TEAN2_HUMAN - dbPTM
TEAN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TEAN2_HUMAN
UniProt AC Q96MN5
Protein Name Transcription elongation factor A N-terminal and central domain-containing protein 2
Gene Name TCEANC2
Organism Homo sapiens (Human).
Sequence Length 208
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MDKFVIRTPRIQNSPQKKDSGGKVYKQATIESLKRVVVVEDIKRWKTMLELPDQTKENLVEALQELKKKIPSREVLKSTRIGHTVNKMRKHSDSEVASLAREVYTEWKTFTEKHSNRPSIEVRSDPKTESLRKNAQKLLSEALELKMDHLLVENIERETFHLCSRLINGPYRRTVRALVFTLKHRAEIRAQVKSGSLPVGTFVQTHKK
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
1Acetylation-------MDKFVIRT
-------CCCEEEEC
13.1122814378
8PhosphorylationMDKFVIRTPRIQNSP
CCCEEEECCCCCCCC
13.0426074081
14PhosphorylationRTPRIQNSPQKKDSG
ECCCCCCCCCCCCCC
16.6025849741
20PhosphorylationNSPQKKDSGGKVYKQ
CCCCCCCCCCCEEEH
59.32-
25PhosphorylationKDSGGKVYKQATIES
CCCCCCEEEHHHHHH
10.81-
26UbiquitinationDSGGKVYKQATIESL
CCCCCEEEHHHHHHH
36.1229967540
47PhosphorylationEDIKRWKTMLELPDQ
ECHHHHHHHHCCCHH
21.7426546556
55PhosphorylationMLELPDQTKENLVEA
HHCCCHHHHHHHHHH
47.9426546556
56UbiquitinationLELPDQTKENLVEAL
HCCCHHHHHHHHHHH
38.6829967540
67UbiquitinationVEALQELKKKIPSRE
HHHHHHHHHHCCCHH
51.7929967540
78PhosphorylationPSREVLKSTRIGHTV
CCHHHHHHHCCCHHH
20.8226074081
79PhosphorylationSREVLKSTRIGHTVN
CHHHHHHHCCCHHHH
25.3926074081
84PhosphorylationKSTRIGHTVNKMRKH
HHHCCCHHHHHHHHC
22.1426074081
90UbiquitinationHTVNKMRKHSDSEVA
HHHHHHHHCCHHHHH
43.9229967540
92PhosphorylationVNKMRKHSDSEVASL
HHHHHHCCHHHHHHH
45.9620873877
94PhosphorylationKMRKHSDSEVASLAR
HHHHCCHHHHHHHHH
36.6620873877
98PhosphorylationHSDSEVASLAREVYT
CCHHHHHHHHHHHHH
27.9524719451
104PhosphorylationASLAREVYTEWKTFT
HHHHHHHHHHHHHHH
8.3229116813
105PhosphorylationSLAREVYTEWKTFTE
HHHHHHHHHHHHHHH
40.3129116813
108UbiquitinationREVYTEWKTFTEKHS
HHHHHHHHHHHHHHC
27.7729967540
109PhosphorylationEVYTEWKTFTEKHSN
HHHHHHHHHHHHHCC
36.5424719451
111PhosphorylationYTEWKTFTEKHSNRP
HHHHHHHHHHHCCCC
49.7224719451
113UbiquitinationEWKTFTEKHSNRPSI
HHHHHHHHHCCCCCE
49.6429967540
127UbiquitinationIEVRSDPKTESLRKN
EEECCCCCCHHHHHH
70.6629967540
137UbiquitinationSLRKNAQKLLSEALE
HHHHHHHHHHHHHHH
49.3229967540

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 TEAN2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TEAN2_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 TEAN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
UB2R2_HUMANUBE2R2physical
28514442
WDR70_HUMANWDR70physical
28514442
UBXN7_HUMANUBXN7physical
28514442
UB2R1_HUMANCDC34physical
28514442
WAC2A_HUMANFAM21Aphysical
28514442
DCA16_HUMANDCAF16physical
28514442
ARI1_HUMANARIH1physical
28514442
NADAP_HUMANSLC4A1APphysical
28514442
KPB2_HUMANPHKA2physical
28514442
RAD18_HUMANRAD18physical
28514442
DCAF1_HUMANVPRBPphysical
28514442
PHKG2_HUMANPHKG2physical
28514442
ANR17_HUMANANKRD17physical
28514442
WASC4_HUMANKIAA1033physical
28514442
HTSF1_HUMANHTATSF1physical
28514442
CTR9_HUMANCTR9physical
28514442
CR025_HUMANC18orf25physical
28514442
PPM1G_HUMANPPM1Gphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TEAN2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP