SFXN4_HUMAN - dbPTM
SFXN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SFXN4_HUMAN
UniProt AC Q6P4A7
Protein Name Sideroflexin-4
Gene Name SFXN4
Organism Homo sapiens (Human).
Sequence Length 337
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Potential iron transporter..
Protein Sequence MSLEQEEETQPGRLLGRRDAVPAFIEPNVRFWITERQSFIRRFLQWTELLDPTNVFISVESIENSRQLLCTNEDVSSPASADQRIQEAWKRSLATVHPDSSNLIPKLFRPAAFLPFMAPTVFLSMTPLKGIKSVILPQVFLCAYMAAFNSINGNRSYTCKPLERSLLMAGAVASSTFLGVIPQFVQMKYGLTGPWIKRLLPVIFLVQASGMNVYMSRSLESIKGIAVMDKEGNVLGHSRIAGTKAVRETLASRIVLFGTSALIPEVFTYFFKRTQYFRKNPGSLWILKLSCTVLAMGLMVPFSFSIFPQIGQIQYCSLEEKIQSPTEETEIFYHRGV
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------MSLEQEEET
------CCHHHCCCC
40.3830108239
2Acetylation------MSLEQEEET
------CCHHHCCCC
40.3822814378
9PhosphorylationSLEQEEETQPGRLLG
CHHHCCCCCCCCCCC
43.2629759185
81 (in isoform 3)Ubiquitination-21.0421890473
81UbiquitinationDVSSPASADQRIQEA
CCCCCCCHHHHHHHH
21.0421890473
90UbiquitinationQRIQEAWKRSLATVH
HHHHHHHHHHHCCCC
38.87-
97UbiquitinationKRSLATVHPDSSNLI
HHHHCCCCCCCCCCH
18.9822817900
101PhosphorylationATVHPDSSNLIPKLF
CCCCCCCCCCHHHHH
42.9324247654
106UbiquitinationDSSNLIPKLFRPAAF
CCCCCHHHHHCHHHH
53.9521890473
106 (in isoform 1)Ubiquitination-53.9521890473
107UbiquitinationSSNLIPKLFRPAAFL
CCCCHHHHHCHHHHH
3.5522817900
107 (in isoform 3)Ubiquitination-3.5521890473
114 (in isoform 3)Ubiquitination-2.4721890473
114UbiquitinationLFRPAAFLPFMAPTV
HHCHHHHHHHCCCEE
2.4721890473
160UbiquitinationGNRSYTCKPLERSLL
CCCCEECCCCHHHHH
44.85-
188AcetylationIPQFVQMKYGLTGPW
HHHHHHHHHCCCHHH
21.05-
188 (in isoform 2)Ubiquitination-21.0521890473
188UbiquitinationIPQFVQMKYGLTGPW
HHHHHHHHHCCCHHH
21.0521890473
197UbiquitinationGLTGPWIKRLLPVIF
CCCHHHHHHHHHHHH
32.8822817900
197AcetylationGLTGPWIKRLLPVIF
CCCHHHHHHHHHHHH
32.8819608861
197 (in isoform 1)Ubiquitination-32.8821890473
209PhosphorylationVIFLVQASGMNVYMS
HHHHHCCCCCCEEEC
22.83-
214 (in isoform 2)Ubiquitination-5.6021890473
214UbiquitinationQASGMNVYMSRSLES
CCCCCCEEECCCHHH
5.6022817900
221 (in isoform 2)Ubiquitination-34.5921890473
221UbiquitinationYMSRSLESIKGIAVM
EECCCHHHCCCEEEE
34.5921890473
223UbiquitinationSRSLESIKGIAVMDK
CCCHHHCCCEEEECC
54.2522817900
223 (in isoform 1)Ubiquitination-54.2521890473
230 (in isoform 1)Ubiquitination-49.8021890473
230UbiquitinationKGIAVMDKEGNVLGH
CCEEEECCCCCCCCC
49.8022817900
324PhosphorylationSLEEKIQSPTEETEI
CHHHHCCCCCCCCCC
36.9426471730
326PhosphorylationEEKIQSPTEETEIFY
HHHCCCCCCCCCCEE
52.2626471730

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 SFXN4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SFXN4_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 SFXN4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SFXN4_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615578Combined oxidative phosphorylation deficiency 18 (COXPD18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SFXN4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND MASS SPECTROMETRY.

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