TERF2_HUMAN - dbPTM
TERF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TERF2_HUMAN
UniProt AC Q15554
Protein Name Telomeric repeat-binding factor 2
Gene Name TERF2
Organism Homo sapiens (Human).
Sequence Length 542
Subcellular Localization Nucleus . Chromosome, telomere . Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase.
Protein Description Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length..
Protein Sequence MAAGAGTAGPASGPGVVRDPAASQPRKRPGREGGEGARRSDTMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDKQPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRLVLEEDSQSTEPSAGLNSSQEAASAPPSKPTVLNQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDEDSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLGMN
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
12PhosphorylationAGTAGPASGPGVVRD
CCCCCCCCCCCCCCC
28.8622210691
18 (in isoform 3)Methylation-35.68-
28 (in isoform 3)Methylation-45.58-
40PhosphorylationGGEGARRSDTMAGGG
CCCCCCCCCCCCCCC
55.5728985074
42PhosphorylationEGARRSDTMAGGGGS
CCCCCCCCCCCCCCC
29.4628111955
49PhosphorylationTMAGGGGSSDGSGRA
CCCCCCCCCCCCCHH
38.0528111955
50PhosphorylationMAGGGGSSDGSGRAA
CCCCCCCCCCCCHHH
63.6128111955
53PhosphorylationGGGSSDGSGRAAGRR
CCCCCCCCCHHHCCH
38.8628111955
55 (in isoform 3)Methylation-8.45-
55MethylationGSSDGSGRAAGRRAS
CCCCCCCHHHCCHHH
8.4520676309
59 (in isoform 3)Asymmetric dimethylarginine-7.43-
59 (in isoform 3)Methylation-7.43-
59MethylationGSGRAAGRRASRSSG
CCCHHHCCHHHCCCC
7.4319596784
60 (in isoform 3)Methylation-11.48-
60MethylationSGRAAGRRASRSSGR
CCHHHCCHHHCCCCC
11.4819596784
63 (in isoform 3)Methylation-39.23-
63MethylationAAGRRASRSSGRARR
HHCCHHHCCCCCCCC
39.2320676329
67 (in isoform 3)Methylation-10.19-
67MethylationRASRSSGRARRGRHE
HHHCCCCCCCCCCCC
10.1920676305
69 (in isoform 3)Methylation-40.99-
69MethylationSRSSGRARRGRHEPG
HCCCCCCCCCCCCCC
40.9920676325
70 (in isoform 3)Methylation-15.26-
70MethylationRSSGRARRGRHEPGL
CCCCCCCCCCCCCCC
15.2620676317
72 (in isoform 3)Methylation-42.13-
72MethylationSGRARRGRHEPGLGG
CCCCCCCCCCCCCCC
42.1320676321
93UbiquitinationGEARLEEAVNRWVLK
CHHHHHHHHHHHHHH
54.74-
135 (in isoform 3)Ubiquitination-3.81-
169AcetylationFDMEAELTPLESAIN
CCCEEEECCHHHHHH
59.80-
169PhosphorylationFDMEAELTPLESAIN
CCCEEEECCHHHHHH
59.8029888752
173AcetylationAELTPLESAINVLEM
EEECCHHHHHHHHHH
64.38-
173PhosphorylationAELTPLESAINVLEM
EEECCHHHHHHHHHH
64.3829888752
188PhosphorylationIKTEFTLTEAVVESS
HHCCCCHHHHHHHHH
29.1516223874
188 (in isoform 3)Phosphorylation-29.15-
211 (in isoform 3)Acetylation-19.39-
211AcetylationVIICIKNKEFEKASK
EEEEECCHHHHHHHH
19.3920167786
215 (in isoform 3)Acetylation-41.78-
215AcetylationIKNKEFEKASKILKK
ECCHHHHHHHHHHHH
41.7820167786
225PhosphorylationKILKKHMSKDPTTQK
HHHHHHCCCCCCHHH
5.5129083192
229 (in isoform 3)Phosphorylation-9.92-
229PhosphorylationKHMSKDPTTQKLRND
HHCCCCCCHHHHHHH
9.92-
230 (in isoform 3)Phosphorylation-47.88-
230PhosphorylationHMSKDPTTQKLRNDL
HCCCCCCHHHHHHHH
47.8822817900
232UbiquitinationSKDPTTQKLRNDLLN
CCCCCHHHHHHHHHH
21.2329967540
241UbiquitinationRNDLLNIIREKNLAH
HHHHHHHHHHCCCCC
27.97-
242UbiquitinationNDLLNIIREKNLAHP
HHHHHHHHHCCCCCH
49.79-
253UbiquitinationLAHPVIQNFSYETFQ
CCCHHHCCCCHHHHH
50.1823000965
257UbiquitinationVIQNFSYETFQQKML
HHCCCCHHHHHHHHH
59.3821890473
280PhosphorylationDAEPYLLTMAKKALK
CHHHHHHHHHHHHHH
45.8024719451
287 (in isoform 3)Sumoylation-19.06-
287SumoylationTMAKKALKSESAASS
HHHHHHHHCCHHHHC
19.0628112733
288 (in isoform 3)Phosphorylation-1.61-
288PhosphorylationMAKKALKSESAASST
HHHHHHHCCHHHHCC
1.61-
290 (in isoform 3)Phosphorylation-22.65-
290PhosphorylationKKALKSESAASSTGK
HHHHHCCHHHHCCCC
22.65-
293UbiquitinationLKSESAASSTGKEDK
HHCCHHHHCCCCCCC
43.7821890473
294PhosphorylationKSESAASSTGKEDKQ
HCCHHHHCCCCCCCC
21.5028985074
297UbiquitinationSAASSTGKEDKQPAP
HHHHCCCCCCCCCCC
30.3024816145
312 (in isoform 3)Dimethylation-36.05-
312MethylationGPVEKPPREPARQLR
CCCCCCCCCHHHHHC
36.0524411731
316 (in isoform 3)Dimethylation-18.25-
316MethylationKPPREPARQLRNPPT
CCCCCHHHHHCCCCC
18.2524411739
323PhosphorylationRQLRNPPTTIGMMTL
HHHCCCCCCHHHHHH
14.5718669648
323 (in isoform 3)Phosphorylation-14.57-
324 (in isoform 3)Phosphorylation-43.66-
324PhosphorylationQLRNPPTTIGMMTLK
HHCCCCCCHHHHHHH
43.6623403867
329PhosphorylationPTTIGMMTLKAAFKT
CCCHHHHHHHHHHHH
63.2923403867
331UbiquitinationTIGMMTLKAAFKTLS
CHHHHHHHHHHHHHC
49.6523000965
334UbiquitinationMMTLKAAFKTLSGAQ
HHHHHHHHHHHCCCC
66.2923000965
335 (in isoform 3)Acetylation-66.97-
335 (in isoform 3)Ubiquitination-66.97-
335UbiquitinationMTLKAAFKTLSGAQD
HHHHHHHHHHCCCCC
66.9721890473
335AcetylationMTLKAAFKTLSGAQD
HHHHHHHHHHCCCCC
66.9725953088
335SumoylationMTLKAAFKTLSGAQD
HHHHHHHHHHCCCCC
66.9728112733
338 (in isoform 3)Phosphorylation-43.30-
338PhosphorylationKAAFKTLSGAQDSEA
HHHHHHHCCCCCHHH
43.30-
338UbiquitinationKAAFKTLSGAQDSEA
HHHHHHHCCCCCHHH
43.3021890473
349UbiquitinationDSEAAFAKLDQKDLV
CHHHHHHHCCCCCCC
55.4932015554
353SumoylationAFAKLDQKDLVLPTQ
HHHHCCCCCCCCCCC
63.2428112733
354UbiquitinationFAKLDQKDLVLPTQA
HHHCCCCCCCCCCCC
43.8022817900
