| Tag | Content |
|---|
| CPLM ID | CPLM-005381 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable ATP-dependent permease |
Protein Synonyms/Alias | |
Gene Name | ADP1 |
Gene Synonyms/Alias | YCR011C; YCR105; YCR11C |
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 |
|---|
| 359 | RNGLGSSKSPIRLPD | 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 | DOMAIN 384 631 ABC transporter.
DOMAIN 793 1044 ABC transmembrane type-2.
NP_BIND 423 430 ATP (By similarity).
MOD_RES 659 659 Phosphoserine.
MOD_RES 702 702 Phosphoserine.
CARBOHYD 50 50 N-linked (GlcNAc...) (Potential).
CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
CARBOHYD 165 165 N-linked (GlcNAc...) (Potential).
CARBOHYD 221 221 N-linked (GlcNAc...) (Potential).
CARBOHYD 935 935 N-linked (GlcNAc...) (Potential). |
Keyword | ATP-binding; Complete proteome; Endoplasmic reticulum; Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1049 AA |
Protein Sequence | MGSHRRYLYY SILSFLLLSC SVVLAKQDKT PFFEGTSSKN SRLTAQDKGN DTCPPCFNCM 60
LPIFECKQFS ECNSYTGRCE CIEGFAGDDC SLPLCGGLSP DESGNKDRPI RAQNDTCHCD 120
NGWGGINCDV CQEDFVCDAF MPDPSIKGTC YKNGMIVDKV FSGCNVTNEK ILQILNGKIP 180
QITFACDKPN QECNFQFWID QLESFYCGLS DCAFEYDLEQ NTSHYKCNDV QCKCVPDTVL 240
CGAKGSIDIS DFLTETIKGP GDFSCDLETR QCKFSEPSMN DLILTVFGDP YITLKCESGE 300
CVHYSEIPGY KSPSKDPTVS WQGKLVLALT AVMVLALFTF ATFYISKSPL FRNGLGSSKS 360
PIRLPDEDAV NNFLQNEDDT LATLSFENIT YSVPSINSDG VEETVLNEIS GIVKPGQILA 420
IMGGSGAGKT TLLDILAMKR KTGHVSGSIK VNGISMDRKS FSKIIGFVDQ DDFLLPTLTV 480
FETVLNSALL RLPKALSFEA KKARVYKVLE ELRIIDIKDR IIGNEFDRGI SGGEKRRVSI 540
ACELVTSPLV LFLDEPTSGL DASNANNVIE CLVRLSSDYN RTLVLSIHQP RSNIFYLFDK 600
LVLLSKGEMV YSGNAKKVSE FLRNEGYICP DNYNIADYLI DITFEAGPQG KRRRIRNISD 660
LEAGTDTNDI DNTIHQTTFT SSDGTTQREW AHLAAHRDEI RSLLRDEEDV EGTDGRRGAT 720
EIDLNTKLLH DKYKDSVYYA ELSQEIEEVL SEGDEESNVL NGDLPTGQQS AGFLQQLSIL 780
NSRSFKNMYR NPKLLLGNYL LTILLSLFLG TLYYNVSNDI SGFQNRMGLF FFILTYFGFV 840
TFTGLSSFAL ERIIFIKERS NNYYSPLAYY ISKIMSEVVP LRVVPPILLS LIVYPMTGLN 900
MKDNAFFKCI GILILFNLGI SLEILTIGII FEDLNNSIIL SVLVLLGSLL FSGLFINTKN 960
ITNVAFKYLK NFSVFYYAYE SLLINEVKTL MLKERKYGLN IEVPGATILS TFGFVVQNLV 1020
FDIKILALFN VVFLIMGYLA LKWIVVEQK 1049 |
Gene Ontology | GO:0005783; C:endoplasmic reticulum; IDA:SGD. GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0016021; C:integral to membrane; ISM:SGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; ISS:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |