| Tag | Content |
|---|
| CPLM ID | CPLM-012525 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Rab GTPase-binding effector protein 1 |
Protein Synonyms/Alias | Rabaptin-4; Rabaptin-5; Rabaptin-5alpha; Renal carcinoma antigen NY-REN-17 |
Gene Name | RABEP1 |
Gene Synonyms/Alias | RAB5EP; RABPT5; RABPT5A |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 107 | QEAIDEVKRQWREEV | ubiquitination | [1] | | 586 | QELEDFIKQSSEDSS | ubiquitination | [1] |
|
Reference | [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] |
Functional Description | Rab effector protein acting as linker between gamma- adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. |
Sequence Annotation | MOD_RES 2 2 N-acetylalanine.
MOD_RES 282 282 N6-acetyllysine.
MOD_RES 407 407 Phosphoserine.
MOD_RES 410 410 Phosphoserine. |
Keyword | 3D-structure; Acetylation; Alternative splicing; Apoptosis; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endocytosis; Endosome; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 862 AA |
Protein Sequence | MAQPGPASQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY LAKEEDLKRQ 60
NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ EAIDEVKRQW REEVASLQAV 120
MKETVRDYEH QFHLRLEQER TQWAQYRESA EREIADLRRR LSEGQEEENL ENEMKKAQED 180
AEKLRSVVMP MEKEIAALKD KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV 240
LNTQKSVLQE DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR 300
MEIVLTSEQL RQVEELKKKD QEDDEQQRLN KRKDHKKADV EEEIKIPVVC ALTQEESSAQ 360
LSNEEEHLDS TRGSVHSLDA GLLLPSGDPF SKSDNDMFKD GLRRAQSTDS LGTSGSLQSK 420
ALGYNYKAKS AGNLDESDFG PLVGADSVSE NFDTASLGSL QMPSGFMLTK DQERAIKAMT 480
PEQEETASLL SSVTQGMESA YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE 540
KQLQGIQIQE AETRDQVKKL QLMLRQANDQ LEKTMKDKQE LEDFIKQSSE DSSHQISALV 600
LRAQASEILL EELQQGLSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND SLQGKHSLHV 660
SLQQAEDFIL PDTTEALREL VLKYREDIIN VRTAADHVEE KLKAEILFLK EQIQAEQCLK 720
ENLEETLQLE IENCKEEIAS ISSLKAELER IKVEKGQATV EQLMFEEKNK AQRLQTELDV 780
SEQVQRDFVK LSQTLQVQLE RIRQADSLER IRAILNDTKL TDINQLPET 829 |
Gene Ontology | GO:0005769; C:early endosome; TAS:ProtInc. GO:0030139; C:endocytic vesicle; IDA:UniProtKB. GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell. GO:0005096; F:GTPase activator activity; IEA:InterPro. GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. GO:0006944; P:cellular membrane fusion; TAS:ProtInc. GO:0006897; P:endocytosis; TAS:ProtInc. GO:0043547; P:positive regulation of GTPase activity; IEA:GOC. GO:0015031; P:protein transport; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |