TTL12_HUMAN - dbPTM
TTL12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTL12_HUMAN
UniProt AC Q14166
Protein Name Tubulin--tyrosine ligase-like protein 12
Gene Name TTLL12
Organism Homo sapiens (Human).
Sequence Length 644
Subcellular Localization
Protein Description
Protein Sequence MEAERGPERRPAERSSPGQTPEEGAQALAEFAALHGPALRASGVPERYWGRLLHKLEHEVFDAGEVFGIMQVEEVEEEEDEAAREVRKQQPNPGNELCYKVIVTRESGLQAAHPNSIFLIDHAWTCRVEHARQQLQQVPGLLHRMANLMGIEFHGELPSTEAVALVLEEMWKFNQTYQLAHGTAEEKMPVWYIMDEFGSRIQHADVPSFATAPFFYMPQQVAYTLLWPLRDLDTGEEVTRDFAYGETDPLIRKCMLLPWAPTDMLDLSSCTPEPPAEHYQAILEENKEKLPLDINPVVHPHGHIFKVYTDVQQVASSLTHPRFTLTQSEADADILFNFSHFKDYRKLSQERPGVLLNQFPCENLLTVKDCLASIARRAGGPEGPPWLPRTFNLRTELPQFVSYFQQRERWGEDNHWICKPWNLARSLDTHVTKSLHSIIRHRESTPKVVSKYIESPVLFLREDVGKVKFDIRYIVLLRSVRPLRLFVYDVFWLRFSNRAFALNDLDDYEKHFTVMNYDPDVVLKQVHCEEFIPEFEKQYPEFPWTDVQAEIFRAFTELFQVACAKPPPLGLCDYPSSRAMYAVDLMLKWDNGPDGRRVMQPQILEVNFNPDCERACRYHPTFFNDVFSTLFLDQPGGCHVTCLV
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
15PhosphorylationERRPAERSSPGQTPE
CCCCCCCCCCCCCHH		32.1822167270
16PhosphorylationRRPAERSSPGQTPEE
CCCCCCCCCCCCHHH		38.9922167270
20PhosphorylationERSSPGQTPEEGAQA
CCCCCCCCHHHHHHH		38.2922167270
42PhosphorylationHGPALRASGVPERYW
HCHHHHHCCCCHHHH		33.6127251275
88UbiquitinationEAAREVRKQQPNPGN
HHHHHHHHHCCCCCC		59.4621890473
100UbiquitinationPGNELCYKVIVTRES
CCCCCEEEEEEECCC		25.21-
177PhosphorylationMWKFNQTYQLAHGTA
HHHHCCHHHCCCCCC		7.5527642862
187UbiquitinationAHGTAEEKMPVWYIM
CCCCCCHHCCEEEEE		39.75-
244PhosphorylationEVTRDFAYGETDPLI
CCCCHHHCCCCCHHH		18.5828152594
247PhosphorylationRDFAYGETDPLIRKC
CHHHCCCCCHHHHHH		38.2620860994
253UbiquitinationETDPLIRKCMLLPWA
CCCHHHHHHCCCCCC		19.59-
279PhosphorylationPEPPAEHYQAILEEN
CCCCHHHHHHHHHHC		7.3727642862
289UbiquitinationILEENKEKLPLDINP
HHHHCHHHCCCCCCC		57.95-
308PhosphorylationHGHIFKVYTDVQQVA
CCCEEEEECCHHHHH		9.6028152594
309PhosphorylationGHIFKVYTDVQQVAS
CCEEEEECCHHHHHH		32.4528152594
317PhosphorylationDVQQVASSLTHPRFT
CHHHHHHHCCCCCEE		27.7827067055
319PhosphorylationQQVASSLTHPRFTLT
HHHHHHCCCCCEEEE		31.6124719451
342UbiquitinationLFNFSHFKDYRKLSQ
EEECHHHHHHHHHHH		48.72-
346SumoylationSHFKDYRKLSQERPG
HHHHHHHHHHHCCCC		46.38-
346UbiquitinationSHFKDYRKLSQERPG
HHHHHHHHHHHCCCC		46.38-
346SumoylationSHFKDYRKLSQERPG
HHHHHHHHHHHCCCC		46.38-
348PhosphorylationFKDYRKLSQERPGVL
HHHHHHHHHCCCCEE		32.7928450419
361S-nitrosocysteineVLLNQFPCENLLTVK
EECCCCCCCCCCCHH		5.98-
361S-nitrosylationVLLNQFPCENLLTVK
EECCCCCCCCCCCHH		5.9819483679
368UbiquitinationCENLLTVKDCLASIA
CCCCCCHHHHHHHHH		37.17-
373PhosphorylationTVKDCLASIARRAGG
CHHHHHHHHHHHHCC		12.1130108239
395PhosphorylationPRTFNLRTELPQFVS
CCCCCCCCCHHHHHH		45.0720068231
402PhosphorylationTELPQFVSYFQQRER
CCHHHHHHHHHHHHH		22.8628152594
403PhosphorylationELPQFVSYFQQRERW
CHHHHHHHHHHHHHH		10.4928152594
419UbiquitinationEDNHWICKPWNLARS
CCCCCCCCHHHHHHH		43.89-
426PhosphorylationKPWNLARSLDTHVTK
CHHHHHHHHCHHHHH		25.6230108239
429PhosphorylationNLARSLDTHVTKSLH
HHHHHHCHHHHHHHH		24.4420873877
432PhosphorylationRSLDTHVTKSLHSII
HHHCHHHHHHHHHHH		13.8120873877
433UbiquitinationSLDTHVTKSLHSIIR
HHCHHHHHHHHHHHH		50.3521906983
433AcetylationSLDTHVTKSLHSIIR
HHCHHHHHHHHHHHH		50.3526051181
434PhosphorylationLDTHVTKSLHSIIRH
HCHHHHHHHHHHHHC		23.1920873877
437PhosphorylationHVTKSLHSIIRHRES
HHHHHHHHHHHCCCC		25.6320873877
447UbiquitinationRHRESTPKVVSKYIE
HCCCCCHHHHHHHHC		56.19-
451UbiquitinationSTPKVVSKYIESPVL
CCHHHHHHHHCCCEE		38.3421906983
452PhosphorylationTPKVVSKYIESPVLF
CHHHHHHHHCCCEEE		11.47-
455PhosphorylationVVSKYIESPVLFLRE
HHHHHHCCCEEEEEC		15.6828857561
508PhosphorylationALNDLDDYEKHFTVM
ECCCHHHHHHHEEEE		26.9228796482
510AcetylationNDLDDYEKHFTVMNY
CCHHHHHHHEEEEEC		37.4821466224
510UbiquitinationNDLDDYEKHFTVMNY
CCHHHHHHHEEEEEC		37.48-
513PhosphorylationDDYEKHFTVMNYDPD
HHHHHHEEEEECCHH		20.68-
517PhosphorylationKHFTVMNYDPDVVLK
HHEEEEECCHHHHEE		15.6821945579
524UbiquitinationYDPDVVLKQVHCEEF
CCHHHHEEEEEHHHH		38.37-
565UbiquitinationLFQVACAKPPPLGLC
HHHHHHCCCCCCCCC		58.92-
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 TTL12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTL12_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
88Ubiquitination95 (7)N ⇒ Srs13058467
  • Molar-incisor hypomineralization
23918034
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2V2_HUMANUBE2V2physical
22939629
UBP34_HUMANUSP34physical
22939629
UBXN7_HUMANUBXN7physical
22939629
UFM1_HUMANUFM1physical
22939629
VATF_HUMANATP6V1Fphysical
22939629
VPS4B_HUMANVPS4Bphysical
22939629
ZYX_HUMANZYXphysical
22939629
UBE2C_HUMANUBE2Cphysical
22939629
UNK_HUMANUNKphysical
22939629
USP9X_HUMANUSP9Xphysical
22939629
ZRAB2_HUMANZRANB2physical
22939629
UBE2B_HUMANUBE2Bphysical
22939629
UBE2A_HUMANUBE2Aphysical
22939629
UB2D1_HUMANUBE2D1physical
22939629
ARP2_HUMANACTR2physical
22863883
ARP3_HUMANACTR3physical
22863883
ARPC4_HUMANARPC4physical
22863883
IPO11_HUMANIPO11physical
22863883
NSUN2_HUMANNSUN2physical
22863883
PPME1_HUMANPPME1physical
22863883
RPR1A_HUMANRPRD1Aphysical
22863883
PFD3_HUMANVBP1physical
22863883
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 TTL12_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 SER-15 AND SER-16, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-20, AND MASSSPECTROMETRY.

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