AP18B_YEAST - dbPTM
AP18B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP18B_YEAST
UniProt AC P53309
Protein Name Clathrin coat assembly protein AP180B
Gene Name YAP1802
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 568
Subcellular Localization Bud . Bud neck . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm .
Protein Description Involved in endocytosis and clathrin cage assembly..
Protein Sequence MSSLYTKLVKGATKIKMAPPKQKYVDPILSGTSSARGLQEITHALDIRLSDTAWTIVYKALIVLHLMIQQGEKDVTLRHYSHNLDVFQLRKISHTTKWSSNDMRALQRYDEYLKTRCEEYGRLGMDHLRDNYSSLKLGSKNQLSMDEELDHVESLEIQINALIRNKYSVSDLENHLLLYAFQLLVQDLLGLYNALNEGVITLLESFFELSIEHAKRTLDLYKDFVDMTEYVVRYLKIGKAVGLKIPVIKHITTKLINSLEEHLREETKRQRGEPSEPQQDRKPSTAISSTSSHNNNSNDKNKSIAQKKLEQIREQKRLLEQQLQNQQLLISPTVPQDAYNPFGSQQQDLNNDTFSFEPTQPQMTAQVPQPTANPFLIPQQQQQALQLTSASTMPQPSEIQITPNLNNQQTGMYASNLQYTPNFTGSGFGGYTTTENNAIMTGTLDPTKTGSNNPFSLENIAREQQQQNFQNSPNPFTLQQAQTTPILAHSQTGNPFQAQNVVTSPMGTYMTNPVAGQLQYASTGAQQQPQMMQGQQTGYVMVPTAFVPINQQQQQQQHQQENPNLIDI
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-----MSSLYTKLVK
-----CCHHHHHHHH		24.8930377154
6Phosphorylation--MSSLYTKLVKGAT
--CCHHHHHHHHCCC		24.1630377154
23AcetylationKMAPPKQKYVDPILS
CCCCCCHHCCCCHHC		54.0624489116
132PhosphorylationMDHLRDNYSSLKLGS
HHHHHHHCHHHCCCC		12.1528889911
133PhosphorylationDHLRDNYSSLKLGSK
HHHHHHCHHHCCCCC		35.1327214570
136UbiquitinationRDNYSSLKLGSKNQL
HHHCHHHCCCCCCCC		53.3923749301
140UbiquitinationSSLKLGSKNQLSMDE
HHHCCCCCCCCCCCH		47.0922817900
221PhosphorylationAKRTLDLYKDFVDMT
HHHHHHHHHHHHHHH		14.2619779198
268UbiquitinationEHLREETKRQRGEPS
HHHHHHHHHHCCCCC		50.2224961812
275PhosphorylationKRQRGEPSEPQQDRK
HHHCCCCCCCCCCCC		58.5724961812
282UbiquitinationSEPQQDRKPSTAISS
CCCCCCCCCCCCCCC		52.1623749301
284PhosphorylationPQQDRKPSTAISSTS
CCCCCCCCCCCCCCC		33.2428889911
285PhosphorylationQQDRKPSTAISSTSS
CCCCCCCCCCCCCCC		36.2224961812
288PhosphorylationRKPSTAISSTSSHNN
CCCCCCCCCCCCCCC		25.7123749301
289PhosphorylationKPSTAISSTSSHNNN
CCCCCCCCCCCCCCC		26.6219779198
290PhosphorylationPSTAISSTSSHNNNS
CCCCCCCCCCCCCCC		27.7123749301
291PhosphorylationSTAISSTSSHNNNSN
CCCCCCCCCCCCCCC		31.3923749301
292PhosphorylationTAISSTSSHNNNSND
CCCCCCCCCCCCCCH		30.2628889911
297PhosphorylationTSSHNNNSNDKNKSI
CCCCCCCCCHHCHHH		48.8323749301
300UbiquitinationHNNNSNDKNKSIAQK
CCCCCCHHCHHHHHH		71.2123749301
302UbiquitinationNNSNDKNKSIAQKKL
CCCCHHCHHHHHHHH		49.3222817900
307UbiquitinationKNKSIAQKKLEQIRE
HCHHHHHHHHHHHHH		50.7522817900
449PhosphorylationGTLDPTKTGSNNPFS
EECCCCCCCCCCCCC		48.6022890988
451PhosphorylationLDPTKTGSNNPFSLE
CCCCCCCCCCCCCHH		38.3722890988
456PhosphorylationTGSNNPFSLENIARE
CCCCCCCCHHHHHHH		35.7122890988
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 AP18B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP18B_YEAST !!
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 AP18B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLA2_YEASTSLA2genetic
14704157
END3_YEASTEND3physical
19591838
MVB12_YEASTMVB12genetic
20526336
ATG14_YEASTATG14physical
22875988
YET3_YEASTYET3physical
22875988
YAP6_YEASTYAP6physical
22875988
MAD1_YEASTMAD1physical
22875988
NNF2_YEASTNNF2physical
22875988
VPS53_YEASTVPS53physical
22875988
PFD1_YEASTPFD1physical
22875988
NNF1_YEASTNNF1physical
22875988
MRP8_YEASTMRP8physical
22875988
DYHC_YEASTDYN1physical
22875988
ENT2_YEASTENT2physical
22875988
RCF1_YEASTRCF1physical
22875988
NU188_YEASTNUP188physical
22875988
PDS5_YEASTPDS5physical
22875988
END3_YEASTEND3physical
22875988
NUF2_YEASTNUF2physical
22875988
YO223_YEASTDSC3physical
22875988
PRS10_YEASTRPT4physical
22875988
NCA2_YEASTNCA2physical
22875988
CLH_YEASTCHC1physical
9531549
CLC1_YEASTCLC1physical
9531549
SEC4_YEASTSEC4genetic
23897890
TRS20_YEASTTRS20genetic
27708008
CDC10_YEASTCDC10genetic
27708008
CDC53_YEASTCDC53genetic
27708008
GPI8_YEASTGPI8genetic
27708008
RRN7_YEASTRRN7genetic
27708008
KTHY_YEASTCDC8genetic
27708008
DCP2_YEASTDCP2genetic
27708008
ORC4_YEASTORC4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP18B_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.

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