NSF1C_HUMAN - dbPTM
NSF1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSF1C_HUMAN
UniProt AC Q9UNZ2
Protein Name NSFL1 cofactor p47
Gene Name NSFL1C
Organism Homo sapiens (Human).
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 (By similarity). Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis (By similarity). May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro). [PubMed: 15498563 Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase]
Protein Sequence MAAERQEALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEDEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGEKRQHSSQDVHVVLKLWKSGFSLDNGELRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLSTSSPAQQAENEAKASSSILIDESEPTTNIQIRLADGGRLVQKFNHSHRISDIRLFIVDARPAMAATSFILMTTFPNKELADESQTLKEANLLNAVIVQRLT
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
29 (in isoform 6)Phosphorylation-33.94-
29PhosphorylationRARFFLESAGWDLQI
HHHHHHHHHCCCHHH		33.9420068231
35UbiquitinationESAGWDLQIALASFY
HHHCCCHHHHHHHHH		19.2121890473
54PhosphorylationDEDIVTISQATPSSV
CCCEEEEEECCCCCC		12.3726074081
54 (in isoform 6)Phosphorylation-12.37-
56 (in isoform 6)Phosphorylation-18.06-
57PhosphorylationIVTISQATPSSVSRG
EEEEEECCCCCCCCC		18.9626074081
59PhosphorylationTISQATPSSVSRGTA
EEEECCCCCCCCCCC		38.7326074081
60PhosphorylationISQATPSSVSRGTAP
EEECCCCCCCCCCCC		25.8926074081
62PhosphorylationQATPSSVSRGTAPSD
ECCCCCCCCCCCCCC		27.2626074081
65 (in isoform 6)Phosphorylation-33.99-
65O-linked_GlycosylationPSSVSRGTAPSDNRV
CCCCCCCCCCCCCCC		33.99OGP
66 (in isoform 6)Phosphorylation-12.39-
68 (in isoform 5)Phosphorylation-45.0824719451
68PhosphorylationVSRGTAPSDNRVTSF
CCCCCCCCCCCCCCH		45.0824719451
73PhosphorylationAPSDNRVTSFRDLIH
CCCCCCCCCHHHHHC		20.9324972180
73 (in isoform 5)Phosphorylation-20.9324719451
73O-linked_GlycosylationAPSDNRVTSFRDLIH
CCCCCCCCCHHHHHC		20.93OGP
74PhosphorylationPSDNRVTSFRDLIHD
CCCCCCCCHHHHHCC		18.5421712546
74 (in isoform 4)Phosphorylation-18.54-
77UbiquitinationNRVTSFRDLIHDQDE
CCCCCHHHHHCCCCC		48.2221890473
93MethylationEEEEEGQRFYAGGSE
HHHHHCCCCCCCCCC		37.08115485623
94 (in isoform 5)Phosphorylation-3.64-
95PhosphorylationEEEGQRFYAGGSERS
HHHCCCCCCCCCCCC		13.4128796482
99PhosphorylationQRFYAGGSERSGQQI
CCCCCCCCCCCCCCC		28.9923401153
101 (in isoform 5)Phosphorylation-48.0224719451
102PhosphorylationYAGGSERSGQQIVGP
CCCCCCCCCCCCCCC		36.5825159151
104 (in isoform 5)Phosphorylation-30.9527251275
112UbiquitinationQIVGPPRKKSPNELV
CCCCCCCCCCCCHHH		64.4722053931
112 (in isoform 1)Ubiquitination-64.4721890473
112 (in isoform 4)Ubiquitination-64.4721890473
113UbiquitinationIVGPPRKKSPNELVD
CCCCCCCCCCCHHHH		72.8721890473
113 (in isoform 1)Ubiquitination-72.8721890473
113 (in isoform 4)Ubiquitination-72.8721890473
114PhosphorylationVGPPRKKSPNELVDD
CCCCCCCCCCHHHHH		35.6719664994
