NSF1C_MOUSE - dbPTM
NSF1C_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSF1C_MOUSE
UniProt AC Q9CZ44
Protein Name NSFL1 cofactor p47
Gene Name Nsfl1c
Organism Mus musculus (Mouse).
Sequence Length 370
Subcellular Localization Nucleus . Golgi apparatus, Golgi stack . Chromosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Predominantly nuclear in interphase cells. Bound to the axial elements of sex chromosomes in pachytene spermatocytes. A small p
Protein Description Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Inhibits the activity of CTSL (in vitro). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase. Also, regulates spindle orientation during mitosis..
Protein Sequence MAEERQDALREFVAVTGTEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEEEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGERRRHSGQDVHVVLKLWKTGFSLDNGDLRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLNTSSPAQQAENEAKASSSILINEAEPTTNIQIRLADGGRLVQKFNHSHRISDIRLFIVDARPAMAATSFVLMTTFPNKELADENQTLKEANLLNAVIVQRLT
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
68PhosphorylationVSRGTAPSDNRVTSF
CCCCCCCCCCCCCCH		45.0825338131
73PhosphorylationAPSDNRVTSFRDLIH
CCCCCCCCCHHHHHC		20.9325266776
73 (in isoform 3)Phosphorylation-20.9325521595
73 (in isoform 2)Phosphorylation-20.9325521595
74PhosphorylationPSDNRVTSFRDLIHD
CCCCCCCCHHHHHCC		18.5425266776
95PhosphorylationEEEGQRFYAGGSERS
HHHCCCCCCCCCCCC		13.4125159016
97 (in isoform 3)Phosphorylation-28.8729514104
97 (in isoform 2)Phosphorylation-28.8729514104
99PhosphorylationQRFYAGGSERSGQQI
CCCCCCCCCCCCCCC		28.9925159016
101 (in isoform 3)Phosphorylation-48.0229514104
101 (in isoform 2)Phosphorylation-48.0229514104
102PhosphorylationYAGGSERSGQQIVGP
CCCCCCCCCCCCCCC		36.5825338131
112UbiquitinationQIVGPPRKKSPNELV
CCCCCCCCCCCCHHH		64.47-
113UbiquitinationIVGPPRKKSPNELVD
CCCCCCCCCCCHHHH		72.87-
114PhosphorylationVGPPRKKSPNELVDD
CCCCCCCCCCHHHHH		35.6727087446
124AcetylationELVDDLFKGAKEHGA
HHHHHHHHHHHHHCC		66.3223236377
124UbiquitinationELVDDLFKGAKEHGA
HHHHHHHHHHHHHCC		66.32-
127UbiquitinationDDLFKGAKEHGAVAV
HHHHHHHHHHCCEEE		59.93-
138PhosphorylationAVAVERVTKSPGETS
CEEEEEECCCCCCCC		31.8424453211
139UbiquitinationVAVERVTKSPGETSK
EEEEEECCCCCCCCC		52.36-
140PhosphorylationAVERVTKSPGETSKP
EEEEECCCCCCCCCC		28.8626824392
144PhosphorylationVTKSPGETSKPRPFA
ECCCCCCCCCCCCCC		48.2225159016
145PhosphorylationTKSPGETSKPRPFAG
CCCCCCCCCCCCCCC		36.0425159016
146UbiquitinationKSPGETSKPRPFAGG
CCCCCCCCCCCCCCC		53.09-
155PhosphorylationRPFAGGGYRLGAAPE
CCCCCCCCCCCCCCH		13.1225159016
165PhosphorylationGAAPEEESAYVAGER
CCCCHHHHCCCCCCC		28.3425367039
167PhosphorylationAPEEESAYVAGERRR
CCHHHHCCCCCCCCC		10.5025159016
176PhosphorylationAGERRRHSGQDVHVV
CCCCCCCCCCCHHHE		36.0227087446
178 (in isoform 3)Phosphorylation-53.2024719451
188UbiquitinationHVVLKLWKTGFSLDN
HHEEEHHHCCCCCCC		49.56-
189PhosphorylationVVLKLWKTGFSLDNG
HEEEHHHCCCCCCCC		31.7026643407
192PhosphorylationKLWKTGFSLDNGDLR
EHHHCCCCCCCCCCC		35.8426643407
245UbiquitinationHRDEDFVKPKGAFKA
CCCCCCCCCCCHHEE		40.79-
251UbiquitinationVKPKGAFKAFTGEGQ
CCCCCHHEECCCCCC		41.90-
259UbiquitinationAFTGEGQKLGSTAPQ
ECCCCCCCCCCCCCC		66.72-
262PhosphorylationGEGQKLGSTAPQVLN
CCCCCCCCCCCCCCC		31.6525619855
263PhosphorylationEGQKLGSTAPQVLNT
CCCCCCCCCCCCCCC		40.3325619855
270PhosphorylationTAPQVLNTSSPAQQA
CCCCCCCCCCHHHHH		26.8127149854
271PhosphorylationAPQVLNTSSPAQQAE
CCCCCCCCCHHHHHH		33.0027087446
272PhosphorylationPQVLNTSSPAQQAEN
CCCCCCCCHHHHHHH		23.4025521595
311UbiquitinationDGGRLVQKFNHSHRI
CCCCEEEECCCCCCC		40.43-
356UbiquitinationADENQTLKEANLLNA
CCCCCHHHHHHHHHH		59.16-
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 NSF1C_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSF1C_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_MOUSEVcpphysical
12529442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSF1C_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-140 ANDSER-176, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND MASSSPECTROMETRY.

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