CENPL_HUMAN - dbPTM
CENPL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPL_HUMAN
UniProt AC Q8N0S6
Protein Name Centromere protein L
Gene Name CENPL
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization Nucleus . Chromosome, centromere . Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Protein Description Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex..
Protein Sequence MDSYSAPESTPSASSRPEDYFIGATPLQKRLESVRKQSSFILTPPRRKIPQCSQLQEDVDPQKVAFLLHKQWTLYSLTPLYKFSYSNLKEYSRLLNAFIVAEKQKGLAVEVGEDFNIKVIFSTLLGMKGTQRDPEAFLVQIVSKSQLPSENREGKVLWTGWFCCVFGDSLLETVSEDFTCLPLFLANGAESNTAIIGTWFQKTFDCYFSPLAINAFNLSWMAAMWTACKMDHYVATTEFLWSVPCSPQSLDISFAIHPEDAKALWDSVHKTPGEVTQEEVDLFMDCLYSHFHRHFKIHLSATRLVRVSTSVASAHTDGKIKILCHKYLIGVLAYLTELAIFQIE
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
3Phosphorylation-----MDSYSAPEST
-----CCCCCCCCCC
21.4923663014
4Phosphorylation----MDSYSAPESTP
----CCCCCCCCCCC
12.4623663014
5Phosphorylation---MDSYSAPESTPS
---CCCCCCCCCCCC
41.1023663014
9PhosphorylationDSYSAPESTPSASSR
CCCCCCCCCCCCCCC
44.5523663014
10PhosphorylationSYSAPESTPSASSRP
CCCCCCCCCCCCCCC
21.4323663014
12PhosphorylationSAPESTPSASSRPED
CCCCCCCCCCCCCCC
40.6523663014
14PhosphorylationPESTPSASSRPEDYF
CCCCCCCCCCCCCCC
31.0823663014
15PhosphorylationESTPSASSRPEDYFI
CCCCCCCCCCCCCCC
52.1223663014
38PhosphorylationLESVRKQSSFILTPP
HHHHHHHCCCCCCCC
30.1930266825
39PhosphorylationESVRKQSSFILTPPR
HHHHHHCCCCCCCCC
17.5130266825
43 (in isoform 2)Phosphorylation-26.8224719451
43PhosphorylationKQSSFILTPPRRKIP
HHCCCCCCCCCCCCC
26.8230266825
48UbiquitinationILTPPRRKIPQCSQL
CCCCCCCCCCCCHHC
61.08-
53PhosphorylationRRKIPQCSQLQEDVD
CCCCCCCHHCCCCCC
28.7830266825
63 (in isoform 3)Ubiquitination-40.7021890473
63 (in isoform 1)Ubiquitination-40.7021890473
63 (in isoform 2)Ubiquitination-40.7021890473
63UbiquitinationQEDVDPQKVAFLLHK
CCCCCHHHHHHHHHC
40.7021890473
73PhosphorylationFLLHKQWTLYSLTPL
HHHHCCCHHHHCCCC
17.2120068231
75PhosphorylationLHKQWTLYSLTPLYK
HHCCCHHHHCCCCHH
8.3420068231
76PhosphorylationHKQWTLYSLTPLYKF
HCCCHHHHCCCCHHC
28.9520068231
78PhosphorylationQWTLYSLTPLYKFSY
CCHHHHCCCCHHCCC
12.8120068231
81PhosphorylationLYSLTPLYKFSYSNL
HHHCCCCHHCCCCCH
15.9320068231
89 (in isoform 2)Ubiquitination-59.88-
89UbiquitinationKFSYSNLKEYSRLLN
HCCCCCHHHHHHHHH
59.88-
122PhosphorylationFNIKVIFSTLLGMKG
CCCHHHHHHHHCCCC
13.6622210691
123PhosphorylationNIKVIFSTLLGMKGT
CCHHHHHHHHCCCCC
18.4322210691
144UbiquitinationFLVQIVSKSQLPSEN
HHEEECCHHHCCCCC
31.182190698
144 (in isoform 1)Ubiquitination-31.1821890473
310PhosphorylationRLVRVSTSVASAHTD
HEEEEECCHHCCCCC
14.26-
321UbiquitinationAHTDGKIKILCHKYL
CCCCCCCHHHHHHHH
32.86-
367 (in isoform 2)Ubiquitination--

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 CENPL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CENPL_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 CENPL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JMJD6_HUMANJMJD6physical
23455924
FAM9B_HUMANFAM9Bphysical
25416956
ICK_HUMANICKphysical
26186194
ICK_HUMANICKphysical
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 CENPL_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP