| Tag |
Content |
LipidDB ID |
LipidDB-10116-00521 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
5.65 |
Molecular Weight |
75252.35 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
RalA-binding protein 1 |
Protein Synonyms/Alias |
RalBP1; Cytocentrin; Dinitrophenyl S-glutathione ATPase; DNP-SG ATPase; Ral-interacting protein 1; |
Gene Name |
Ralbp1 |
Gene Synonyms/Alias |
|
Created Date |
15-AUG-2003 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
4 | Canonical | ****MTECFLPPTSS | [1] | S-Palmitoylation | 291 | Canonical | MPRFEEACGRTTEVE | [1] | S-Palmitoylation |
|
Organism |
Rattus norvegicus (Rat) |
NCBI Taxa ID |
10116 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin (By similarity). Involved in the assembly and function of the mitotic apparatus. |
Sequence Annotation |
Domain: 192 380 Rho-GAP.
Region: 86 415 Enhances GTP hydrolysis activity ofCDC42.
Region: 375 626 Interacts with RalA.
Modified residue: 2 2 N-acetylthreonine.
Modified residue: 29 29 Phosphoserine.
Modified residue: 62 62 Phosphoserine.
Modified residue: 92 92 Phosphoserine.
Modified residue: 93 93 Phosphoserine.
Modified residue: 463 463 Phosphoserine.
|
Protein Length |
647 AA. |
Protein Sequence
(Canonical) |
MTECFLPPTS SPSEHRRAEH GSGLTRTPSS EEISPTKFPE LYRTGEPSPP HDILHEPPDI 60
VSDDEKDHGK KKGKFKKKEK RTEGYVAFQE DSSGDEAESP SKMKRSKGIH VFKKPSFSKK 120
KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK CKDFTAADVV KQWKEKKKKK KPTQEPEVPQ 180
TDAPSLRPIF GAPFADAVER TMMYDGIRLP AVFRECVDYM EKHGMKCEGI YRVSGIKSKV 240
DELKAAYDRE ESPNLEEYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTEVEKV 300
QEFQRLLREL PEYNHLLLSW LIVHMDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVL 360
FTHVQELFGT VLLKQVTRPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI 420
KDFSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE ETNENEEVIN 480
ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIDRLRAE IAEIQSRQHG RSETEEYSSD 540
SESESEDEEE LQIILEDLQR QNEELEIKNN HLNQAVHEER EAIVELRVQL RLLQMLRAKS 600
EQQLQEEEEP ERRGGTGPLP CEGVLEVRAA KEQAKPSPSK DRKETPI 647
|
FASTA
(Canonical) |
>LipidDB-10116-00521|Q62796
MTECFLPPTSSPSEHRRAEHGSGLTRTPSSEEISPTKFPELYRTGEPSPPHDILHEPPDI
VSDDEKDHGKKKGKFKKKEKRTEGYVAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKK
KEKDFKIKEKPKEEKHKEEKHKEEKHKEKKCKDFTAADVVKQWKEKKKKKKPTQEPEVPQ
TDAPSLRPIFGAPFADAVERTMMYDGIRLPAVFRECVDYMEKHGMKCEGIYRVSGIKSKV
DELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTEVEKV
QEFQRLLRELPEYNHLLLSWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVL
FTHVQELFGTVLLKQVTRPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGI
KDFSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEETNENEEVIN
ILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQHGRSETEEYSSD
SESESEDEEELQIILEDLQRQNEELEIKNNHLNQAVHEEREAIVELRVQLRLLQMLRAKS
EQQLQEEEEPERRGGTGPLPCEGVLEVRAAKEQAKPSPSKDRKETPI
|
Gene Ontology |
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW GO:0016021; C:integral component of membrane; IEA:InterPro GO:0043005; C:neuron projection; IDA:RGD GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW GO:0006897; P:endocytosis; IMP:RGD GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW GO:0007052; P:mitotic spindle organization; IDA:RGD GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD GO:0007264; P:small GTPase mediated signal transduction; IPI:RGD |
Interpro |
|
Pfam |
|
SMART |
|
PROSITE |
|
PRINTS |
|