CPLM-020246

Genbank Nucleotide ID

Transmembrane emp24 domain-containing protein 9

Protein Synonyms/Alias

GMP25; Glycoprotein 25L2; p24 family protein alpha-2; p24alpha2; p25

Homo sapiens (Human)

Position	Peptide	Type	References
71	YRTQLYDKQREEYQP	ubiquitination	[1, 2]
90	LGMFVEVKDPEDKVI	ubiquitination	[1]
160	AEIAAKDKLSELQLR	ubiquitination	[1, 2, 3, 4, 5, 6]
180	EQVEQIQKEQNYQRW	ubiquitination	[1, 2, 4, 5, 6, 7, 8, 9]
226	VWQMRHLKSFFEAKK	ubiquitination	[1, 3, 6]
232	LKSFFEAKKLV****	ubiquitination	[1]

[1] 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]
[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] 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]
[4] 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]
[5] 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]
[6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[7] 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]
[8] 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]
[9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]

Functional Description

Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer- dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB.

DOMAIN 47 145 GOLD.
REGION 121 160 Required for interaction with STX17.
MOTIF 228 235 COPI vesicle coat-binding (Potential).
MOTIF 228 229 COPII vesicle coat-binding (Potential).
CARBOHYD 125 125 N-linked (GlcNAc...).

Coiled coil; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane; Polymorphism; Protein transport; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0030140; C:trans-Golgi network transport vesicle; TAS:UniProtKB.
GO:0048205; P:COPI coating of Golgi vesicle; IMP:UniProtKB.
GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.

PF01105; EMP24_GP25L