PACN1_HUMAN - dbPTM
PACN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PACN1_HUMAN
UniProt AC Q9BY11
Protein Name Protein kinase C and casein kinase substrate in neurons protein 1
Gene Name PACSIN1
Organism Homo sapiens (Human).
Sequence Length 444
Subcellular Localization Cytoplasm. Cell projection. Cell junction, synapse, synaptosome. Cell projection, ruffle membrane. Membrane
Peripheral membrane protein. Cytoplasmic vesicle membrane
Peripheral membrane protein. Cell junction, synapse. Cytoplasm, cytosol. Cell membrane
Protein Description Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). Binds to membranes via its F-BAR domain and mediates membrane tubulation..
Protein Sequence MSSSYDEASLAPEETTDSFWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAIRGADAQEDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTTTKKEKQPKKAEGVALTNATGAVESTSQAGDRGSVSSYDRGQPYATEWSDDESGNPFGGSETNGGANPFEDDSKGVRVRALYDYDGQEQDELSFKAGDELTKLGEEDEQGWCRGRLDSGQLGLYPANYVEAI
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------MSSSYDEAS
------CCCCCCCCC
28.1728348404
3Phosphorylation-----MSSSYDEASL
-----CCCCCCCCCC
31.4528348404
4Phosphorylation----MSSSYDEASLA
----CCCCCCCCCCC
29.3328348404
9PhosphorylationSSSYDEASLAPEETT
CCCCCCCCCCCCCCC
24.0222210691
15PhosphorylationASLAPEETTDSFWEV
CCCCCCCCCCCHHHC
33.9527251275
16PhosphorylationSLAPEETTDSFWEVG
CCCCCCCCCCHHHCC
32.6927251275
25PhosphorylationSFWEVGNYKRTVKRI
CHHHCCCHHHEEEEC
8.9122210691
28PhosphorylationEVGNYKRTVKRIDDG
HCCCHHHEEEECCHH
26.6522210691
65AcetylationQQLTDWAKRWRQLIE
HHHHHHHHHHHHHHH
48.527671053
79PhosphorylationEKGPQYGSLERAWGA
HHCCCCCCHHHHHHH
23.3226091039
95PhosphorylationMTEADKVSELHQEVK
HCHHHHHHHHHHHHH
39.9322210691
121PhosphorylationKNWQKDAYHKQIMGG
HHHHHHHHHHHHHHC
21.4926074081
182PhosphorylationMNSKTEQSVTPEQQK
HHHHCCCCCCHHHHH
23.0223312004
184PhosphorylationSKTEQSVTPEQQKKL
HHCCCCCCHHHHHHH
26.7625849741
264PhosphorylationNLAENSSYIHVYREL
CHHCCCCCHHHHHHH
8.5525332170
329PhosphorylationKAEGVALTNATGAVE
CCCCCEEECCCCCCE
17.0529449344
332PhosphorylationGVALTNATGAVESTS
CCEEECCCCCCEECC
27.9529449344
337PhosphorylationNATGAVESTSQAGDR
CCCCCCEECCCCCCC
27.1028102081
338PhosphorylationATGAVESTSQAGDRG
CCCCCEECCCCCCCC
16.0230278072
339PhosphorylationTGAVESTSQAGDRGS
CCCCEECCCCCCCCC
27.5830278072
346PhosphorylationSQAGDRGSVSSYDRG
CCCCCCCCCCCCCCC
21.5125849741
348PhosphorylationAGDRGSVSSYDRGQP
CCCCCCCCCCCCCCC
25.5230278072
349PhosphorylationGDRGSVSSYDRGQPY
CCCCCCCCCCCCCCC
28.9725849741
350PhosphorylationDRGSVSSYDRGQPYA
CCCCCCCCCCCCCCC
11.3630278072
361PhosphorylationQPYATEWSDDESGNP
CCCCCCCCCCCCCCC
29.0224076635
365PhosphorylationTEWSDDESGNPFGGS
CCCCCCCCCCCCCCC
51.3618510355
372PhosphorylationSGNPFGGSETNGGAN
CCCCCCCCCCCCCCC
41.4428348404
374PhosphorylationNPFGGSETNGGANPF
CCCCCCCCCCCCCCC
40.6428348404
394PhosphorylationGVRVRALYDYDGQEQ
CCEEEEEECCCCCCC
16.0921082442
405PhosphorylationGQEQDELSFKAGDEL
CCCCCEEEECCCCHH
23.7424719451
430PhosphorylationWCRGRLDSGQLGLYP
CCCCCCCCCCCCCEE
32.7922617229

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
346SPhosphorylationKinasePAK6Q9NQU5
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PACN1_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 PACN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PACN3_HUMANPACSIN3physical
11082044
PACN1_HUMANPACSIN1physical
11082044
KAT7_HUMANKAT7physical
16169070
HD_HUMANHTTphysical
12354780
DYN1_HUMANDNM1physical
11082044
SYNJ1_HUMANSYNJ1physical
11082044
WASL_HUMANWASLphysical
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
FRIH_HUMANFTH1physical
20936779
ATP8_HUMANATP8physical
20936779
SPTB2_HUMANSPTBN1physical
20936779
TPM4_HUMANTPM4physical
20936779
GAS7_HUMANGAS7physical
20936779
PACN2_HUMANPACSIN2physical
20936779
COBL1_HUMANCOBLL1physical
20936779
COBL_HUMANCOBLphysical
20936779
EHBP1_HUMANEHBP1physical
20936779
JADE2_HUMANJADE2physical
20936779
RHG17_HUMANARHGAP17physical
20936779
ANR24_HUMANANKRD24physical
20936779
RTKN2_HUMANRTKN2physical
20936779
COBL1_HUMANCOBLL1physical
28514442
COBL_HUMANCOBLphysical
28514442
PACN2_HUMANPACSIN2physical
28514442
MPRIP_HUMANMPRIPphysical
28514442
RAI14_HUMANRAI14physical
28514442
PACN3_HUMANPACSIN3physical
28514442
TARA_HUMANTRIOBPphysical
28514442
CYTN_HUMANCST1physical
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 PACN1_HUMAN

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Related Literatures of Post-Translational Modification

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