CDAN1_HUMAN - dbPTM
CDAN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDAN1_HUMAN
UniProt AC Q8IWY9
Protein Name Codanin-1
Gene Name CDAN1
Organism Homo sapiens (Human).
Sequence Length 1227
Subcellular Localization Cytoplasm. Nucleus. Membrane
Multi-pass membrane protein . Mainly detected as a cytoplasmic protein.
Protein Description May act as a negative regulator of ASF1 in chromatin assembly..
Protein Sequence MAAVLESLLREEVSVAAVVRWIARSTQGSEDNAGEAAALSSLRALRKEFVPFLLNFLREQSSRVLPQGPPTPAKTPGASAALPGRPGGPPRGSRGARSQLFPPTEAQSTAAEAPLARRGGRRRGPGPARERGGRGLEEGVSGESLPGAGGRRLRGSGSPSRPSLTLSDPPNLSNLEEFPPVGSVPPGPTGTKPSRRINPTPVSEERSLSKPKTCFTSPPISCVPSSQPSALDTSPWGLGLPPGCRSLQEEREMLRKERSKQLQQSPTPTCPTPELGSPLPSRTGSLTDEPADPARVSSRQRLELVALVYSSCIAENLVPNLFLELFFVFQLLTARRMVTAKDSDPELSPAVLDSLESPLFQSIHDCVFFAVQVLECHFQVLSNLDKGTLKLLAENERLLCFSPALQGRLRAAYEGSVAKVSLVMPPSTQAVSFQPETDNRANFSSDRAFHTFKKQRDVFYEVLREWEDHHEEPGWDFEKGLGSRIRAMMGQLSAACSHSHFVRLFQKQLLQMCQSPGGAGGTVLGEAPDVLSMLGADKLGRLWRLQERLMAPQSSGGPCPPPTFPGCQGFFRDFILSASSFQFNQHLMDSLSLKIQELNGLALPQHEPNDEDGESDVDWQGERKQFAVVLLSLRLLAKFLGFVAFLPYRGPEPPPTGELQDSILALRSQVPPVLDVRTLLQRGLQARRAVLTVPWLVEFLSFADHVVPLLEYYRDIFTLLLRLHRSLVLSQESEGKMCFLNKLLLLAVLGWLFQIPTVPEDLFFLEEGPSYAFEVDTVAPEHGLDNAPVVDQQLLYTCCPYIGELRKLLASWVSGSSGRSGGFMRKITPTTTTSLGAQPSQTSQGLQAQLAQAFFHNQPPSLRRTVEFVAERIGSNCVKHIKATLVADLVRQAESLLQEQLVTQGEEGGDPAQLLEILCSQLCPHGAQALALGREFCQRKSPGAVRALLPEETPAAVLSSAENIAVGLATEKACAWLSANITALIRREVKAAVSRTLRAQGPEPAARGERRGCSRACEHHAPLPSHLISEIKDVLSLAVGPRDPDEGVSPEHLEQLLGQLGQTLRCRQFLCPPAEQHLAKCSVELASLLVADQIPILGPPAQYRLERGQARRLLHMLLSLWKEDFQGPVPLQLLLSPRNVGLLADTRPREWDLLLFLLRELVEKGLMGRMEIEACLGSLHQAQWPGDFAEELATLSNLFLAEPHLPEPQLRACELVQPNRGTVLAQS
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
2Acetylation------MAAVLESLL
------CHHHHHHHH
19.9922223895
40PhosphorylationAGEAAALSSLRALRK
HHHHHHHHHHHHHHH
23.7030301811
41PhosphorylationGEAAALSSLRALRKE
HHHHHHHHHHHHHHH
23.7925954137
71PhosphorylationVLPQGPPTPAKTPGA
CCCCCCCCCCCCCCC
38.7330266825
75PhosphorylationGPPTPAKTPGASAAL
CCCCCCCCCCCCCCC
29.1230576142
79PhosphorylationPAKTPGASAALPGRP
CCCCCCCCCCCCCCC
21.7130576142
93PhosphorylationPGGPPRGSRGARSQL
CCCCCCCCCCCHHHC
28.9022496350
131MethylationGPGPARERGGRGLEE
CCCCCCCCCCCCCCC
47.52-
134MethylationPARERGGRGLEEGVS
CCCCCCCCCCCCCCC
49.72-
141PhosphorylationRGLEEGVSGESLPGA
CCCCCCCCCCCCCCC
47.9328555341
144PhosphorylationEEGVSGESLPGAGGR
CCCCCCCCCCCCCCC
43.3128555341
156PhosphorylationGGRRLRGSGSPSRPS
CCCCCCCCCCCCCCC
29.6628122231
158PhosphorylationRRLRGSGSPSRPSLT
CCCCCCCCCCCCCCC
22.7722817900
160PhosphorylationLRGSGSPSRPSLTLS
CCCCCCCCCCCCCCC
59.5328122231
163PhosphorylationSGSPSRPSLTLSDPP
CCCCCCCCCCCCCCC
32.6428122231
165PhosphorylationSPSRPSLTLSDPPNL
CCCCCCCCCCCCCCC
28.6728122231
167PhosphorylationSRPSLTLSDPPNLSN
CCCCCCCCCCCCCCC
42.7228122231
173PhosphorylationLSDPPNLSNLEEFPP
CCCCCCCCCCCCCCC
46.1128122231
194PhosphorylationGPTGTKPSRRINPTP
CCCCCCCCCCCCCCC
35.4325072903
200PhosphorylationPSRRINPTPVSEERS
CCCCCCCCCCCCCCC
31.6625072903
203PhosphorylationRINPTPVSEERSLSK
CCCCCCCCCCCCCCC
34.6421815630
203O-linked_GlycosylationRINPTPVSEERSLSK
CCCCCCCCCCCCCCC
34.6430620550
209PhosphorylationVSEERSLSKPKTCFT
CCCCCCCCCCCCCCC
48.4324719451
259PhosphorylationEMLRKERSKQLQQSP
HHHHHHHHHHHHHCC
26.3328111955
260UbiquitinationMLRKERSKQLQQSPT
HHHHHHHHHHHHCCC
62.34-
264 (in isoform 1)Phosphorylation-61.0328842319
265PhosphorylationRSKQLQQSPTPTCPT
HHHHHHHCCCCCCCC
20.1330278072
267PhosphorylationKQLQQSPTPTCPTPE
HHHHHCCCCCCCCCC
36.1630278072
269PhosphorylationLQQSPTPTCPTPELG
HHHCCCCCCCCCCCC
33.3330278072
272PhosphorylationSPTPTCPTPELGSPL
CCCCCCCCCCCCCCC
31.3822617229
277PhosphorylationCPTPELGSPLPSRTG
CCCCCCCCCCCCCCC
35.5730278072
281PhosphorylationELGSPLPSRTGSLTD
CCCCCCCCCCCCCCC
50.5930278072
283PhosphorylationGSPLPSRTGSLTDEP
CCCCCCCCCCCCCCC
35.1530108239
285PhosphorylationPLPSRTGSLTDEPAD
CCCCCCCCCCCCCCC
27.7323927012
287PhosphorylationPSRTGSLTDEPADPA
CCCCCCCCCCCCCHH
39.7628450419
390UbiquitinationNLDKGTLKLLAENER
CCCHHHHHHHHHCCC
41.0929967540
413PhosphorylationQGRLRAAYEGSVAKV
HHHHHHHHCCCEEEE
21.6022985185
416PhosphorylationLRAAYEGSVAKVSLV
HHHHHCCCEEEEEEE
13.6322985185
453UbiquitinationDRAFHTFKKQRDVFY
HHHHHHHHHHHHHHH
49.5029967540
515PhosphorylationQLLQMCQSPGGAGGT
HHHHHHCCCCCCCCE
22.15-
522PhosphorylationSPGGAGGTVLGEAPD
CCCCCCCEECCCCCC
16.19-
532PhosphorylationGEAPDVLSMLGADKL
CCCCCHHHHHCHHHH
16.29-
590PhosphorylationFNQHLMDSLSLKIQE
HCHHHHHHHHHHHHH
13.0924719451
592PhosphorylationQHLMDSLSLKIQELN
HHHHHHHHHHHHHHC
31.4124719451
662PhosphorylationPTGELQDSILALRSQ
CCCCHHHHHHHHHCC
13.41-
668PhosphorylationDSILALRSQVPPVLD
HHHHHHHCCCCCCCC
36.06-
701PhosphorylationPWLVEFLSFADHVVP
HHHHHHHHHCHHHHH
24.57-
712PhosphorylationHVVPLLEYYRDIFTL
HHHHHHHHHHHHHHH
12.08-
713PhosphorylationVVPLLEYYRDIFTLL
HHHHHHHHHHHHHHH
7.76-
811PhosphorylationELRKLLASWVSGSSG
HHHHHHHHHHCCCCC
28.1628270605
814PhosphorylationKLLASWVSGSSGRSG
HHHHHHHCCCCCCCC
27.0528270605
816PhosphorylationLASWVSGSSGRSGGF
HHHHHCCCCCCCCCC
23.3228270605
817PhosphorylationASWVSGSSGRSGGFM
HHHHCCCCCCCCCCC
41.5728270605
828UbiquitinationGGFMRKITPTTTTSL
CCCCCCCCCCCCCCC
20.0224816145
879UbiquitinationRIGSNCVKHIKATLV
HHCHHHHHHHHHHHH
41.6429967540
882UbiquitinationSNCVKHIKATLVADL
HHHHHHHHHHHHHHH
34.73-
940AcetylationGREFCQRKSPGAVRA
CHHHHHCCCCCHHHH
34.817822375
1025PhosphorylationEHHAPLPSHLISEIK
HCCCCCCHHHHHHHH
38.3129083192
1029PhosphorylationPLPSHLISEIKDVLS
CCCHHHHHHHHHHHH
39.3629083192
1136PhosphorylationVPLQLLLSPRNVGLL
CCCHHEECCCCCCCC
23.0624719451
1164UbiquitinationLLRELVEKGLMGRME
HHHHHHHCCCCCCHH
50.2824816145
1165UbiquitinationLRELVEKGLMGRMEI
HHHHHHCCCCCCHHH
13.8524816145
1172UbiquitinationGLMGRMEIEACLGSL
CCCCCHHHHHHHHHH
2.7324816145
1173UbiquitinationLMGRMEIEACLGSLH
CCCCHHHHHHHHHHH
21.7424816145

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 CDAN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDAN1_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 CDAN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IPO4_HUMANIPO4physical
22407294
ASF1A_HUMANASF1Aphysical
22407294
ASF1B_HUMANASF1Bphysical
22407294
ACTN1_HUMANACTN1physical
22863883
SF3A3_HUMANSF3A3physical
22863883

Drug and Disease Associations
Kegg Disease
H00917 Congenital dyserythropoietic anemias (CDAs)
OMIM Disease
224120Anemia, congenital dyserythropoietic, 1A (CDAN1A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDAN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-71; SER-265 AND SER-277,AND MASS SPECTROMETRY.

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