CLUA1_HUMAN - dbPTM
CLUA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLUA1_HUMAN
UniProt AC Q96AJ1
Protein Name Clusterin-associated protein 1
Gene Name CLUAP1
Organism Homo sapiens (Human).
Sequence Length 413
Subcellular Localization Cell projection, cilium . Nucleus .
Protein Description Required for cilia biogenesis. Appears to function within the multiple intraflagellar transport complex B (IFT-B). Key regulator of hedgehog signaling..
Protein Sequence MSFRDLRNFTEMMRALGYPRHISMENFRTPNFGLVSEVLLWLVKRYEPQTDIPPDVDTEQDRVFFIKAIAQFMATKAHIKLNTKKLYQADGYAVKELLKITSVLYNAMKTKGMEGSEIVEEDVNKFKFDLGSKIADLKAARQLASEITSKGASLYDLLGMEVELREMRTEAIARPLEINETEKVMRIAIKEILTQVQKTKDLLNNVASDEANLEAKIEKRKLELERNRKRLETLQSVRPCFMDEYEKTEEELQKQYDTYLEKFQNLTYLEQQLEDHHRMEQERFEEAKNTLCLIQNKLKEEEKRLLKSGSNDDSDIDIQEDDESDSELEERRLPKPQTAMEMLMQGRPGKRIVGTMQGGDSDDNEDSEESEIDMEDDDDEDDDLEDESISLSPTKPNRRVRKSEPLDESDNDF
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
2Phosphorylation------MSFRDLRNF
------CCHHHHHHH		29.0524719451
34 (in isoform 2)Ubiquitination-3.1621906983
50 (in isoform 2)Ubiquitination-46.7621906983
80UbiquitinationMATKAHIKLNTKKLY
HHHHHHHHCCCCHHH		26.31-
85AcetylationHIKLNTKKLYQADGY
HHHCCCCHHHCCCCH		50.8419816681
85UbiquitinationHIKLNTKKLYQADGY
HHHCCCCHHHCCCCH		50.84-
95AcetylationQADGYAVKELLKITS
CCCCHHHHHHHHHHH		34.1819816693
95UbiquitinationQADGYAVKELLKITS
CCCCHHHHHHHHHHH		34.18-
111UbiquitinationLYNAMKTKGMEGSEI
HHHHHHHCCCCCCHH		51.2221906983
111 (in isoform 1)Ubiquitination-51.2221906983
116PhosphorylationKTKGMEGSEIVEEDV
HHCCCCCCHHHHHHH		15.7330622161
125UbiquitinationIVEEDVNKFKFDLGS
HHHHHHHHHCCCCCH		50.18-
133 (in isoform 1)Ubiquitination-39.8621906983
133UbiquitinationFKFDLGSKIADLKAA
HCCCCCHHHHHHHHH		39.8621906983
138UbiquitinationGSKIADLKAARQLAS
CHHHHHHHHHHHHHH		40.31-
165DimethylationLGMEVELREMRTEAI
HCCEEEHHHHHHHHH		23.35-
168DimethylationEVELREMRTEAIARP
EEEHHHHHHHHHHCC		25.35-
190UbiquitinationKVMRIAIKEILTQVQ
HHHHHHHHHHHHHHH		29.67-
194PhosphorylationIAIKEILTQVQKTKD
HHHHHHHHHHHHHHH		32.15-
198UbiquitinationEILTQVQKTKDLLNN
HHHHHHHHHHHHHHH		59.70-
199PhosphorylationILTQVQKTKDLLNNV
HHHHHHHHHHHHHHH		16.82-
200UbiquitinationLTQVQKTKDLLNNVA
HHHHHHHHHHHHHHH		54.1121906983
200 (in isoform 1)Ubiquitination-54.1121906983
208PhosphorylationDLLNNVASDEANLEA
HHHHHHHCCHHHHHH		31.5327499020
216 (in isoform 1)Ubiquitination-41.8621906983
216UbiquitinationDEANLEAKIEKRKLE
CHHHHHHHHHHHHHH		41.8621906983
254UbiquitinationKTEEELQKQYDTYLE
HCHHHHHHHHHHHHH		64.55-
262UbiquitinationQYDTYLEKFQNLTYL
HHHHHHHHHHHHHHH		50.05-
267PhosphorylationLEKFQNLTYLEQQLE
HHHHHHHHHHHHHHH		33.3429083192
268PhosphorylationEKFQNLTYLEQQLED
HHHHHHHHHHHHHHH		16.0629083192
297UbiquitinationTLCLIQNKLKEEEKR
HHHHHHHHCHHHHHH		44.56-
308PhosphorylationEEKRLLKSGSNDDSD
HHHHHHHCCCCCCCC		47.6327732954
310PhosphorylationKRLLKSGSNDDSDID
HHHHHCCCCCCCCCC		44.1527732954
314PhosphorylationKSGSNDDSDIDIQED
HCCCCCCCCCCCCCC		39.0530278072
324PhosphorylationDIQEDDESDSELEER
CCCCCCCCHHHHHHH		54.1330278072
326PhosphorylationQEDDESDSELEERRL
CCCCCCHHHHHHHCC		54.0527732954
392PhosphorylationEDESISLSPTKPNRR
CCCCCCCCCCCCCCC		24.5924719451
403PhosphorylationPNRRVRKSEPLDESD
CCCCCCCCCCCCCCC		33.6023403867
409PhosphorylationKSEPLDESDNDF---
CCCCCCCCCCCC---		41.1830278072
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
-KUbiquitinationE3 ubiquitin ligaseSYVN1Q86TM6
PMID:17451556
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLUA1_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 CLUA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CINP_HUMANCINPphysical
16189514
CLUS_HUMANCLUphysical
15480429
A4_HUMANAPPphysical
21832049
EFC4B_HUMANCRACR2Aphysical
26186194
UBX10_HUMANUBXN10physical
26389662
EFC4B_HUMANCRACR2Aphysical
28514442
IFT20_HUMANIFT20physical
27173435
IFT57_HUMANIFT57physical
27173435
IF172_HUMANIFT172physical
27173435
ASAP2_HUMANASAP2physical
27173435
STX18_HUMANSTX18physical
27173435
PTHB1_HUMANBBS9physical
27173435
MIPT3_HUMANTRAF3IP1physical
27173435
BBS1_HUMANBBS1physical
27173435
TT30A_HUMANTTC30Aphysical
27173435
BBS7_HUMANBBS7physical
27173435
BBS2_HUMANBBS2physical
27173435
TT30B_HUMANTTC30Bphysical
27173435
ICK_HUMANICKphysical
27173435
IFT46_HUMANIFT46physical
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 CLUA1_HUMAN

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Related Literatures of Post-Translational Modification
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-409, AND MASSSPECTROMETRY.
"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 SER-409, AND MASSSPECTROMETRY.

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