114 (in isoform 4)Phosphorylation-35.67-
114 (in isoform 5)Ubiquitination-35.6721890473
115 (in isoform 5)Ubiquitination-47.3921890473
116 (in isoform 5)Phosphorylation-63.4324719451
124MethylationELVDDLFKGAKEHGA
HHHHHHHHHHHHHCC		66.3272601707
124UbiquitinationELVDDLFKGAKEHGA
HHHHHHHHHHHHHCC		66.3222053931
124AcetylationELVDDLFKGAKEHGA
HHHHHHHHHHHHHCC		66.3223236377
124 (in isoform 1)Ubiquitination-66.3221890473
124 (in isoform 4)Ubiquitination-66.3221890473
126 (in isoform 5)Ubiquitination-18.0421890473
127UbiquitinationDDLFKGAKEHGAVAV
HHHHHHHHHHCCEEE		59.9321906983
1272-HydroxyisobutyrylationDDLFKGAKEHGAVAV
HHHHHHHHHHCCEEE		59.93-
127 (in isoform 1)Ubiquitination-59.9321890473
127 (in isoform 4)Ubiquitination-59.9321890473
129 (in isoform 5)Ubiquitination-28.8921890473
138PhosphorylationAVAVERVTKSPGETS
CEEEEEECCCCCCCC		31.8423927012
139UbiquitinationVAVERVTKSPGETSK
EEEEEECCCCCCCCC		52.36-
139AcetylationVAVERVTKSPGETSK
EEEEEECCCCCCCCC		52.3625953088
140PhosphorylationAVERVTKSPGETSKP
EEEEECCCCCCCCCC		28.8623927012
140 (in isoform 4)Phosphorylation-28.8628387310
141 (in isoform 5)Ubiquitination-46.31-
142 (in isoform 5)Phosphorylation-58.8824719451
144PhosphorylationVTKSPGETSKPRPFA
ECCCCCCCCCCCCCC		48.2223927012
145PhosphorylationTKSPGETSKPRPFAG
CCCCCCCCCCCCCCC		36.0423927012
146AcetylationKSPGETSKPRPFAGG
CCCCCCCCCCCCCCC		53.0923954790
146UbiquitinationKSPGETSKPRPFAGG
CCCCCCCCCCCCCCC		53.0921890473
146 (in isoform 1)Ubiquitination-53.0921890473
148 (in isoform 5)Ubiquitination-42.5821890473
155PhosphorylationRPFAGGGYRLGAAPE
CCCCCCCCCCCCCCH		13.1223403867
157 (in isoform 4)Ubiquitination-4.0521890473
160 (in isoform 6)Phosphorylation-15.39-
161 (in isoform 6)Phosphorylation-49.34-
165PhosphorylationGAAPEEESAYVAGEK
CCCCHHHHHHHCCCC		28.3421945579
167PhosphorylationAPEEESAYVAGEKRQ
CCHHHHHHHCCCCCC		10.5021945579
167NitrationAPEEESAYVAGEKRQ
CCHHHHHHHCCCCCC		10.50-
172AcetylationSAYVAGEKRQHSSQD
HHHHCCCCCCCCCCC		57.3423954790
172UbiquitinationSAYVAGEKRQHSSQD
HHHHCCCCCCCCCCC		57.3422053931
1722-HydroxyisobutyrylationSAYVAGEKRQHSSQD
HHHHCCCCCCCCCCC		57.34-
172 (in isoform 1)Ubiquitination-57.3421890473
174 (in isoform 5)Ubiquitination-52.4621890473
176PhosphorylationAGEKRQHSSQDVHVV
CCCCCCCCCCCHHHH		22.7430266825
177PhosphorylationGEKRQHSSQDVHVVL
CCCCCCCCCCHHHHH		28.4230266825
179 (in isoform 5)Phosphorylation-34.1424719451
188UbiquitinationHVVLKLWKSGFSLDN
HHHHHHHHCCCCCCC		51.6521890473
188 (in isoform 1)Ubiquitination-51.6521890473
189PhosphorylationVVLKLWKSGFSLDNG
HHHHHHHCCCCCCCC		33.2225850435
190 (in isoform 5)Ubiquitination-16.6621890473
191 (in isoform 5)Phosphorylation-9.4024719451
192PhosphorylationKLWKSGFSLDNGELR
HHHHCCCCCCCCCCC		38.0428258704
194 (in isoform 5)Phosphorylation-60.9527251275
199MethylationSLDNGELRSYQDPSN
