C_HUMANTAF1Cphysical
28514442
NDUF7_HUMANNDUFAF7physical
28514442
TAF1D_HUMANTAF1Dphysical
28514442
TXLNG_HUMANTXLNGphysical
28514442
ZNF92_HUMANZNF92physical
28514442
SRBD1_HUMANSRBD1physical
28514442
TXLNA_HUMANTXLNAphysical
28514442
DACH2_HUMANDACH2physical
28514442
ZMYM1_HUMANZMYM1physical
28514442
TRAF7_HUMANTRAF7physical
28514442
CUL2_HUMANCUL2physical
28514442
DDX24_HUMANDDX24physical
28514442
MICU2_HUMANMICU2physical
28514442
TSYL1_HUMANTSPYL1physical
28514442
BAP18_HUMANC17orf49physical
28514442
AN30B_HUMANANKRD30Bphysical
28514442
MICU1_HUMANMICU1physical
28514442
BBX_HUMANBBXphysical
28514442
CK5P3_HUMANCDK5RAP3physical
28514442
BBS2_HUMANBBS2physical
28514442
ZN761_HUMANZNF761physical
28514442
BBS1_HUMANBBS1physical
28514442
MBB1A_HUMANMYBBP1Aphysical
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 TRI44_HUMAN

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Related Literatures of Post-Translational Modification

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