FANCL_HUMAN - dbPTM
FANCL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FANCL_HUMAN
UniProt AC Q9NW38
Protein Name E3 ubiquitin-protein ligase FANCL
Gene Name FANCL
Organism Homo sapiens (Human).
Sequence Length 375
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Ubiquitin ligase protein that mediates monoubiquitination of FANCD2 in the presence of UBE2T, a key step in the DNA damage pathway. [PubMed: 12973351]
Protein Sequence MAVTEASLLRQCPLLLPQNRSKTVYEGFISAQGRDFHLRIVLPEDLQLKNARLLCSWQLRTILSGYHRIVQQRMQHSPDLMSFMMELKMLLEVALKNRQELYALPPPPQFYSSLIEEIGTLGWDKLVYADTCFSTIKLKAEDASGREHLITLKLKAKYPAESPDYFVDFPVPFCASWTPQSSLISIYSQFLAAIESLKAFWDVMDEIDEKTWVLEPEKPPRSATARRIALGNNVSINIEVDPRHPTMLPECFFLGADHVVKPLGIKLSRNIHLWDPENSVLQNLKDVLEIDFPARAILEKSDFTMDCGICYAYQLDGTIPDQVCDNSQCGQPFHQICLYEWLRGLLTSRQSFNIIFGECPYCSKPITLKMSGRKH
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------MAVTEASLL
------CCCCHHHHH
19.5522814378
4Phosphorylation----MAVTEASLLRQ
----CCCCHHHHHHH
19.1224719451
7Phosphorylation-MAVTEASLLRQCPL
-CCCCHHHHHHHCCC
23.0024719451
22 (in isoform 2)Ubiquitination-38.48-
22UbiquitinationLLPQNRSKTVYEGFI
CCCCCCCCCEEEEEE
38.4821906983
49 (in isoform 2)Ubiquitination-35.28-
49UbiquitinationLPEDLQLKNARLLCS
CCHHHHCCCHHHHHH
35.2833845483
77PhosphorylationVQQRMQHSPDLMSFM
HHHHHHCCCCHHHHH
11.8329038488
82PhosphorylationQHSPDLMSFMMELKM
HCCCCHHHHHHHHHH
19.7929038488
128PhosphorylationLGWDKLVYADTCFST
CCCCCEEEECCCEEE
14.8129496907
139SumoylationCFSTIKLKAEDASGR
CEEEEEEEEECCCCC
44.73-
139UbiquitinationCFSTIKLKAEDASGR
CEEEEEEEEECCCCC
44.73-
139SumoylationCFSTIKLKAEDASGR
CEEEEEEEEECCCCC
44.73-
144UbiquitinationKLKAEDASGREHLIT
EEEEECCCCCEEEEE
51.1821963094
149UbiquitinationDASGREHLITLKLKA
CCCCCEEEEEEEEEE
2.4721963094
153UbiquitinationREHLITLKLKAKYPA
CEEEEEEEEEECCCC
39.0129967540
154UbiquitinationEHLITLKLKAKYPAE
EEEEEEEEEECCCCC
7.9921963094
164UbiquitinationKYPAESPDYFVDFPV
CCCCCCCCEEECCCC
59.8021963094
169UbiquitinationSPDYFVDFPVPFCAS
CCCEEECCCCCCCCC
5.7421963094
178PhosphorylationVPFCASWTPQSSLIS
CCCCCCCCCHHHHHH
14.68-
218UbiquitinationTWVLEPEKPPRSATA
EEEECCCCCCCCCCC
71.6629967540
223UbiquitinationPEKPPRSATARRIAL
CCCCCCCCCCCEEEC
13.4229967540
261UbiquitinationLGADHVVKPLGIKLS
CCCCEECCCCCCEEE
33.1721963094
266UbiquitinationVVKPLGIKLSRNIHL
ECCCCCCEEECCEEE
38.3121963094
266 (in isoform 2)Ubiquitination-38.31-
271UbiquitinationGIKLSRNIHLWDPEN
CCEEECCEEEECCCC
2.4721963094
271 (in isoform 2)Ubiquitination-2.47-
276UbiquitinationRNIHLWDPENSVLQN
CCEEEECCCCCHHHH
30.9621963094
281UbiquitinationWDPENSVLQNLKDVL
ECCCCCHHHHHHHHH
2.5421963094
286UbiquitinationSVLQNLKDVLEIDFP
CHHHHHHHHHCCCCC
54.0921963094
347PhosphorylationEWLRGLLTSRQSFNI
HHHHHHHHCCCCEEE
27.2324719451
351PhosphorylationGLLTSRQSFNIIFGE
HHHHCCCCEEEEEEE
21.10-
364UbiquitinationGECPYCSKPITLKMS
EECCCCCCCEEEEEC
36.56-
369 (in isoform 2)Ubiquitination-23.52-

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
178TPhosphorylationKinaseGSK3BP49841
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FANCL_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 FANCL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCA_HUMANFANCAphysical
16474167
FANCG_HUMANFANCGphysical
16474167
FANCF_HUMANFANCFphysical
16474167
UBE2W_HUMANUBE2Wphysical
21229326
PCNA_HUMANPCNAphysical
20937699
FANCM_HUMANFANCMphysical
20347429
FANCA_HUMANFANCAphysical
20347429
FP100_HUMANC17orf70physical
20347429
FANCG_HUMANFANCGphysical
20347429
CENPS_HUMANAPITD1physical
20347429
CENPX_HUMANSTRA13physical
20347429
FANCA_HUMANFANCAphysical
18174376
FANCM_HUMANFANCMphysical
18174376
FANCG_HUMANFANCGphysical
18174376
FANCB_HUMANFANCBphysical
17396147
FANCA_HUMANFANCAphysical
17396147
FP100_HUMANC17orf70physical
17396147
FANCM_HUMANFANCMphysical
17396147
UBE2T_HUMANUBE2Tphysical
16916645
FANCL_HUMANFANCLphysical
16916645
FANCB_HUMANFANCBphysical
16720839
FANCM_HUMANFANCMphysical
16116422
FANCA_HUMANFANCAphysical
16116422
FANCL_HUMANFANCLphysical
17396147
UBE2T_HUMANUBE2Tphysical
21775430
UBE2T_HUMANUBE2Tphysical
24389026
FACD2_HUMANFANCD2physical
24623813
FANCI_HUMANFANCIphysical
24623813
UBE2T_HUMANUBE2Tphysical
19111657
UBE2W_HUMANUBE2Wphysical
19111657
FP100_HUMANC17orf70physical
24910428
4ET_HUMANEIF4ENIF1physical
25416956
DOCK8_HUMANDOCK8physical
25416956
LZTS2_HUMANLZTS2physical
25416956
RIM3A_HUMANRIMBP3physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
RBM45_HUMANRBM45physical
25416956
IHO1_HUMANCCDC36physical
25416956
FANCA_HUMANFANCAphysical
22343915
FANCM_HUMANFANCMphysical
22343915
FANCG_HUMANFANCGphysical
22343915
FAP20_HUMANC1orf86physical
22343915
FP100_HUMANC17orf70physical
22343915
UBE2T_HUMANUBE2Tphysical
26046368
FACD2_HUMANFANCD2physical
28162934
UBE2T_HUMANUBE2Tphysical
28162934
PP1R7_HUMANPPP1R7physical
27173435
ATRIP_HUMANATRIPphysical
23723247
FANCM_HUMANFANCMphysical
27398742
FANCA_HUMANFANCAphysical
27398742
FACD2_HUMANFANCD2physical
25489943
FANCA_HUMANFANCAphysical
26269593

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614083Fanconi anemia complementation group L (FANCL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FANCL_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP