| Tag | Content |
|---|
| CPLM ID | CPLM-004724 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dipeptidyl aminopeptidase B |
Protein Synonyms/Alias | DPAP B; YSCV |
Gene Name | DAP2 |
Gene Synonyms/Alias | YHR028C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 365 | FLIDTIAKTSNVVRN | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | |
Sequence Annotation | ACT_SITE 679 679 Charge relay system (By similarity).
ACT_SITE 756 756 Charge relay system (By similarity).
ACT_SITE 789 789 Charge relay system (By similarity).
CARBOHYD 63 63 N-linked (GlcNAc...) (Potential).
CARBOHYD 79 79 N-linked (GlcNAc...) (Potential).
CARBOHYD 110 110 N-linked (GlcNAc...) (Potential).
CARBOHYD 139 139 N-linked (GlcNAc...) (Potential).
CARBOHYD 372 372 N-linked (GlcNAc...) (Potential).
CARBOHYD 392 392 N-linked (GlcNAc...) (Potential).
CARBOHYD 421 421 N-linked (GlcNAc...) (Potential).
CARBOHYD 738 738 N-linked (GlcNAc...) (Potential). |
Keyword | 3D-structure; Aminopeptidase; Complete proteome; Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome; Serine protease; Signal-anchor; Transmembrane; Transmembrane helix; Vacuole. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 818 AA |
Protein Sequence | MEGGEEEVER IPDELFDTKK KHLLDKLIRV GIILVLLIWG TVLLLKSIPH HSNTPDYQEP 60
NSNYTNDGKL KVSFSVVRNN TFQPKYHELQ WISDNKIESN DLGLYVTFMN DSYVVKSVYD 120
DSYNSVLLEG KTFIHNGQNL TVESITASPD LKRLLIRTNS VQNWRHSTFG SYFVYDKSSS 180
SFEEIGNEVA LAIWSPNSND IAYVQDNNIY IYSAISKKTI RAVTNDGSSF LFNGKPDWVY 240
EEEVFEDDKA AWWSPTGDYL AFLKIDESEV GEFIIPYYVQ DEKDIYPEMR SIKYPKSGTP 300
NPHAELWVYS MKDGTSFHPR ISGNKKDGSL LITEVTWVGN GNVLVKTTDR SSDILTVFLI 360
DTIAKTSNVV RNESSNGGWW EITHNTLFIP ANETFDRPHN GYVDILPIGG YNHLAYFENS 420
NSSHYKTLTE GKWEVVNGPL AFDSMENRLY FISTRKSSTE RHVYYIDLRS PNEIIEVTDT 480
SEDGVYDVSF SSGRRFGLLT YKGPKVPYQK IVDFHSRKAE KCDKGNVLGK SLYHLEKNEV 540
LTKILEDYAV PRKSFRELNL GKDEFGKDIL VNSYEILPND FDETLSDHYP VFFFAYGGPN 600
SQQVVKTFSV GFNEVVASQL NAIVVVVDGR GTGFKGQDFR SLVRDRLGDY EARDQISAAS 660
LYGSLTFVDP QKISLFGWSY GGYLTLKTLE KDGGRHFKYG MSVAPVTDWR FYDSVYTERY 720
MHTPQENFDG YVESSVHNVT ALAQANRFLL MHGTGDDNVH FQNSLKFLDL LDLNGVENYD 780
VHVFPDSDHS IRYHNANVIV FDKLLDWAKR AFDGQFVK 818 |
Gene Ontology | GO:0000329; C:fungal-type vacuole membrane; IDA:SGD. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. GO:0008239; F:dipeptidyl-peptidase activity; IDA:SGD. GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. GO:0016485; P:protein processing; ISS:SGD. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |