TULP3_HUMAN - dbPTM
TULP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TULP3_HUMAN
UniProt AC O75386
Protein Name Tubby-related protein 3
Gene Name TULP3
Organism Homo sapiens (Human).
Sequence Length 442
Subcellular Localization Nucleus. Cell membrane. Cell projection, cilium. Cytoplasm. Secreted. Does not have a cleavable signal peptide and is secreted by a non-conventional pathway (By similarity). Translocates from the plasma membrane to the nucleus upon activation of guan
Protein Description Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. Not involved in ciliogenesis..
Protein Sequence MEASRCRLSPSGDSVFHEEMMKMRQAKLDYQRLLLEKRQRKKRLEPFMVQPNPEARLRRAKPRASDEQTPLVNCHTPHSNVILHGIDGPAAVLKPDEVHAPSVSSSVVEEDAENTVDTASKPGLQERLQKHDISESVNFDEETDGISQSACLERPNSASSQNSTDTGTSGSATAAQPADNLLGDIDDLEDFVYSPAPQGVTVRCRIIRDKRGMDRGLFPTYYMYLEKEENQKIFLLAARKRKKSKTANYLISIDPVDLSREGESYVGKLRSNLMGTKFTVYDRGICPMKGRGLVGAAHTRQELAAISYETNVLGFKGPRKMSVIIPGMTLNHKQIPYQPQNNHDSLLSRWQNRTMENLVELHNKAPVWNSDTQSYVLNFRGRVTQASVKNFQIVHKNDPDYIVMQFGRVADDVFTLDYNYPLCAVQAFGIGLSSFDSKLACE
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
9PhosphorylationEASRCRLSPSGDSVF
CCCCCCCCCCCCCHH
9.5425159151
11PhosphorylationSRCRLSPSGDSVFHE
CCCCCCCCCCCHHHH
52.4330576142
14PhosphorylationRLSPSGDSVFHEEMM
CCCCCCCCHHHHHHH
30.1529978859
27UbiquitinationMMKMRQAKLDYQRLL
HHHHHHHHHHHHHHH
33.29-
30PhosphorylationMRQAKLDYQRLLLEK
HHHHHHHHHHHHHHH
13.13-
245UbiquitinationARKRKKSKTANYLIS
EHHHCCCCCCCEEEE
61.6121890473
245UbiquitinationARKRKKSKTANYLIS
EHHHCCCCCCCEEEE
61.6121890473
245UbiquitinationARKRKKSKTANYLIS
EHHHCCCCCCCEEEE
61.61-
268UbiquitinationEGESYVGKLRSNLMG
CCCHHHHHHHHCCCC
30.59-
277UbiquitinationRSNLMGTKFTVYDRG
HHCCCCCEEEEEECC
33.0521890473
277UbiquitinationRSNLMGTKFTVYDRG
HHCCCCCEEEEEECC
33.0521890473
277UbiquitinationRSNLMGTKFTVYDRG
HHCCCCCEEEEEECC
33.05-
291MethylationGICPMKGRGLVGAAH
CCCCCCCCCCCCCCC
29.74115919169
316UbiquitinationETNVLGFKGPRKMSV
CCCCCCCCCCCCEEE
67.2321890473
316UbiquitinationETNVLGFKGPRKMSV
CCCCCCCCCCCCEEE
67.23-
316UbiquitinationETNVLGFKGPRKMSV
CCCCCCCCCCCCEEE
67.2321890473
322PhosphorylationFKGPRKMSVIIPGMT
CCCCCCEEEEECCCC
17.1322496350
345PhosphorylationQPQNNHDSLLSRWQN
CCCCCHHHHHHHHHH
24.5324719451
348PhosphorylationNNHDSLLSRWQNRTM
CCHHHHHHHHHHHHH
36.4424719451
441 (in isoform 2)Phosphorylation-10.3826552605

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 TULP3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TULP3_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 TULP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPIP1_HUMANPSTPIP1physical
25416956
ROP1A_HUMANROPN1physical
25416956
ANR54_HUMANANKRD54physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
TT21B_HUMANTTC21Bphysical
28514442
WDR35_HUMANWDR35physical
28514442
ANR54_HUMANANKRD54physical
28514442
LYSM1_HUMANLYSMD1physical
28514442
WDR19_HUMANWDR19physical
28514442
IF140_HUMANIFT140physical
28514442
ARI1_HUMANARIH1physical
28514442
FOXK2_HUMANFOXK2physical
28514442
IF122_HUMANIFT122physical
28514442
SIR1_HUMANSIRT1physical
28514442
GNL1_HUMANGNL1physical
28514442
KANL2_HUMANKANSL2physical
28514442
BCR_HUMANBCRphysical
28514442
PDLI5_HUMANPDLIM5physical
28514442
FOXK1_HUMANFOXK1physical
28514442
ARI2_HUMANARIH2physical
28514442
MCRS1_HUMANMCRS1physical
28514442
PML_HUMANPMLphysical
28514442
MYPT1_HUMANPPP1R12Aphysical
28514442
KPBB_HUMANPHKBphysical
28514442
DCA16_HUMANDCAF16physical
28514442
RAD18_HUMANRAD18physical
28514442
NUMB_HUMANNUMBphysical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
GGPPS_HUMANGGPS1physical
28514442
UBP7_HUMANUSP7physical
28514442
WAPL_HUMANWAPALphysical
28514442
KBTB7_HUMANKBTBD7physical
28514442
OBSL1_HUMANOBSL1physical
28514442
RN138_HUMANRNF138physical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
MTMR3_HUMANMTMR3physical
28514442
THNS1_HUMANTHNSL1physical
28514442
MK09_HUMANMAPK9physical
28514442
TUB_HUMANTUBphysical
28514442
PARN_HUMANPARNphysical
28514442
JMJD6_HUMANJMJD6physical
28514442
KLH42_HUMANKLHL42physical
28514442
ANKH1_HUMANANKHD1physical
28514442
MK03_HUMANMAPK3physical
28514442
BACH2_HUMANBACH2physical
28514442
DPH1_HUMANDPH1physical
28514442
IF122_HUMANIFT122physical
27173435
WDR19_HUMANWDR19physical
27173435
WDR35_HUMANWDR35physical
27173435
TT21B_HUMANTTC21Bphysical
27173435
FOXK2_HUMANFOXK2physical
27173435
RALB_HUMANRALBphysical
27173435
IFT43_HUMANIFT43physical
27173435
EXOC3_HUMANEXOC3physical
27173435

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 TULP3_HUMAN

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Related Literatures of Post-Translational Modification

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