359PhosphorylationQKDLVLPTQALPASP
CCCCCCCCCCCCCCH
1.3223927012
365 (in isoform 3)Phosphorylation-52.8823822953
365PhosphorylationPTQALPASPALKNKR
CCCCCCCCHHHCCCC
52.8829255136
366UbiquitinationTQALPASPALKNKRP
CCCCCCCHHHCCCCC
59.8222817900
368PhosphorylationALPASPALKNKRPRK
CCCCCHHHCCCCCCC
29.3417525332
369UbiquitinationLPASPALKNKRPRKD
CCCCHHHCCCCCCCC
67.6922817900
369SumoylationLPASPALKNKRPRKD
CCCCHHHCCCCCCCC
67.6928112733
372UbiquitinationSPALKNKRPRKDENE
CHHHCCCCCCCCCCC
42.3723503661
375UbiquitinationLKNKRPRKDENESSA
HCCCCCCCCCCCCCC
36.8924816145
375SumoylationLKNKRPRKDENESSA
HCCCCCCCCCCCCCC
36.8928112733
378UbiquitinationKRPRKDENESSAPAD
CCCCCCCCCCCCCCC
38.4024816145
379PhosphorylationRPRKDENESSAPADG
CCCCCCCCCCCCCCC
38.1418669648
380PhosphorylationPRKDENESSAPADGE
CCCCCCCCCCCCCCC
30.8517525332
380 (in isoform 3)Phosphorylation-30.85-
390UbiquitinationPADGEGGSELQPKNK
CCCCCCCCCCCCCCC
50.9421906983
402UbiquitinationKNKRMTISRLVLEED
CCCCCEEEEEEEECC
81.892190698
410 (in isoform 3)Phosphorylation-49.69-
410PhosphorylationRLVLEEDSQSTEPSA
EEEEECCCCCCCCCC
49.6923401153
412PhosphorylationVLEEDSQSTEPSAGL
EEECCCCCCCCCCCC
38.7630108239
413 (in isoform 3)Phosphorylation-24.86-
413PhosphorylationLEEDSQSTEPSAGLN
EECCCCCCCCCCCCC
24.8630108239
416PhosphorylationDSQSTEPSAGLNSSQ
CCCCCCCCCCCCCCH
30.1130108239
421PhosphorylationEPSAGLNSSQEAASA
CCCCCCCCCHHHHHC
51.7030108239
422 (in isoform 3)Phosphorylation-45.97-
422PhosphorylationPSAGLNSSQEAASAP
CCCCCCCCHHHHHCC
45.9717525332
427 (in isoform 3)Phosphorylation-44.3827251275
427PhosphorylationNSSQEAASAPPSKPT
CCCHHHHHCCCCCCC
44.3820068231
431PhosphorylationEAASAPPSKPTVLNQ
HHHHCCCCCCCCCCC
38.7529449344
432 (in isoform 3)Ubiquitination-3.07-
432UbiquitinationAASAPPSKPTVLNQP
HHHCCCCCCCCCCCC
3.0722817900
434PhosphorylationSAPPSKPTVLNQPLP
HCCCCCCCCCCCCCC
23.3128122231
435UbiquitinationAPPSKPTVLNQPLPG
CCCCCCCCCCCCCCC
8.5922817900
444 (in isoform 3)Ubiquitination-5.85-
444UbiquitinationNQPLPGEKNPKVPKG
CCCCCCCCCCCCCCC
5.8522817900
446AcetylationPLPGEKNPKVPKGKW
CCCCCCCCCCCCCCC
49.78-
447 (in isoform 3)Acetylation-48.76-
447UbiquitinationLPGEKNPKVPKGKWN
CCCCCCCCCCCCCCC
48.7622817900
447AcetylationLPGEKNPKVPKGKWN
CCCCCCCCCCCCCCC
48.76-
449AcetylationGEKNPKVPKGKWNSS
CCCCCCCCCCCCCCC
54.43-
450UbiquitinationEKNPKVPKGKWNSSN
CCCCCCCCCCCCCCC
11.8122817900
452AcetylationNPKVPKGKWNSSNGV
CCCCCCCCCCCCCCC
8.1525953088
452SumoylationNPKVPKGKWNSSNGV
CCCCCCCCCCCCCCC
8.1528112733
453UbiquitinationPKVPKGKWNSSNGVE
CCCCCCCCCCCCCCC
48.7223503661
456 (in isoform 3)Phosphorylation-60.62-
456PhosphorylationPKGKWNSSNGVEEKE
CCCCCCCCCCCCCCC
60.6228985074
488 (in isoform 3)Acetylation-24.12-
488AcetylationDSTTNITKKQKWTVE
CCCCCCCCCCCEEEC
24.1218197706
489 (in isoform 3)Acetylation-44.44-
489AcetylationSTTNITKKQKWTVEE
CCCCCCCCCCEEECH
44.4418197706
491AcetylationTNITKKQKWTVEESE
CCCCCCCCEEECHHH
15.3818197706
495AcetylationKKQKWTVEESEWVKA
CCCCEEECHHHHHHH
43.81-
530 (in isoform 3)Acetylation--
530AcetylationNRTAVMIKDRWRTMK
CCEEEEHHHHHHHHH
18197706
537AcetylationKDRWRTMKRLGMN--
HHHHHHHHHHCCC--
18197706

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
20SPhosphorylationKinaseCHEK2O96017
GPS
230TPhosphorylationKinaseATMQ13315
Uniprot
365SPhosphorylationKinaseCDK2P24941
PSP
365SPhosphorylationKinaseMAPK1P28482
GPS
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:21057505

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TERF2_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 TERF2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WRN_HUMANWRNphysical
12181313
RAD50_HUMANRAD50physical
15100233
XRCC5_HUMANXRCC5physical
15100233
TE2IP_HUMANTERF2IPphysical
15100233
RAD50_HUMANRAD50physical
10888888
TE2IP_HUMANTERF2IPphysical
10888888
MRE11_HUMANMRE11Aphysical
10888888
NBN_HUMANNBNphysical
10888888
WRN_HUMANWRNphysical
18212065
MRE11_HUMANMRE11Aphysical
18212065
RAD50_HUMANRAD50physical
18212065
ORC1_HUMANORC1physical
18761675
ORC2_HUMANORC2physical
18761675
ORC3_HUMANORC3physical
18761675
ORC6_HUMANORC6physical
18761675
BRCA1_HUMANBRCA1physical
19797051
ANM1_HUMANPRMT1physical
19596784
TE2IP_HUMANTERF2IPphysical
21217703
DCR1B_HUMANDCLRE1Bphysical
21217703
TINF2_HUMANTINF2physical
20811636
ZCCHL_HUMANZC3HAV1Lphysical
20811636
RB15B_HUMANRBM15Bphysical
20811636
POTE1_HUMANPOT1physical
20811636
TPA_HUMANPLATphysical
20811636
IMA1_HUMANKPNA2physical
20811636
TERF1_HUMANTERF1physical
20811636
CHIP_HUMANSTUB1physical
20811636
TYY1_HUMANYY1physical
20811636
RBM33_HUMANRBM33physical
20811636
PABP4_HUMANPABPC4physical
20811636
MCCB_HUMANMCCC2physical
20811636
CSK2B_HUMANCSNK2Bphysical
20811636
BMP2K_HUMANBMP2Kphysical
20811636
CYFP1_HUMANCYFIP1physical
20811636
DDX3X_HUMANDDX3Xphysical
20811636
SF3B4_HUMANSF3B4physical
20811636
S10A8_HUMANS100A8physical
20811636
HSP74_HUMANHSPA4physical
20811636
ACTN1_HUMANACTN1physical
20811636
MCM7_HUMANMCM7physical
20811636
DDB1_HUMANDDB1physical
20811636
PRDX4_HUMANPRDX4physical
20811636
RGF1C_HUMANRASGEF1Cphysical
20811636
CDK9_HUMANCDK9physical
20811636
FBX21_HUMANFBXO21physical
20811636
BI2L1_HUMANBAIAP2L1physical
20811636
CHD8_HUMANCHD8physical
20811636
TOX4_HUMANTOX4physical
20811636
CLK3_HUMANCLK3physical
20811636
SC16A_HUMANSEC16Aphysical
20811636
DJB11_HUMANDNAJB11physical
20811636
TLN1_HUMANTLN1physical
20811636
MYO10_HUMANMYO10physical
20811636
ABCD1_HUMANABCD1physical
20811636
S10A7_HUMANS100A7physical
20811636
IMB1_HUMANKPNB1physical
20811636
USP9X_HUMANUSP9Xphysical
20811636
CSK22_HUMANCSNK2A2physical
20811636
PLOD2_HUMANPLOD2physical
20811636
RING1_HUMANRING1physical
20811636
ZN281_HUMANZNF281physical
20811636
FOXJ3_HUMANFOXJ3physical
20811636
LARP7_HUMANLARP7physical
20811636
IRS4_HUMANIRS4physical
20811636
S30BP_HUMANSAP30BPphysical
20811636
DYST_HUMANDSTphysical
20811636
UGDH_HUMANUGDHphysical
20811636
ERH_HUMANERHphysical
20811636
PREP_HUMANPITRM1physical
20811636
MYH10_HUMANMYH10physical
20811636
AT2B1_HUMANATP2B1physical
20811636
AT2B3_HUMANATP2B3physical
20811636
CARM1_HUMANCARM1physical
20811636
SLTM_HUMANSLTMphysical
20811636
NT5D2_HUMANNT5DC2physical
20811636
TR150_HUMANTHRAP3physical
20811636
CALD1_HUMANCALD1physical
20811636
XRCC5_HUMANXRCC5physical
20811636
ENPL_HUMANHSP90B1physical
20811636
ACLY_HUMANACLYphysical
20811636
PRPS3_HUMANPRPS1L1physical
20811636
IDH3A_HUMANIDH3Aphysical
20811636
HS105_HUMANHSPH1physical
20811636
MACD2_HUMANMACROD2physical
20811636
BAG3_HUMANBAG3physical
20811636
TNKS1_HUMANTNKSphysical
20811636
CCNT1_HUMANCCNT1physical
20811636
MYH9_HUMANMYH9physical
20811636
TBPL1_HUMANTBPL1physical
20811636
RS8_HUMANRPS8physical
20811636
KCD15_HUMANKCTD15physical
20811636
PLOD1_HUMANPLOD1physical
20811636
TBX1_HUMANTBX1physical
20811636
RSBNL_HUMANRSBN1Lphysical
20811636
TRPC5_HUMANTRPC5physical
20811636
T2AG_HUMANGTF2A2physical
20811636
DPOD1_HUMANPOLD1physical
20811636
SYNE1_HUMANSYNE1physical
20811636
PDIP3_HUMANPOLDIP3physical
20811636
RS6_HUMANRPS6physical
20811636
AP2A2_HUMANAP2A2physical
20811636
ZN703_HUMANZNF703physical
20811636
G3BP2_HUMANG3BP2physical
20811636
SC24B_HUMANSEC24Bphysical
20811636
CCNT2_HUMANCCNT2physical
20811636
OSB11_HUMANOSBPL11physical
20811636
SK2L2_HUMANSKIV2L2physical
20811636
ZGPAT_HUMANZGPATphysical
20811636
CHD7_HUMANCHD7physical
20811636
VIR_HUMANKIAA1429physical
20811636
MACF1_HUMANMACF1physical
20811636
SMC3_HUMANSMC3physical
20811636
CT027_HUMANC20orf27physical
20811636
PIMT_HUMANPCMT1physical
20811636
GANAB_HUMANGANABphysical
20811636
ANM5_HUMANPRMT5physical
20811636
NEXMI_HUMANKIAA2022physical
20811636
TDRD6_HUMANTDRD6physical
20811636
SYNE2_HUMANSYNE2physical
20811636
CENPF_HUMANCENPFphysical
20811636
TAF2_HUMANTAF2physical
20811636
RYR2_HUMANRYR2physical
20811636
ATN1_HUMANATN1physical
20811636
CDC37_HUMANCDC37physical
20811636
CDK13_HUMANCDK13physical
20811636
BRE1B_HUMANRNF40physical
20811636
UTRO_HUMANUTRNphysical
20811636
DMD_HUMANDMDphysical
20811636
RGPA1_HUMANRALGAPA1physical
20811636
DNJA2_HUMANDNAJA2physical
20811636
TF2AA_HUMANGTF2A1physical
20811636
DHX33_HUMANDHX33physical
20811636
KI13B_HUMANKIF13Bphysical
20811636
RHG20_HUMANARHGAP20physical
20811636
GANP_HUMANMCM3APphysical
20811636
RAVR1_HUMANRAVER1physical
20811636
EDC3_HUMANEDC3physical
20811636
U2AF2_HUMANU2AF2physical
20811636
PRDX3_HUMANPRDX3physical
20811636
IVD_HUMANIVDphysical
20811636
RTL6_HUMANLDOC1Lphysical
20811636
ARMC6_HUMANARMC6physical
20811636
SRS11_HUMANSRSF11physical
20811636
RU17_HUMANSNRNP70physical
20811636
MARK3_HUMANMARK3physical
20811636
PFKAL_HUMANPFKLphysical
20811636
CLASR_HUMANCLASRPphysical
20811636
DKC1_HUMANDKC1physical
20811636
FXR2_HUMANFXR2physical
20811636
SYDM_HUMANDARS2physical
20811636
SDF2L_HUMANSDF2L1physical
20811636
TBC15_HUMANTBC1D15physical
20811636
CLPB_HUMANCLPBphysical
20811636
UBP15_HUMANUSP15physical
20811636
PAXB1_HUMANPAXBP1physical
20811636
HS74L_HUMANHSPA4Lphysical
20811636
REPI1_HUMANREPIN1physical
20811636
DHX40_HUMANDHX40physical
20811636
L2GL1_HUMANLLGL1physical
20811636
MYOM2_HUMANMYOM2physical
20811636
BRD2_HUMANBRD2physical
20811636
MARF1_HUMANKIAA0430physical
20811636
ZC3HD_HUMANZC3H13physical
20811636
NFRKB_HUMANNFRKBphysical
20811636
DHX37_HUMANDHX37physical
20811636
REV3L_HUMANREV3Lphysical
20811636
SRRM2_HUMANSRRM2physical
20811636
MECP2_HUMANMECP2physical
20811636
TCOF_HUMANTCOF1physical
20811636
P5CR2_HUMANPYCR2physical
20811636
NDKM_HUMANNME4physical
20811636
DUS11_HUMANDUSP11physical
20811636
BCKD_HUMANBCKDKphysical
20811636
TRI47_HUMANTRIM47physical
20811636
SNX22_HUMANSNX22physical
20811636
WDR5_HUMANWDR5physical
20811636
SELB_HUMANEEFSECphysical
20811636
AASS_HUMANAASSphysical
20811636
GPTC8_HUMANGPATCH8physical
20811636
OSBL9_HUMANOSBPL9physical
20811636
ZKSC4_HUMANZKSCAN4physical
20811636
TFP11_HUMANTFIP11physical
20811636
CYLC2_HUMANCYLC2physical
20811636
PCBP1_HUMANPCBP1physical
20811636
POTE1_HUMANPOT1physical
15383534
TERF2_HUMANTERF2physical
15383534
TINF2_HUMANTINF2physical
15383534
SIAH1_HUMANSIAH1physical
21057505
TINF2_HUMANTINF2physical
15316005
TE2IP_HUMANTERF2IPphysical
21044950
HMGN1_HUMANHMGN1physical
21044950
R113A_HUMANRNF113Aphysical
21044950
NUCL_HUMANNCLphysical
21044950
RPR1B_HUMANRPRD1Bphysical
21044950
HMGN2_HUMANHMGN2physical
21044950
RL13_HUMANRPL13physical
21044950
H2AX_HUMANH2AFXphysical
21044950
CC137_HUMANCCDC137physical
21044950
ASSY_HUMANASS1physical
21044950
WDR4_HUMANWDR4physical
21044950
LYAR_HUMANLYARphysical
21044950
DDX21_HUMANDDX21physical
21044950
HDGR2_HUMANHDGFRP2physical
21044950
ZCH18_HUMANZC3H18physical
21044950
HEXI1_HUMANHEXIM1physical
21044950
HEXI2_HUMANHEXIM2physical
21044950
SRSF6_HUMANSRSF6physical
21044950
NASP_HUMANNASPphysical
21044950
XRCC6_HUMANXRCC6physical
21044950
HMGB1_HUMANHMGB1physical
21044950
NAIF1_HUMANNAIF1physical
21044950
CTBP1_HUMANCTBP1physical
21044950
TERF2_HUMANTERF2physical
21044950
LANC2_HUMANLANCL2physical
21044950
MGN2_HUMANMAGOHBphysical
21044950
BANP_HUMANBANPphysical
21044950
TOIP1_HUMANTOR1AIP1physical
21044950
SET_HUMANSETphysical
21044950
PTMA_HUMANPTMAphysical
21044950
TALDO_HUMANTALDO1physical
21044950
APEX1_HUMANAPEX1physical
21044950
DDX24_HUMANDDX24physical
21044950
OCM2_HUMANOCM2physical
21044950
PPM1G_HUMANPPM1Gphysical
21044950
HMGN4_HUMANHMGN4physical
21044950
SP100_HUMANSP100physical
21044950
NUMA1_HUMANNUMA1physical
21044950
HMGN3_HUMANHMGN3physical
21044950
DX39A_HUMANDDX39Aphysical
21044950
ANXA5_HUMANANXA5physical
21044950
TYB10_HUMANTMSB10physical
21044950
NXNL1_HUMANNXNL1physical
21044950
AF1L2_HUMANAFAP1L2physical
21044950
GNMT_HUMANGNMTphysical
21044950
TINF2_HUMANTINF2physical
21044950
REST_HUMANRESTphysical
18818083
TEP1_HUMANTEP1physical
19329795
BLM_HUMANBLMphysical
19329795
HS90A_HUMANHSP90AA1physical
19329795
TOP2A_HUMANTOP2Aphysical
19329795
SF3B2_HUMANSF3B2physical
19329795
DCR1B_HUMANDCLRE1Bphysical
16730175
SLX4_HUMANSLX4physical
23994477
SLX4_HUMANSLX4physical
24012755
EP300_HUMANEP300physical
23307557
TINF2_HUMANTINF2physical
23307557
CHAP1_HUMANCHAMP1physical
26344197
TE2IP_HUMANTERF2IPphysical
26344197
TE2IP_HUMANTERF2IPphysical
26450775
PIAS1_HUMANPIAS1physical
26450775
RNF4_HUMANRNF4physical
26450775
TE2IP_HUMANTERF2IPphysical
23086976
TE2IP_HUMANTERF2IPphysical
27214791
TERF2_HUMANTERF2physical
24895130
UCHL1_HUMANUCHL1physical
29126443
TE2IP_HUMANTERF2IPphysical
29126443

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 TERF2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"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 SER-323, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368 AND SER-380, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.

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