CPLM-009309

Genbank Nucleotide ID

Ras-related protein Rab-14

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
35	LHQFTEKKFMADCPH	ubiquitination	[1, 2]
59	IIEVSGQKIKLQIWD	ubiquitination	[2]
61	EVSGQKIKLQIWDTA	ubiquitination	[2]
125	VIILIGNKADLEAQR	ubiquitination	[2, 3, 4, 5]
140	DVTYEEAKQFAEENG	ubiquitination	[3]
170	DAFLEAAKKIYQNIQ	ubiquitination	[3, 5, 6, 7]
171	AFLEAAKKIYQNIQD	ubiquitination	[2, 6, 8]
193	AESGVQHKPSAPQGG	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9]

[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] 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]
[4] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[6] 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]
[7] 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]
[8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[9] 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

Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N- cadherin/CDH2 shedding and cell-cell adhesion.

NP_BIND 18 26 GTP.
NP_BIND 66 70 GTP.
NP_BIND 124 127 GTP.
NP_BIND 154 156 GTP.
MOTIF 40 48 Effector region (By similarity).
MOD_RES 2 2 N-acetylalanine.
MOD_RES 98 98 Phosphothreonine (By similarity).
MOD_RES 99 99 Phosphotyrosine (By similarity).
MOD_RES 215 215 Cysteine methyl ester (By similarity).
LIPID 213 213 S-geranylgeranyl cysteine (By
LIPID 215 215 S-geranylgeranyl cysteine (By

3D-structure; Acetylation; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Polymorphism; Prenylation; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO:0005829; C:cytosol; ISS:UniProtKB.
GO:0005769; C:early endosome; ISS:UniProtKB.
GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO:0005795; C:Golgi stack; ISS:UniProtKB.
GO:0005770; C:late endosome; ISS:UniProtKB.
GO:0005764; C:lysosome; ISS:UniProtKB.
GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; ISS:UniProtKB.
GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
GO:0019003; F:GDP binding; IDA:UniProtKB.
GO:0005525; F:GTP binding; IDA:UniProtKB.
GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO:0016044; P:cellular membrane organization; TAS:Reactome.
GO:0009790; P:embryo development; ISS:UniProtKB.
GO:0032456; P:endocytic recycling; IDA:UniProtKB.
GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB.
GO:0007269; P:neurotransmitter secretion; NAS:UniProtKB.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
GO:0007264; P:small GTPase mediated signal transduction; NAS:UniProtKB.

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

PR00449; RASTRNSFRMNG.