ZFAN6_HUMAN - dbPTM
ZFAN6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZFAN6_HUMAN
UniProt AC Q6FIF0
Protein Name AN1-type zinc finger protein 6
Gene Name ZFAND6
Organism Homo sapiens (Human).
Sequence Length 208
Subcellular Localization Cytoplasm.
Protein Description Involved in regulation of TNF-alpha induced NF-kappa-B activation and apoptosis. Involved in modulation of 'Lys-48'-linked polyubiquitination status of TRAF2 and decreases association of TRAF2 with RIPK1. Required for PTS1 target sequence-dependent protein import into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro involved in PEX5 export from the cytosol to peroxisomes (By similarity)..
Protein Sequence MAQETNHSQVPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQNSSNGRISPPATSVSSLSESLPVQCTDGSVPEAQSALDSTSSSMQPSPVSNQSLLSESVASSQLDSTSVDKAVPETEDVQASVSDTAQQPSEEQSKSLEKPKQKKNRCFMCRKKVGLTGFECRCGNVYCGVHRYSDVHNCSYNYKADAAEKIRKENPVVVGEKIQKI
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
5Phosphorylation---MAQETNHSQVPM
---CCCCCCCCCCCE
26.5924043423
8PhosphorylationMAQETNHSQVPMLCS
CCCCCCCCCCCEEEC
34.6424043423
15PhosphorylationSQVPMLCSTGCGFYG
CCCCEEECCCCCCCC
24.7124043423
16PhosphorylationQVPMLCSTGCGFYGN
CCCEEECCCCCCCCC
35.1824043423
21PhosphorylationCSTGCGFYGNPRTNG
ECCCCCCCCCCCCCC
10.9824043423
26PhosphorylationGFYGNPRTNGMCSVC
CCCCCCCCCCCCCHH
37.0624043423
31PhosphorylationPRTNGMCSVCYKEHL
CCCCCCCCHHHHHHH
13.3124043423
34PhosphorylationNGMCSVCYKEHLQRQ
CCCCCHHHHHHHHHH
19.7724043423
35UbiquitinationGMCSVCYKEHLQRQN
CCCCHHHHHHHHHHC
33.27-
43PhosphorylationEHLQRQNSSNGRISP
HHHHHHCCCCCCCCC
19.4926074081
44PhosphorylationHLQRQNSSNGRISPP
HHHHHCCCCCCCCCC
51.3426074081
49PhosphorylationNSSNGRISPPATSVS
CCCCCCCCCCCCCHH
24.3826074081
53PhosphorylationGRISPPATSVSSLSE
CCCCCCCCCHHHCCC
35.1226074081
54PhosphorylationRISPPATSVSSLSES
CCCCCCCCHHHCCCC
23.3126074081
56PhosphorylationSPPATSVSSLSESLP
CCCCCCHHHCCCCCC
25.9026074081
57PhosphorylationPPATSVSSLSESLPV
CCCCCHHHCCCCCCC
33.4926074081
59PhosphorylationATSVSSLSESLPVQC
CCCHHHCCCCCCCCC
27.3826074081
88PhosphorylationTSSSMQPSPVSNQSL
CCCCCCCCCCCCHHH
22.5026074081
91PhosphorylationSMQPSPVSNQSLLSE
CCCCCCCCCHHHHCH
32.3226074081
110UbiquitinationSQLDSTSVDKAVPET
HCCCCCCCCCCCCCC
9.9121890473
114UbiquitinationSTSVDKAVPETEDVQ
CCCCCCCCCCCHHCC
5.6122817900
117PhosphorylationVDKAVPETEDVQASV
CCCCCCCCHHCCCHH
31.2625159151
123PhosphorylationETEDVQASVSDTAQQ
CCHHCCCHHCCCCCC
12.6928450419
125 (in isoform 2)Ubiquitination-27.0921890473
125UbiquitinationEDVQASVSDTAQQPS
HHCCCHHCCCCCCCC
27.0921890473
125PhosphorylationEDVQASVSDTAQQPS
HHCCCHHCCCCCCCC
27.0928450419
127PhosphorylationVQASVSDTAQQPSEE
CCCHHCCCCCCCCHH
20.8930576142
128UbiquitinationQASVSDTAQQPSEEQ
CCHHCCCCCCCCHHH
15.8224816145
129UbiquitinationASVSDTAQQPSEEQS
CHHCCCCCCCCHHHH
58.7822817900
132PhosphorylationSDTAQQPSEEQSKSL
CCCCCCCCHHHHHHC
49.8023401153
136PhosphorylationQQPSEEQSKSLEKPK
CCCCHHHHHHCCCHH
27.7329116813
137 (in isoform 1)Ubiquitination-59.7721890473
137UbiquitinationQPSEEQSKSLEKPKQ
CCCHHHHHHCCCHHH
59.7721890473
138PhosphorylationPSEEQSKSLEKPKQK
CCHHHHHHCCCHHHH
47.1929496963
141UbiquitinationEQSKSLEKPKQKKNR
HHHHHCCCHHHHCCC
63.9122817900
143AcetylationSKSLEKPKQKKNRCF
HHHCCCHHHHCCCEE
82.7425953088
143UbiquitinationSKSLEKPKQKKNRCF
HHHCCCHHHHCCCEE
82.7424816145
148UbiquitinationKPKQKKNRCFMCRKK
CHHHHCCCEEECCCC
24.7527667366
154UbiquitinationNRCFMCRKKVGLTGF
CCEEECCCCCCCCCE
47.0533845483
155UbiquitinationRCFMCRKKVGLTGFE
CEEECCCCCCCCCEE
23.3724816145
157UbiquitinationFMCRKKVGLTGFECR
EECCCCCCCCCEEEE
26.8032015554
159PhosphorylationCRKKVGLTGFECRCG
CCCCCCCCCEEEECC
33.6228555341
159UbiquitinationCRKKVGLTGFECRCG
CCCCCCCCCEEEECC
33.6227667366
165UbiquitinationLTGFECRCGNVYCGV
CCCEEEECCCEEEEE
7.6133845483
166UbiquitinationTGFECRCGNVYCGVH
CCEEEECCCEEEEEE
13.7932015554
168UbiquitinationFECRCGNVYCGVHRY
EEEECCCEEEEEEEC
2.2532015554
169UbiquitinationECRCGNVYCGVHRYS
EEECCCEEEEEEECC
6.3624816145
174UbiquitinationNVYCGVHRYSDVHNC
CEEEEEEECCCCCCC
30.1927667366
176PhosphorylationYCGVHRYSDVHNCSY
EEEEEECCCCCCCCC
32.8725159151
177UbiquitinationCGVHRYSDVHNCSYN
EEEEECCCCCCCCCE
36.4432015554
180UbiquitinationHRYSDVHNCSYNYKA
EECCCCCCCCCEECH
19.1133845483
182PhosphorylationYSDVHNCSYNYKADA
CCCCCCCCCEECHHH
23.0225159151
183UbiquitinationSDVHNCSYNYKADAA
CCCCCCCCEECHHHH
25.3932015554
185PhosphorylationVHNCSYNYKADAAEK
CCCCCCEECHHHHHH
10.18-
186UbiquitinationHNCSYNYKADAAEKI
CCCCCEECHHHHHHH
35.8327667366
192UbiquitinationYKADAAEKIRKENPV
ECHHHHHHHHHHCCE
42.9832015554
195UbiquitinationDAAEKIRKENPVVVG
HHHHHHHHHCCEEEE
66.3733845483
204AcetylationNPVVVGEKIQKI---
CCEEEEHHHCCC---
44.5023954790
204UbiquitinationNPVVVGEKIQKI---
CCEEEEHHHCCC---
44.5027667366
207AcetylationVVGEKIQKI------
EEEHHHCCC------
54.5825953088
207UbiquitinationVVGEKIQKI------
EEEHHHCCC------
54.5824816145

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 ZFAN6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFAN6_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 ZFAN6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
21810480
CDV3_HUMANCDV3physical
26344197
CIRBP_HUMANCIRBPphysical
26344197
GSHB_HUMANGSSphysical
26344197
ROA3_HUMANHNRNPA3physical
26344197
NONO_HUMANNONOphysical
26344197
TXLNG_HUMANTXLNGphysical
26344197
TRAF2_HUMANTRAF2physical
28514442
BIRC2_HUMANBIRC2physical
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 ZFAN6_HUMAN

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Related Literatures of Post-Translational Modification

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