PACN2_HUMAN - dbPTM
PACN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PACN2_HUMAN
UniProt AC Q9UNF0
Protein Name Protein kinase C and casein kinase substrate in neurons protein 2
Gene Name PACSIN2
Organism Homo sapiens (Human).
Sequence Length 486
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Early endosome. Recycling endosome membrane. Cell projection, ruffle membrane
Peripheral membrane protein
Cytoplasmic side. Cell membrane
P
Protein Description Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. May also play a role in the formation of caveolae at the cell membrane. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis..
Protein Sequence MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ
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
39PhosphorylationDDGHRLCSDLMNCLH
CCHHHHHHHHHHHHH		38.07-
53AcetylationHERARIEKAYAQQLT
HHHHHHHHHHHHHHH		44.3025953088
53MalonylationHERARIEKAYAQQLT
HHHHHHHHHHHHHHH		44.3026320211
53UbiquitinationHERARIEKAYAQQLT
HHHHHHHHHHHHHHH		44.30-
72UbiquitinationRWRQLVEKGPQYGTV
HHHHHHHHCCCCCHH		69.30-
76PhosphorylationLVEKGPQYGTVEKAW
HHHHCCCCCHHHHHH		20.2128152594
78PhosphorylationEKGPQYGTVEKAWMA
HHCCCCCHHHHHHHH		22.1328152594
88PhosphorylationKAWMAFMSEAERVSE
HHHHHHHCHHHHHHH		27.48-
105SulfoxidationLEVKASLMNDDFEKI
HHHHHHHCCCCHHHH		4.8421406390
111UbiquitinationLMNDDFEKIKNWQKE
HCCCCHHHHHHHHHH		60.00-
117AcetylationEKIKNWQKEAFHKQM
HHHHHHHHHHHHHHH		42.5019608861
117UbiquitinationEKIKNWQKEAFHKQM
HHHHHHHHHHHHHHH		42.5019608861
122MalonylationWQKEAFHKQMMGGFK
HHHHHHHHHHHCCHH		33.1732601280
129AcetylationKQMMGGFKETKEAED
HHHHCCHHHCHHHHH		68.6825953088
129UbiquitinationKQMMGGFKETKEAED
HHHHCCHHHCHHHHH		68.68-
131PhosphorylationMMGGFKETKEAEDGF
HHCCHHHCHHHHHHH		34.4730576142
1672-HydroxyisobutyrylationHAACKEEKLAISREA
HHHHHHHHHHHHHHH		44.29-
167UbiquitinationHAACKEEKLAISREA
HHHHHHHHHHHHHHH		44.29-
171 (in isoform 2)Phosphorylation-20.6124719451
171PhosphorylationKEEKLAISREANSKA
HHHHHHHHHHHHCCC		20.6124719451
176PhosphorylationAISREANSKADPSLN
HHHHHHHCCCCCCCC		35.9528122231
177 (in isoform 2)Ubiquitination-57.5321906983
177 (in isoform 1)Ubiquitination-57.5321906983
177UbiquitinationISREANSKADPSLNP
HHHHHHCCCCCCCCH		57.532190698
181PhosphorylationANSKADPSLNPEQLK
HHCCCCCCCCHHHHH		41.1328122231
188UbiquitinationSLNPEQLKKLQDKIE
CCCHHHHHHHHHHHH		51.65-
193AcetylationQLKKLQDKIEKCKQD
HHHHHHHHHHHHHHH		39.5425953088
213UbiquitinationEKYEKSLKELDQGTP
HHHHHHHHHHHCCCH		64.42-
213 (in isoform 2)Ubiquitination-64.42-
263 (in isoform 2)Phosphorylation-6.3627642862
264UbiquitinationLSNVAGYKAIYHDLE
HHHCCCHHHHHHCHH		27.65-
267PhosphorylationVAGYKAIYHDLEQSI
CCCHHHHHHCHHHHH		8.30-
267 (in isoform 2)Phosphorylation-8.3027642862
273PhosphorylationIYHDLEQSIRAADAV
HHHCHHHHHHHHHHH		12.5023186163
284MethylationADAVEDLRWFRANHG
HHHHHHHHHHHHHCC		42.69115486319
294SulfoxidationRANHGPGMAMNWPQF
HHHCCCCCCCCCHHH		3.4430846556
296SulfoxidationNHGPGMAMNWPQFEE
HCCCCCCCCCHHHHH		3.9130846556
305PhosphorylationWPQFEEWSADLNRTL
CHHHHHHHHHHHHHH		18.3822167270
311 (in isoform 2)Phosphorylation-28.1924719451
311PhosphorylationWSADLNRTLSRREKK
HHHHHHHHHCHHHHH		28.1922167270
313PhosphorylationADLNRTLSRREKKKA
HHHHHHHCHHHHHHC		28.7822167270
313 (in isoform 2)Phosphorylation-28.7824719451
321PhosphorylationRREKKKATDGVTLTG
HHHHHHCCCCEEEEE		42.0125159151
325 (in isoform 2)Phosphorylation-24.9230108239
327 (in isoform 2)Phosphorylation-27.0128450419
332 (in isoform 2)Phosphorylation-37.9328450419
336 (in isoform 2)Phosphorylation-47.1628450419
336PhosphorylationINQTGDQSLPSKPSS
ECCCCCCCCCCCCCC		47.1625159151
339 (in isoform 2)Phosphorylation-63.5923663014
339PhosphorylationTGDQSLPSKPSSTLN
CCCCCCCCCCCCCCC		63.5924719451
342 (in isoform 2)Phosphorylation-39.4323663014
342PhosphorylationQSLPSKPSSTLNVPS
CCCCCCCCCCCCCCC		39.4322199227
343 (in isoform 2)Phosphorylation-45.5023663014
343PhosphorylationSLPSKPSSTLNVPSN
CCCCCCCCCCCCCCC		45.5022199227
344PhosphorylationLPSKPSSTLNVPSNP
CCCCCCCCCCCCCCH		27.0422199227
345 (in isoform 2)Phosphorylation-7.0325849741
346 (in isoform 2)Phosphorylation-43.6825849741
347 (in isoform 2)Phosphorylation-6.5523663014
354PhosphorylationVPSNPAQSAQSQSSY
CCCCHHHCCCCCCCC		30.3130576142
357PhosphorylationNPAQSAQSQSSYNPF
CHHHCCCCCCCCCCC		31.5730576142
359PhosphorylationAQSAQSQSSYNPFED
HHCCCCCCCCCCCCC		39.7830576142
360PhosphorylationQSAQSQSSYNPFEDE
HCCCCCCCCCCCCCC		22.6930576142
361PhosphorylationSAQSQSSYNPFEDED
CCCCCCCCCCCCCCC		31.9128270605
370PhosphorylationPFEDEDDTGSTVSEK
CCCCCCCCCCCCCCC		45.4125159151
372PhosphorylationEDEDDTGSTVSEKDD
CCCCCCCCCCCCCCC		27.9425159151
373PhosphorylationDEDDTGSTVSEKDDT
CCCCCCCCCCCCCCC		29.4225159151
375PhosphorylationDDTGSTVSEKDDTKA
CCCCCCCCCCCCCCC		38.7325159151
380PhosphorylationTVSEKDDTKAKNVSS
CCCCCCCCCCCCCCC		42.9330576142
383UbiquitinationEKDDTKAKNVSSYEK
CCCCCCCCCCCCCCC		60.48-
386PhosphorylationDTKAKNVSSYEKTQS
CCCCCCCCCCCCCCC		36.2721712546
387PhosphorylationTKAKNVSSYEKTQSY
CCCCCCCCCCCCCCC		32.7828796482
388PhosphorylationKAKNVSSYEKTQSYP
CCCCCCCCCCCCCCC		17.5928796482
391PhosphorylationNVSSYEKTQSYPTDW
CCCCCCCCCCCCCCC		15.7125850435
393PhosphorylationSSYEKTQSYPTDWSD
CCCCCCCCCCCCCCC		38.0123927012
394PhosphorylationSYEKTQSYPTDWSDD
CCCCCCCCCCCCCCC		10.5923927012
394 (in isoform 2)Phosphorylation-10.5927642862
396PhosphorylationEKTQSYPTDWSDDES
CCCCCCCCCCCCCCC		41.7023927012
396 (in isoform 2)Phosphorylation-41.7027642862
399PhosphorylationQSYPTDWSDDESNNP
CCCCCCCCCCCCCCC		37.6826503892
403PhosphorylationTDWSDDESNNPFSST
CCCCCCCCCCCCCCC		49.2323927012
408PhosphorylationDESNNPFSSTDANGD
CCCCCCCCCCCCCCC		33.3223927012
409PhosphorylationESNNPFSSTDANGDS
CCCCCCCCCCCCCCC		30.5926657352
410PhosphorylationSNNPFSSTDANGDSN
CCCCCCCCCCCCCCC		37.6225137130
416PhosphorylationSTDANGDSNPFDDDA
CCCCCCCCCCCCCCC		48.0428464451
424PhosphorylationNPFDDDATSGTEVRV
CCCCCCCCCCCEEEE		34.3828188228
425PhosphorylationPFDDDATSGTEVRVR
CCCCCCCCCCEEEEE		45.5025850435
427PhosphorylationDDDATSGTEVRVRAL
CCCCCCCCEEEEEEE		30.9523927012
446PhosphorylationGQEHDELSFKAGDEL
CCCCCEEEECCCCCC		23.7425159151
455UbiquitinationKAGDELTKMEDEDEQ
CCCCCCCCCCCCCCC		53.57-
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
313SPhosphorylationKinasePKC-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PACN2_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 PACN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PACN3_HUMANPACSIN3physical
11082044
PACN1_HUMANPACSIN1physical
16189514
PACN2_HUMANPACSIN2physical
16189514
TNFL6_HUMANFASLGphysical
12023017
DYN1_HUMANDNM1physical
11082044
SYNJ1_HUMANSYNJ1physical
11082044
WASL_HUMANWASLphysical
11082044
PACN1_HUMANPACSIN1physical
11082044
PACN2_HUMANPACSIN2physical
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
ANS1A_HUMANANKS1Aphysical
22863883
2A5G_HUMANPPP2R5Cphysical
22863883
SWP70_HUMANSWAP70physical
22863883
PACN2_HUMANPACSIN2physical
25416956
PACN1_HUMANPACSIN1physical
25416956
COBL_HUMANCOBLphysical
26186194
COBL1_HUMANCOBLL1physical
26186194
THG1_HUMANTHG1Lphysical
26186194
WIPF2_HUMANWIPF2physical
26186194
MPRIP_HUMANMPRIPphysical
26186194
CH60_HUMANHSPD1physical
26344197
COBL_HUMANCOBLphysical
28514442
COBL1_HUMANCOBLL1physical
28514442
THG1_HUMANTHG1Lphysical
28514442
MPRIP_HUMANMPRIPphysical
28514442
WIPF2_HUMANWIPF2physical
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 PACN2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-370; SER-372; THR-373AND SER-375, AND MASS SPECTROMETRY.

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