NFS1_HUMAN - dbPTM
NFS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFS1_HUMAN
UniProt AC Q9Y697
Protein Name Cysteine desulfurase, mitochondrial
Gene Name NFS1
Organism Homo sapiens (Human).
Sequence Length 457
Subcellular Localization Isoform Mitochondrial: Mitochondrion .
Isoform Cytoplasmic: Cytoplasm . Nucleus .
Protein Description Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor..
Protein Sequence MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
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
6 (in isoform 2)Phosphorylation-8.2222210691
26PhosphorylationGPKPAAPTRGLRLRV
CCCCCCCCCCCEEEE		32.42-
99PhosphorylationTHAYGWESEAAMERA
CCCCCCCHHHHHHHH		26.48-
112PhosphorylationRARQQVASLIGADPR
HHHHHHHHHHCCCHH		22.9720068231
120 (in isoform 2)Ubiquitination-45.9121906983
147UbiquitinationRFYRSRKKHLITTQT
HHHHHCCCCEEEECC		42.40-
157AcetylationITTQTEHKCVLDSCR
EEECCCCEEHHHHCH		21.5826822725
157MalonylationITTQTEHKCVLDSCR
EEECCCCEEHHHHCH		21.5826320211
157UbiquitinationITTQTEHKCVLDSCR
EEECCCCEEHHHHCH		21.58-
180 (in isoform 1)Ubiquitination-51.3821906983
180AcetylationVTYLPVQKSGIIDLK
EEEEECCCCCEECHH		51.3825038526
180UbiquitinationVTYLPVQKSGIIDLK
EEEEECCCCCEECHH		51.382190698
187AcetylationKSGIIDLKELEAAIQ
CCCEECHHHHHHHHC		57.4125038526
188 (in isoform 2)Ubiquitination-60.17-
212UbiquitinationVNNEIGVKQPIAEIG
ECCCCCCCCCHHHHH		45.18-
226AcetylationGRICSSRKVYFHTDA
HHHHCCCCEEEECHH		43.1426051181
226MalonylationGRICSSRKVYFHTDA
HHHHCCCCEEEECHH		43.1426320211
226SuccinylationGRICSSRKVYFHTDA
HHHHCCCCEEEECHH		43.1427452117
226UbiquitinationGRICSSRKVYFHTDA
HHHHCCCCEEEECHH		43.14-
239UbiquitinationDAAQAVGKIPLDVND
HHHHHHCCCCCCCCC		34.25-
248UbiquitinationPLDVNDMKIDLMSIS
CCCCCCCEEEEEEEE		35.61-
248AcetylationPLDVNDMKIDLMSIS
CCCCCCCEEEEEEEE		35.6125038526
258UbiquitinationLMSISGHKIYGPKGV
EEEEECCCCCCCCCC		40.94-
258OtherLMSISGHKIYGPKGV
EEEEECCCCCCCCCC		40.94-
258N6-(pyridoxal phosphate)lysineLMSISGHKIYGPKGV
EEEEECCCCCCCCCC		40.94-
263UbiquitinationGHKIYGPKGVGAIYI
CCCCCCCCCCCEEEE		62.96-
269PhosphorylationPKGVGAIYIRRRPRV
CCCCCEEEEECCCCE		6.4529496907
320AcetylationQEMEYDHKRISKLSE
HHHHCCHHHHHHHHH		48.8325038526
335UbiquitinationRLIQNIMKSLPDVVM
HHHHHHHHHCCCCHH		45.07-
397PhosphorylationYVLRAIGTDEDLAHS
HHEEECCCCHHHCCC		30.0627732954
404PhosphorylationTDEDLAHSSIRFGIG
CCHHHCCCCCCCCCC		23.1227732954
405PhosphorylationDEDLAHSSIRFGIGR
CHHHCCCCCCCCCCC		14.1227732954
414PhosphorylationRFGIGRFTTEEEVDY
CCCCCCCCCHHHHHH		31.7522817900
415PhosphorylationFGIGRFTTEEEVDYT
CCCCCCCCHHHHHHH		38.3922817900
421PhosphorylationTTEEEVDYTVEKCIQ
CCHHHHHHHHHHHHH		20.19-
422PhosphorylationTEEEVDYTVEKCIQH
CHHHHHHHHHHHHHH		20.09-
425UbiquitinationEVDYTVEKCIQHVKR
HHHHHHHHHHHHHHH		32.09-
437PhosphorylationVKRLREMSPLWEMVQ
HHHHHHCCHHHHHHH		16.4629978859
451PhosphorylationQDGIDLKSIKWTQH-
HHCCCHHHCCCCCC-		36.38-
453UbiquitinationGIDLKSIKWTQH---
CCCHHHCCCCCC---		51.81-
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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:21219885
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFS1_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 NFS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ISCU_HUMANISCUphysical
24573684
MRP1_HUMANABCC1physical
26344197
ACADM_HUMANACADMphysical
26344197
SUCB1_HUMANSUCLA2physical
26344197
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
DB00160L-Alanine
DB00151L-Cysteine
Regulatory Network of NFS1_HUMAN

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Related Literatures of Post-Translational Modification

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