PACN3_HUMAN - dbPTM
PACN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PACN3_HUMAN
UniProt AC Q9UKS6
Protein Name Protein kinase C and casein kinase substrate in neurons protein 3
Gene Name PACSIN3
Organism Homo sapiens (Human).
Sequence Length 424
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side. Detected at the inner aspect of the plasma membrane in myotubes..
Protein Description Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity (By similarity)..
Protein Sequence MAPEEDAGGEALGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGTVEKGPQYGTLEKAWHAFFTAAERLSALHLEVREKLQGQDSERVRAWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHAARKDEKTAQTRESHAKADSAVSQEQLRKLQERVERCAKEAEKTKAQYEQTLAELHRYTPRYMEDMEQAFETCQAAERQRLLFFKDMLLTLHQHLDLSSSEKFHELHRDLHQGIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRTISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPGSPGTGQDEEWSDEESPRKAATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA
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
51AcetylationQERARIEKAYAQQLA
HHHHHHHHHHHHHHH		44.3026051181
70UbiquitinationKWRGTVEKGPQYGTL
HHHCCCCCCCCCCCH		72.1123000965
74PhosphorylationTVEKGPQYGTLEKAW
CCCCCCCCCCHHHHH		18.4029496907
76PhosphorylationEKGPQYGTLEKAWHA
CCCCCCCCHHHHHHH		27.1529496907
141UbiquitinationDGFRKAQKPWLKRLK
HHHHHHCCHHHHHHH		42.9229967540
145UbiquitinationKAQKPWLKRLKEVEA
HHCCHHHHHHHHHHH		52.3932015554
148UbiquitinationKPWLKRLKEVEASKK
CHHHHHHHHHHHHHH		64.8433845483
166PhosphorylationAARKDEKTAQTRESH
HHHHCHHHHHHHHHH		23.19-
169PhosphorylationKDEKTAQTRESHAKA
HCHHHHHHHHHHHHH		33.66-
172PhosphorylationKTAQTRESHAKADSA
HHHHHHHHHHHHCHH		26.0021601212
175UbiquitinationQTRESHAKADSAVSQ
HHHHHHHHHCHHCCH		47.5032015554
178PhosphorylationESHAKADSAVSQEQL
HHHHHHCHHCCHHHH		35.1221815630
181PhosphorylationAKADSAVSQEQLRKL
HHHCHHCCHHHHHHH		27.9325159151
276PhosphorylationHQGIEAASDEEDLRW
HHHHHHCCCHHHHHH		53.2329255136
286PhosphorylationEDLRWWRSTHGPGMA
HHHHHHHHCCCCCCC		15.8426437602
303PhosphorylationWPQFEEWSLDTQRTI
CHHHHEECCCHHHCC		21.4628857561
309PhosphorylationWSLDTQRTISRKEKG
ECCCHHHCCCCHHCC		17.3126437602
319PhosphorylationRKEKGGRSPDEVTLT
CHHCCCCCCCCEEEE		39.7219664994
324PhosphorylationGRSPDEVTLTSIVPT
CCCCCCEEEEEEEEC		23.4430266825
326PhosphorylationSPDEVTLTSIVPTRD
CCCCEEEEEEEECCC		13.6730266825
327PhosphorylationPDEVTLTSIVPTRDG
CCCEEEEEEEECCCC		25.3830266825
331PhosphorylationTLTSIVPTRDGTAPP
EEEEEEECCCCCCCC		30.4223927012
335PhosphorylationIVPTRDGTAPPPQSP
EEECCCCCCCCCCCC		40.0422167270
341PhosphorylationGTAPPPQSPGSPGTG
CCCCCCCCCCCCCCC		36.6822167270
344PhosphorylationPPPQSPGSPGTGQDE
CCCCCCCCCCCCCCC		24.4423459991
347PhosphorylationQSPGSPGTGQDEEWS
CCCCCCCCCCCCCCC		34.7523401153
354PhosphorylationTGQDEEWSDEESPRK
CCCCCCCCCCCCHHH		38.1222167270
358PhosphorylationEEWSDEESPRKAATG
CCCCCCCCHHHHHHC		28.1422167270
361UbiquitinationSDEESPRKAATGVRV
CCCCCHHHHHHCCHH		45.8429967540
364PhosphorylationESPRKAATGVRVRAL
CCHHHHHHCCHHEEH		40.8622210691
372PhosphorylationGVRVRALYDYAGQEA
CCHHEEHHHHCCCCC		13.1121945579
374PhosphorylationRVRALYDYAGQEADE
HHEEHHHHCCCCCHH		10.0821945579
383PhosphorylationGQEADELSFRAGEEL
CCCCHHHHHHHHHHH		15.6121945579
394PhosphorylationGEELLKMSEEDEQGW
HHHHHHCCHHHCCCC		35.9322468782
414PhosphorylationQSGRIGLYPANYVEC
CCCCCEEEECCCEEE		8.6228796482
418PhosphorylationIGLYPANYVECVGA-
CEEEECCCEEECCC-		10.3428796482
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 PACN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PACN3_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 PACN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PYGM_HUMANPYGMphysical
17353931
RL23A_HUMANRPL23Aphysical
17353931
NOL3_HUMANNOL3physical
17353931
DYN1_HUMANDNM1physical
11082044
SYNJ1_HUMANSYNJ1physical
11082044
WASL_HUMANWASLphysical
11082044
PACN1_HUMANPACSIN1physical
11082044
PACN2_HUMANPACSIN2physical
11082044
PACN3_HUMANPACSIN3physical
11082044
SYCC_HUMANCARSphysical
19041431
CYFP2_HUMANCYFIP2physical
19041431
ASAP1_HUMANASAP1physical
19041431
DYN2_HUMANDNM2physical
19041431
HSP7C_HUMANHSPA8physical
19041431
KHDR1_HUMANKHDRBS1physical
19041431
MILK1_HUMANMICALL1physical
19041431
AB1IP_HUMANAPBB1IPphysical
19041431
WASP_HUMANWASphysical
19041431
WIPF1_HUMANWIPF1physical
19041431
SBK1_HUMANSBK1physical
19041431
PACN1_HUMANPACSIN1physical
25416956
COBL_HUMANCOBLphysical
26186194
PACN2_HUMANPACSIN2physical
26186194
COBL1_HUMANCOBLL1physical
26186194
PACN2_HUMANPACSIN2physical
28514442
COBL1_HUMANCOBLL1physical
28514442
COBL_HUMANCOBLphysical
28514442
MILK1_HUMANMICALL1physical
28514442
RAI14_HUMANRAI14physical
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 PACN3_HUMAN

loading...

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-383, 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-344, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-319; THR-324;SER-327; SER-354 AND SER-383, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-319, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory