NSF1C_RAT - dbPTM
NSF1C_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSF1C_RAT
UniProt AC O35987
Protein Name NSFL1 cofactor p47
Gene Name Nsfl1c
Organism Rattus norvegicus (Rat).
Sequence Length 370
Subcellular Localization Nucleus . Golgi apparatus, Golgi stack . Chromosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Predominantly nuclear in interphase cells (PubMed:12810701). Bound to the axial elements of sex chromosomes in pachytene sperma
Protein Description Reduces the ATPase activity of VCP. [PubMed: 9824302]
Protein Sequence MAEERQDALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEEEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGERRRHSGQDVHVVLKLWKTGFSLDNGDLRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLNTSSPAQQAENEAKASSSILINEAEPTTNIQIRLADGGRLVQKFNHSHRISDIRLFIVDARPAMAATSFVLMTTFPNKELADENQTLKEANLLNAVIVQRLT
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
65PhosphorylationPSSVSRGTAPSDNRV
CCCCCCCCCCCCCCC
33.9923984901
68PhosphorylationVSRGTAPSDNRVTSF
CCCCCCCCCCCCCCH
45.0823984901
73PhosphorylationAPSDNRVTSFRDLIH
CCCCCCCCCHHHHHC
20.9323984901
74PhosphorylationPSDNRVTSFRDLIHD
CCCCCCCCHHHHHCC
18.5423984901
95PhosphorylationEEEGQRFYAGGSERS
HHHCCCCCCCCCCCC
13.4123984901
99PhosphorylationQRFYAGGSERSGQQI
CCCCCCCCCCCCCCC
28.9923984901
102PhosphorylationYAGGSERSGQQIVGP
CCCCCCCCCCCCCCC
36.58-
114PhosphorylationVGPPRKKSPNELVDD
CCCCCCCCCCHHHHH
35.6723712012
124AcetylationELVDDLFKGAKEHGA
HHHHHHHHHHHHHCC
66.3222902405
127UbiquitinationDDLFKGAKEHGAVAV
HHHHHHHHHHCCEEE
59.93-
138PhosphorylationAVAVERVTKSPGETS
CEEEEEECCCCCCCC
31.8428432305
140PhosphorylationAVERVTKSPGETSKP
EEEEECCCCCCCCCC
28.8629779826
144PhosphorylationVTKSPGETSKPRPFA
ECCCCCCCCCCCCCC
48.2228432305
145PhosphorylationTKSPGETSKPRPFAG
CCCCCCCCCCCCCCC
36.0428432305
146UbiquitinationKSPGETSKPRPFAGG
CCCCCCCCCCCCCCC
53.09-
146AcetylationKSPGETSKPRPFAGG
CCCCCCCCCCCCCCC
53.0922902405
167PhosphorylationAPEEESAYVAGERRR
CCHHHHCCCCCCCCC
10.5022276854
176PhosphorylationAGERRRHSGQDVHVV
CCCCCCCCCCCHHHE
36.0223712012
189PhosphorylationVVLKLWKTGFSLDNG
HEEEHHHCCCCCCCC
31.7027097102
192PhosphorylationKLWKTGFSLDNGDLR
EHHHCCCCCCCCCCC
35.8427097102
245AcetylationHRDEDFVKPKGAFKA
CCCCCCCCCCCHHEE
40.7922902405
251AcetylationVKPKGAFKAFTGEGQ
CCCCCHHEECCCCCC
41.9022902405
270PhosphorylationTAPQVLNTSSPAQQA
CCCCCCCCCCHHHHH
26.8127097102
271PhosphorylationAPQVLNTSSPAQQAE
CCCCCCCCCHHHHHH
33.0027097102
272PhosphorylationPQVLNTSSPAQQAEN
CCCCCCCCHHHHHHH
23.4023589303
285PhosphorylationENEAKASSSILINEA
HHHHHHCCCEEEECC
26.6826022182
286PhosphorylationNEAKASSSILINEAE
HHHHHCCCEEEECCC
20.9326022182
295PhosphorylationLINEAEPTTNIQIRL
EEECCCCCCEEEEEE
24.7926022182
311UbiquitinationDGGRLVQKFNHSHRI
CCCCEEEECCCCCCC
40.43-

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
140SPhosphorylationKinaseCDK1P39951
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSF1C_RAT !!

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 NSF1C_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPL4_RATNploc4physical
10811609
TERA_RATVcpphysical
10811609

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSF1C_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.

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