CPLM-009567

Genbank Nucleotide ID

Ras-related protein Rab-1A

Protein Synonyms/Alias

YPT1-related protein

Homo sapiens (Human)

Position	Peptide	Type	References
58	RTIELDGKTIKLQIW	ubiquitination	[1, 2]
61	ELDGKTIKLQIWDTA	ubiquitination	[3]
103	QESFNNVKQWLQEID	ubiquitination	[4]
119	YASENVNKLLVGNKC	ubiquitination	[1, 2, 4, 5]
125	NKLLVGNKCDLTTKK	ubiquitination	[2]
187	ATAGGAEKSNVKIQS	ubiquitination	[1, 2, 4, 6]
191	GAEKSNVKIQSTPVK	ubiquitination	[1, 4]

[1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

Probably required for transit of protein from the ER through Golgi compartment. Binds GTP and GDP and possesses intrinsic GTPase activity.

NP_BIND 18 26 GTP.
NP_BIND 66 70 GTP (By similarity).
NP_BIND 124 127 GTP.
NP_BIND 154 156 GTP.
MOTIF 40 48 Effector region (By similarity).
MOD_RES 2 2 N-acetylserine.
MOD_RES 79 79 O-(2-cholinephosphoryl)serine; by
MOD_RES 194 194 Phosphoserine; by CDK1 (Probable).
LIPID 204 204 S-geranylgeranyl cysteine.
LIPID 205 205 S-geranylgeranyl cysteine.

3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO:0000139; C:Golgi membrane; TAS:Reactome.
GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO:0003924; F:GTPase activity; TAS:ProtInc.
GO:0000278; P:mitotic cell cycle; TAS:Reactome.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.

IPR027417; P-loop_NTPase.
IPR005225; Small_GTP-bd_dom.
IPR001806; Small_GTPase.
IPR003579; Small_GTPase_Rab_type.

PR00449; RASTRNSFRMNG.