P11233

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession RALA_HUMAN; P11233;
Entrez ID 5898
GenBank Protein ID NM_005402.3; XM_006715762.2; XM_011515466.1;
GenBank Nucleotide ID NP_005393.2; XP_006715825.1; XP_011513768.1;
Protein Name Ras-related protein Ral-A
Gene Name RALA; RAL
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionMultifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling (PubMed:20005108). Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells (PubMed:19306925). During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody (PubMed:18756269).
Sequence
(Fasta)
MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE 60
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV 120
PFLLVGNKSD LEDKRQVSVE EAKNRAEQWN VNYVETSAKT RANVDKVFFD LMREIRARKM 180
EDSKEKNGKK KRKSLAKRIR ERCCIL 207

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Serine PhosphorylationPancreatic cancer/carcinoma/adenocarcinomaPS19419901077
[Reference]: Furthermore, such transformation and in some cases also tumorigenesis depend upon S194 of RalA, a known Aurora-A phosphorylation site.?

※ Disease Cross-ref Annotation

DatabaseAnnotation
GWASdb
(count: 3)
rs13311977; Calcium levels; calcium metabolism disease|atherosclerosis
rs1034771; Body Mass Index; obesity
rs10486802; Urinary metabolites; kidney disease

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 11)
(view all)
11        NKPKGQNSLALHKVI     dbPAF
138       LEDKRQVSVEEAKNR     dbPAF
153       AEQWNVNYVETSAKT     dbPAF
183       RARKMEDSKEKNGKK     dbPAF
194       NGKKKRKSLAKRIRE     dbPAF
22        HKVIMVGSGGVGKSA     dbPAF
Ubiquitination
(count: 8)
(view all)
128       PFLLVGNKSDLEDKR     PLMD
134       NKSDLEDKRQVSVEE     PLMD
143       QVSVEEAKNRAEQWN     PLMD
159       NYVETSAKTRANVDK     PLMD
166       KTRANVDKVFFDLMR     PLMD
179       MREIRARKMEDSKEK     PLMD
Glycation
(count: 4)
128       PFLLVGNKSDLEDKR     PLMD
143       QVSVEEAKNRAEQWN     PLMD
16        QNSLALHKVIMVGSG     PLMD
166       KTRANVDKVFFDLMR     PLMD
Malonylation
(count: 1)
16        QNSLALHKVIMVGSG     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource
P11233P62158HPRD; MINT
P11233Q13485HPRD; MINT