CCCCCCCCCCCCCCH		29.08115485639
200PhosphorylationLDNGELRSYQDPSNA
CCCCCCCCCCCCCHH		39.5128152594
201PhosphorylationDNGELRSYQDPSNAQ
CCCCCCCCCCCCHHH		15.5328152594
220 (in isoform 4)Ubiquitination-33.3621890473
223MethylationGEVPAELRRLAHGGQ
CCCCHHHHHHHCCCC		24.07115485631
228 (in isoform 4)Ubiquitination-23.7121890473
235SulfoxidationGGQVNLDMEDHRDED
CCCCCCCCCCCCCCC		8.0030846556
240 (in isoform 4)Phosphorylation-57.29-
241 (in isoform 4)Phosphorylation-53.99-
245UbiquitinationHRDEDFVKPKGAFKA
CCCCCCCCCCCHHEE		40.79-
245AcetylationHRDEDFVKPKGAFKA
CCCCCCCCCCCHHEE		40.7923236377
247TrimethylationDEDFVKPKGAFKAFT
CCCCCCCCCHHEECC		58.09-
247UbiquitinationDEDFVKPKGAFKAFT
CCCCCCCCCHHEECC		58.09-
247 (in isoform 5)Ubiquitination-58.09-
247MethylationDEDFVKPKGAFKAFT
CCCCCCCCCHHEECC		58.09-
251AcetylationVKPKGAFKAFTGEGQ
CCCCCHHEECCCCCC		41.9025953088
251TrimethylationVKPKGAFKAFTGEGQ
CCCCCHHEECCCCCC		41.90-
251UbiquitinationVKPKGAFKAFTGEGQ
CCCCCHHEECCCCCC		41.9021906983
251MethylationVKPKGAFKAFTGEGQ
CCCCCHHEECCCCCC		41.90-
251 (in isoform 1)Ubiquitination-41.9021890473
251 (in isoform 4)Ubiquitination-41.9021890473
253 (in isoform 5)Ubiquitination-10.4521890473
254PhosphorylationKGAFKAFTGEGQKLG
CCHHEECCCCCCCCC		38.9026437602
259UbiquitinationAFTGEGQKLGSTAPQ
ECCCCCCCCCCCCCC		66.7221906983
259 (in isoform 1)Ubiquitination-66.7221890473
261 (in isoform 5)Ubiquitination-29.9521890473
262PhosphorylationGEGQKLGSTAPQVLS
CCCCCCCCCCCCCCC		31.6525867546
263PhosphorylationEGQKLGSTAPQVLST
CCCCCCCCCCCCCCC		40.3323403867
269PhosphorylationSTAPQVLSTSSPAQQ
CCCCCCCCCCCHHHH		27.6423401153
270PhosphorylationTAPQVLSTSSPAQQA
CCCCCCCCCCHHHHH		29.1230278072
271PhosphorylationAPQVLSTSSPAQQAE
CCCCCCCCCHHHHHH		30.8323401153
272PhosphorylationPQVLSTSSPAQQAEN
CCCCCCCCHHHHHHH		25.0925159151
274 (in isoform 5)Phosphorylation-18.9624719451
282UbiquitinationQQAENEAKASSSILI
HHHHHHHHHCCCEEE		42.4921906983
282 (in isoform 1)Ubiquitination-42.4921890473
284 (in isoform 5)Ubiquitination-24.7421890473
285PhosphorylationENEAKASSSILIDES
HHHHHHCCCEEECCC		26.6822817901
286PhosphorylationNEAKASSSILIDESE
HHHHHCCCEEECCCC		20.9322817901
311UbiquitinationDGGRLVQKFNHSHRI
CCCCEEEECCCCCCC		40.43-
313 (in isoform 5)Ubiquitination-42.67-
319PhosphorylationFNHSHRISDIRLFIV
CCCCCCCCCEEEEEE		27.2624719451
321 (in isoform 5)Phosphorylation-3.0924719451
325 (in isoform 4)Ubiquitination-3.0321890473
352PhosphorylationNKELADESQTLKEAN
CHHHCCCHHHHHHHH		29.0721815630
354PhosphorylationELADESQTLKEANLL
HHCCCHHHHHHHHHH		49.42-
356UbiquitinationADESQTLKEANLLNA
CCCHHHHHHHHHHHH		59.162190698
356 (in isoform 1)Ubiquitination-59.1621890473
358 (in isoform 5)Ubiquitination-15.4721890473
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
140SPhosphorylationKinaseCDK1P06493
PSP
176SPhosphorylationKinasePKACAP17612
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSF1C_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 NSF1C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
12810701
LIPS_HUMANLIPEphysical
16169070
RL22_HUMANRPL22physical
16169070
TADBP_HUMANTARDBPphysical
16169070
TERA_HUMANVCPphysical
18775313
NPL4_HUMANNPLOC4physical
18775313
UFD1_HUMANUFD1Lphysical
18775313
CUL1_HUMANCUL1physical
18775313
CUL2_HUMANCUL2physical
18775313
CUL3_HUMANCUL3physical
18775313
UBR1_HUMANUBR1physical
18775313
PSMD2_HUMANPSMD2physical
18775313
HIF1A_HUMANHIF1Aphysical
18775313
PPB1_HUMANALPPphysical
18775313
VCIP1_HUMANVCPIP1physical
18775313
PHAX_HUMANPHAXphysical
21900206
TERA_HUMANVCPphysical
21900206
ACBP_HUMANDBIphysical
21900206
TERA_HUMANVCPphysical
12473691
VCIP1_HUMANVCPIP1physical
12473691
TERA_HUMANVCPphysical
22350894
TCPB_HUMANCCT2physical
22939629
SH3L1_HUMANSH3BGRLphysical
22939629
UBC_HUMANUBCphysical
22990857
ALDOC_HUMANALDOCphysical
22863883
CAN2_HUMANCAPN2physical
22863883
DHX15_HUMANDHX15physical
22863883
PAPS1_HUMANPAPSS1physical
22863883
IPP2_HUMANPPP1R2physical
22863883
TBB2A_HUMANTUBB2Aphysical
22863883
EFTU_HUMANTUFMphysical
22863883
TERA_HUMANVCPphysical
16275660
UBC_HUMANUBCphysical
18775313
UBC_HUMANUBCphysical
16007098
TERA_HUMANVCPphysical
22466964
ITPA_HUMANITPAphysical
26344197
PRS4_HUMANPSMC1physical
26344197
1433S_HUMANSFNphysical
26344197
UBXN4_HUMANUBXN4physical
26344197
TERA_HUMANVCPphysical
26344197
F104A_HUMANFAM104Aphysical
26389662
TERA_HUMANVCPphysical
26389662
ASPC1_HUMANASPSCR1physical
26389662
VCIP1_HUMANVCPIP1physical
26389662
MYH13_HUMANMYH13physical
26389662
FAF1_HUMANFAF1physical
26389662
ACD11_HUMANACAD11physical
26389662
FGGY_HUMANFGGYphysical
26389662
IDE_HUMANIDEphysical
26389662
LACTB_HUMANLACTBphysical
26389662
NPL4_HUMANNPLOC4physical
26389662
UFD1_HUMANUFD1Lphysical
26389662
UBX2A_HUMANUBXN2Aphysical
26389662
UBXN7_HUMANUBXN7physical
26389662
TERA_HUMANVCPphysical
27785701
FGGY_HUMANFGGYphysical
28514442
ASPC1_HUMANASPSCR1physical
28514442
TERA_HUMANVCPphysical
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 NSF1C_HUMAN

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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-114 AND SER-272, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, 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-114 AND SER-272, ANDMASS SPECTROMETRY.
"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-114; SER-140 ANDSER-272, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-165 ANDTYR-167, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, 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-114, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND MASSSPECTROMETRY.

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