ADA21_HUMAN - dbPTM
ADA21_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA21_HUMAN
UniProt AC Q9UKJ8
Protein Name Disintegrin and metalloproteinase domain-containing protein 21
Gene Name ADAM21
Organism Homo sapiens (Human).
Sequence Length 722
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description May be involved in sperm maturation and/or fertilization. May also be involved in epithelia functions associated with establishing and maintaining gradients of ions or nutrients..
Protein Sequence MAVDGTLVYIRVTLLLLWLGVFLSISGYCQAGPSQHFTSPEVVIPLKVISRGRSAKAPGWLSYSLRFGGQKHVVHMRVKKLLVSRHLPVFTYTDDRALLEDQLFIPDDCYYHGYVEAAPESLVVFSACFGGFRGVLKISGLTYEIEPIRHSATFEHLVYKINSNETQFPAMRCGLTEKEVARQQLEFEEAENSALEPKSAGDWWTHAWFLELVVVVNHDFFIYSQSNISKVQEDVFLVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMTSIEQVLNDFSQWKQISLSQLQHDAAHMFIKNSLISILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCIMNTFRVPAEKFTNCSYADFMKTTLNQGSCLHNPPRLGEIFMLKRCGNGVVEREEQCDCGSVQQCEQDACCLLNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPEDRYVQDGIPCSDSAYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVRDIPLLQDHFTLQHTHINGVTCWGIDYHLRMNISDIGEVKDGTVCGPGKICIHKKCVSLSVLSHVCLPETCNMKGICNNKHHCHCGYGWSPPYCQHRGYGGSIDSGPASAKRGVFLPLIVIPSLSVLTFLFTVGLLMYLRQCSGPKETKAHSSG
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
47UbiquitinationPEVVIPLKVISRGRS
CCEEEEEEEEECCCC
31.97-
54PhosphorylationKVISRGRSAKAPGWL
EEEECCCCCCCCCEE
36.6246159067
64PhosphorylationAPGWLSYSLRFGGQK
CCCEEEEEEEECCEE
15.0824719451
84PhosphorylationRVKKLLVSRHLPVFT
EEHHHHHHCCCCCEE
17.6024719451
164N-linked_GlycosylationLVYKINSNETQFPAM
EEEECCCCCCCCCCC
52.42UniProtKB CARBOHYD
176PhosphorylationPAMRCGLTEKEVARQ
CCCCCCCCHHHHHHH
30.2323663014
227N-linked_GlycosylationFFIYSQSNISKVQED
EEEEECCCHHHCCCE
34.61UniProtKB CARBOHYD
286PhosphorylationFSQWKQISLSQLQHD
HHHHHCCCHHHHHHH
21.3423663014
288PhosphorylationQWKQISLSQLQHDAA
HHHCCCHHHHHHHHH
23.2723663014
377N-linked_GlycosylationVPAEKFTNCSYADFM
CCHHHCCCCCHHHHH
18.83UniProtKB CARBOHYD
387PhosphorylationYADFMKTTLNQGSCL
HHHHHHHCCCCCCCC
20.4226503514
392PhosphorylationKTTLNQGSCLHNPPR
HHCCCCCCCCCCCCC
12.0726503514
437N-linked_GlycosylationQDACCLLNCTLRPGA
HHEEEEECCCCCCCC
12.09UniProtKB CARBOHYD
478N-linked_GlycosylationCDLPEWCNGTSHQCP
CCCCHHHCCCCCCCC
58.83UniProtKB CARBOHYD
546N-linked_GlycosylationRFGHCGINGTTYLKC
CCCCCCCCCCCEEEE
27.35UniProtKB CARBOHYD
600N-linked_GlycosylationIDYHLRMNISDIGEV
EEEEEECCHHHCCCC
24.95UniProtKB CARBOHYD
667PhosphorylationPYCQHRGYGGSIDSG
CCCCCCCCCCCCCCC
20.4729970186
673PhosphorylationGYGGSIDSGPASAKR
CCCCCCCCCCCCCCC
45.0329970186
677PhosphorylationSIDSGPASAKRGVFL
CCCCCCCCCCCCCCH
37.1468726479

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 ADA21_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA21_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 ADA21_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCSK1_HUMANPCSK1Nphysical
28514442
VEGFB_HUMANVEGFBphysical
28514442
AMGO1_HUMANAMIGO1physical
28514442
1B07_HUMANHLA-Bphysical
28514442
1B18_HUMANHLA-Bphysical
28514442
EGFL7_HUMANEGFL7physical
28514442
ITB5_HUMANITGB5physical
28514442
GBB2_HUMANGNB2physical
28514442
CALX_HUMANCANXphysical
28514442
DYR2_HUMANDHFRL1physical
28514442
PLXA2_HUMANPLXNA2physical
28514442
LRRC3_HUMANLRRC3physical
28514442
CCPG1_HUMANCCPG1physical
28514442
LCLT1_HUMANLCLAT1physical
28514442
MANF_HUMANMANFphysical
28514442
CHSS3_HUMANCHSY3physical
28514442
ASPH2_HUMANASPHD2physical
28514442
ACTA_HUMANACTA2physical
28514442
LRFN3_HUMANLRFN3physical
28514442
PLXB2_HUMANPLXNB2physical
28514442
GPC4_HUMANGPC4physical
28514442
ANR46_HUMANANKRD46physical
28514442
DEFM_HUMANPDFphysical
28514442
GRP78_HUMANHSPA5physical
28514442
GOGA5_HUMANGOLGA5physical
28514442
LRP10_HUMANLRP10physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADA21_HUMAN

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Related Literatures of Post-Translational Modification

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