MAP11_HUMAN - dbPTM
MAP11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAP11_HUMAN
UniProt AC P53582
Protein Name Methionine aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_03174}
Gene Name METAP1
Organism Homo sapiens (Human).
Sequence Length 386
Subcellular Localization Cytoplasm .
Protein Description Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle..
Protein Sequence MAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHGDLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKSGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTDTGCEILTRRLDSARPHFMSQF
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------MAAVETRVC
------CCCCEEEEE
19413330
19AcetylationDGCSSEAKLQCPTCI
CCCCCHHHCCCCCCE
26051181
19UbiquitinationDGCSSEAKLQCPTCI
CCCCCHHHCCCCCCE
32015554
30UbiquitinationPTCIKLGIQGSYFCS
CCCEEEEECCCEEEC
23503661
33PhosphorylationIKLGIQGSYFCSQEC
EEEEECCCEEECHHH
28857561
34PhosphorylationKLGIQGSYFCSQECF
EEEECCCEEECHHHH
22817900
36UbiquitinationGIQGSYFCSQECFKG
EECCCEEECHHHHCC
21963094
42AcetylationFCSQECFKGSWATHK
EECHHHHCCCHHHHH
26051181
49MalonylationKGSWATHKLLHKKAK
CCCHHHHHHHHHHHH
26320211
49UbiquitinationKGSWATHKLLHKKAK
CCCHHHHHHHHHHHH
29967540
88UbiquitinationYRYTGKLRPHYPLMP
CEECCCCCCCCCCCC
23503661
94UbiquitinationLRPHYPLMPTRPVPS
CCCCCCCCCCCCCCC
21963094
98UbiquitinationYPLMPTRPVPSYIQR
CCCCCCCCCCCCCCC
21963094
110UbiquitinationIQRPDYADHPLGMSE
CCCCCCCCCCCCCCH
23503661
116UbiquitinationADHPLGMSESEQALK
CCCCCCCCHHHHHHC
21963094
123UbiquitinationSESEQALKGTSQIKL
CHHHHHHCCCCCEEE
23503661
129UbiquitinationLKGTSQIKLLSSEDI
HCCCCCEEECCHHHH
21906983
132PhosphorylationTSQIKLLSSEDIEGM
CCCEEECCHHHHHHH
27499020
133PhosphorylationSQIKLLSSEDIEGMR
CCEEECCHHHHHHHH
27499020
156UbiquitinationVLDVAAGMIKPGVTT
HHHHHCCCCCCCCCH
21963094
158UbiquitinationDVAAGMIKPGVTTEE
HHHCCCCCCCCCHHH
-
178UbiquitinationHLACIARNCYPSPLN
HHHHHHHCCCCCCCC
21963094
180PhosphorylationACIARNCYPSPLNYY
HHHHHCCCCCCCCCC
28152594
182PhosphorylationIARNCYPSPLNYYNF
HHHCCCCCCCCCCCC
28152594
185UbiquitinationNCYPSPLNYYNFPKS
CCCCCCCCCCCCCHH
22817900
186PhosphorylationCYPSPLNYYNFPKSC
CCCCCCCCCCCCHHH
28152594
187PhosphorylationYPSPLNYYNFPKSCC
CCCCCCCCCCCHHHC
28152594
191UbiquitinationLNYYNFPKSCCTSVN
CCCCCCCHHHCCCCH
21963094
191SumoylationLNYYNFPKSCCTSVN
CCCCCCCHHHCCCCH
-
218UbiquitinationLQEGDIVNVDITLYR
CCCCCEEEEEEEEEE
22817900
220UbiquitinationEGDIVNVDITLYRNG
CCCEEEEEEEEEECC
22817900
234UbiquitinationGYHGDLNETFFVGEV
CCCCCCCCCEEEEEE
22817900
243UbiquitinationFFVGEVDDGARKLVQ
EEEEEECHHHHHHHH
22817900
251PhosphorylationGARKLVQTTYECLMQ
HHHHHHHHHHHHHHH
20068231
252PhosphorylationARKLVQTTYECLMQA
HHHHHHHHHHHHHHH
20068231
253PhosphorylationRKLVQTTYECLMQAI
HHHHHHHHHHHHHHH
20068231
265UbiquitinationQAIDAVKPGVRYREL
HHHHHCCCCCCHHHH
22817900
267UbiquitinationIDAVKPGVRYRELGN
HHHCCCCCCHHHHHH
22817900
269PhosphorylationAVKPGVRYRELGNII
HCCCCCCHHHHHHHH
29496907
269UbiquitinationAVKPGVRYRELGNII
HCCCCCCHHHHHHHH
22817900
276UbiquitinationYRELGNIIQKHAQAN
HHHHHHHHHHHHHHC
22817900
278UbiquitinationELGNIIQKHAQANGF
HHHHHHHHHHHHCCC
21906983
286PhosphorylationHAQANGFSVVRSYCG
HHHHCCCHHHHHHCC
28857561
290PhosphorylationNGFSVVRSYCGHGIH
CCCHHHHHHCCCCHH
28152594
291PhosphorylationGFSVVRSYCGHGIHK
CCHHHHHHCCCCHHH
28152594
298UbiquitinationYCGHGIHKLFHTAPN
HCCCCHHHHHCCCCC
22817900
298AcetylationYCGHGIHKLFHTAPN
HCCCCHHHHHCCCCC
26051181
300UbiquitinationGHGIHKLFHTAPNVP
CCCHHHHHCCCCCCC
22817900
309PhosphorylationTAPNVPHYAKNKAVG
CCCCCCHHHCCCCCE
20068231
311UbiquitinationPNVPHYAKNKAVGVM
CCCCHHHCCCCCEEE
22817900
311AcetylationPNVPHYAKNKAVGVM
CCCCHHHCCCCCEEE
25953088
313UbiquitinationVPHYAKNKAVGVMKS
CCHHHCCCCCEEEEC
27667366
377PhosphorylationILTRRLDSARPHFMS
HHHHHHHHCCHHHHH
23186163
384PhosphorylationSARPHFMSQF-----
HCCHHHHHCC-----
28464451

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 MAP11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAP11_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 MAP11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MAP11_HUMAN !!

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 MAP11_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP