IFT81_HUMAN - dbPTM
IFT81_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFT81_HUMAN
UniProt AC Q8WYA0
Protein Name Intraflagellar transport protein 81 homolog
Gene Name IFT81
Organism Homo sapiens (Human).
Sequence Length 676
Subcellular Localization Cell projection, cilium .
Protein Description Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis..
Protein Sequence MSDQIKFIMDSLNKEPFRKNYNLITFDSLEPMQLLQVLSDVLAEIDPKQLVDIREEMPEQTAKRMLSLLGILKYKPSGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRTNELKKRAYLARFLIKLEVPSEFLQDETVADTNKQYEELMEAFKTLHKEYEQLKISGFSTAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQWMLKIARQLRVEKEREEYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAAADAKPESLMKRLEEEIKFNLYMVTEKFPKELENKKKELHFLQKVVSEPAMGHSDLLELESKINEINTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQEAKEKLASLEREASVKRNQTREFDGTEVLKGDEFKRYVNKLRSKSTVFKKKHQIIAELKAEFGLLQRTEELLKQRHENIQQQLQTMEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLYSLVSEKKSALASVIKELRQLRQKYQELTQECDEKKSQYDSCAAGLESNRSKLEQEVRRLREECLQEESRYHYTNCMIKNLEVQLRRATDEMKAYISSDQQEKRKAIREQYTKNTAEQENLGKKLREKQKVIRESHGPNMKQAKMWRDLEQLMECKKQCFLKQQSQTSIGQVIQEGGEDRLIL
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------MSDQIKFIM
------CCHHHHHHH		37.9222814378
2Phosphorylation------MSDQIKFIM
------CCHHHHHHH		37.9221406692
14UbiquitinationFIMDSLNKEPFRKNY
HHHHHCCCCCCCCCC		72.55-
61 (in isoform 3)Phosphorylation-32.27-
61PhosphorylationREEMPEQTAKRMLSL
HHHCCHHHHHHHHHH		32.2719664994
73SumoylationLSLLGILKYKPSGNA
HHHHHHHHCCCCCCC		49.67-
75UbiquitinationLLGILKYKPSGNATD
HHHHHHCCCCCCCCC		30.99-
75SumoylationLLGILKYKPSGNATD
HHHHHHCCCCCCCCC		30.99-
144PhosphorylationVADTNKQYEELMEAF
CCCCHHHHHHHHHHH		17.0029496907
152UbiquitinationEELMEAFKTLHKEYE
HHHHHHHHHHHHHHH		58.17-
156UbiquitinationEAFKTLHKEYEQLKI
HHHHHHHHHHHHHHC		66.17-
158PhosphorylationFKTLHKEYEQLKISG
HHHHHHHHHHHHCCC		17.49-
182UbiquitinationISAMEEEKDQLIKRV
HHHCHHHHHHHHHHH		54.80-
187UbiquitinationEEKDQLIKRVEHLKK
HHHHHHHHHHHHHHH		60.01-
216UbiquitinationARQLRVEKEREEYLA
HHHHHHHHHHHHHHH		60.25-
226UbiquitinationEEYLAQQKQEQKNQL
HHHHHHHHHHHHHHH		43.66-
230UbiquitinationAQQKQEQKNQLFHAV
HHHHHHHHHHHHHHH		46.00-
248UbiquitinationQRVQNQLKSMRQAAA
HHHHHHHHHHHHHHH		32.23-
249PhosphorylationRVQNQLKSMRQAAAD
HHHHHHHHHHHHHHH		27.99-
261PhosphorylationAADAKPESLMKRLEE
HHHCCHHHHHHHHHH		42.14-
264UbiquitinationAKPESLMKRLEEEIK
CCHHHHHHHHHHHHH		60.15-
290 (in isoform 3)Acetylation-68.09-
290AcetylationKELENKKKELHFLQK
HHHHHHHHHHHHHHH		68.0919608861
297UbiquitinationKELHFLQKVVSEPAM
HHHHHHHHHHCCCCC		46.91-
329UbiquitinationEINQLIEKKMMRNEP
HHHHHHHHHHHCCCC		38.69-
330UbiquitinationINQLIEKKMMRNEPI
HHHHHHHHHHCCCCC		25.74-
333MethylationLIEKKMMRNEPIEGK
HHHHHHHCCCCCCCH		40.6412019789
340UbiquitinationRNEPIEGKLSLYRQQ
CCCCCCCHHHHHHHH		23.32-
342 (in isoform 3)Phosphorylation-27.17-
342PhosphorylationEPIEGKLSLYRQQAS
CCCCCHHHHHHHHHH		27.1718767875
345MethylationEGKLSLYRQQASIIS
CCHHHHHHHHHHHHH		27.6812019799
349PhosphorylationSLYRQQASIISRKKE
HHHHHHHHHHHHHHH		19.0024719451
352PhosphorylationRQQASIISRKKEAKA
HHHHHHHHHHHHHHH		36.0624719451
371PhosphorylationEAKEKLASLEREASV
HHHHHHHHHHHHHHH		41.0025849741
377PhosphorylationASLEREASVKRNQTR
HHHHHHHHHCCCCCC		24.3429514088
383PhosphorylationASVKRNQTREFDGTE
HHHCCCCCCCCCCCE		35.40-
393UbiquitinationFDGTEVLKGDEFKRY
CCCCEEECHHHHHHH		70.28-
398UbiquitinationVLKGDEFKRYVNKLR
EECHHHHHHHHHHHH		40.55-
400PhosphorylationKGDEFKRYVNKLRSK
CHHHHHHHHHHHHCC		14.68-
414UbiquitinationKSTVFKKKHQIIAEL
CCHHHHHHHHHHHHH		41.13-
436UbiquitinationQRTEELLKQRHENIQ
HHHHHHHHHHHHHHH		58.89-
453UbiquitinationLQTMEEKKGISGYSY
HHHHHHHCCCCCCCC		65.83-
472UbiquitinationLERVSALKSEVDEMK
HHHHHHHHHHHHHHC		44.26-
4792-HydroxyisobutyrylationKSEVDEMKGRTLDDM
HHHHHHHCCCCHHHH		43.10-
479UbiquitinationKSEVDEMKGRTLDDM
HHHHHHHCCCCHHHH		43.10-
492UbiquitinationDMSEMVKKLYSLVSE
HHHHHHHHHHHHHHH		41.04-
5002-HydroxyisobutyrylationLYSLVSEKKSALASV
HHHHHHHHHHHHHHH		44.51-
500UbiquitinationLYSLVSEKKSALASV
HHHHHHHHHHHHHHH		44.51-
501UbiquitinationYSLVSEKKSALASVI
HHHHHHHHHHHHHHH		36.59-
509UbiquitinationSALASVIKELRQLRQ
HHHHHHHHHHHHHHH		48.84-
529UbiquitinationTQECDEKKSQYDSCA
HHHHHHHHHHHHHHH		40.52-
532PhosphorylationCDEKKSQYDSCAAGL
HHHHHHHHHHHHHHH		19.5429759185
544PhosphorylationAGLESNRSKLEQEVR
HHHHHHHHHHHHHHH		45.9329457462
545UbiquitinationGLESNRSKLEQEVRR
HHHHHHHHHHHHHHH		53.45-
586UbiquitinationRRATDEMKAYISSDQ
HHCCHHHHHHHCCCH		35.67-
588PhosphorylationATDEMKAYISSDQQE
CCHHHHHHHCCCHHH		8.87-
596UbiquitinationISSDQQEKRKAIREQ
HCCCHHHHHHHHHHH		55.66-
596AcetylationISSDQQEKRKAIREQ
HCCCHHHHHHHHHHH		55.6619810283
5962-HydroxyisobutyrylationISSDQQEKRKAIREQ
HCCCHHHHHHHHHHH		55.66-
598UbiquitinationSDQQEKRKAIREQYT
CCHHHHHHHHHHHHH		60.27-
604PhosphorylationRKAIREQYTKNTAEQ
HHHHHHHHHHHHHHH		18.2227067055
605PhosphorylationKAIREQYTKNTAEQE
HHHHHHHHHHHHHHH		19.9427067055
606UbiquitinationAIREQYTKNTAEQEN
HHHHHHHHHHHHHHH		47.57-
628PhosphorylationKQKVIRESHGPNMKQ
HHHHHHHHHCCCHHH		24.7224670416
649UbiquitinationLEQLMECKKQCFLKQ
HHHHHHHHHHHHHHC		32.35-
650UbiquitinationEQLMECKKQCFLKQQ
HHHHHHHHHHHHHCC		65.05-
658PhosphorylationQCFLKQQSQTSIGQV
HHHHHCCCCCCHHHH		32.6929978859
660PhosphorylationFLKQQSQTSIGQVIQ
HHHCCCCCCHHHHHH		27.7921815630
661PhosphorylationLKQQSQTSIGQVIQE
HHCCCCCCHHHHHHC		19.6529978859
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 IFT81_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFT81_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 IFT81_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
IFT88_HUMANIFT88physical
22939629
IFT46_HUMANIFT46physical
26186194
PRAME_HUMANPRAMEphysical
26186194
IFT74_HUMANIFT74physical
26186194
SPA5L_HUMANSPATA5L1physical
26186194
NDC80_HUMANNDC80physical
26186194
CEP44_HUMANCEP44physical
26186194
PCM1_HUMANPCM1physical
26186194
UBX10_HUMANUBXN10physical
26389662
IFT74_HUMANIFT74physical
28514442
PRAME_HUMANPRAMEphysical
28514442
NDC80_HUMANNDC80physical
28514442
IFT46_HUMANIFT46physical
28514442
CEP44_HUMANCEP44physical
28514442
PCM1_HUMANPCM1physical
28514442
SPA5L_HUMANSPATA5L1physical
28514442
IFT74_HUMANIFT74physical
27173435
IFT25_HUMANHSPB11physical
27173435
IFT88_HUMANIFT88physical
27173435
IFT46_HUMANIFT46physical
27173435
IFT52_HUMANIFT52physical
27173435
IFT27_HUMANIFT27physical
27173435
TT30B_HUMANTTC30Bphysical
27173435
TT30A_HUMANTTC30Aphysical
27173435
IFT22_HUMANIFT22physical
27173435
IF172_HUMANIFT172physical
27173435
IFT56_HUMANTTC26physical
27173435
CC28B_HUMANCCDC28Bphysical
27173435
IFT20_HUMANIFT20physical
27173435
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 IFT81_HUMAN

loading...

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-290, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory