CPLM-008195

Genbank Nucleotide ID

Transmembrane emp24 domain-containing protein 10

Protein Synonyms/Alias

21 kDa transmembrane-trafficking protein; S31III125; S31I125; Tmp-21-I; Transmembrane protein Tmp21; p23; p24 family protein delta-1; p24delta1; p24delta

Homo sapiens (Human)

Position	Peptide	Type	References
42	HLPINSRKCLREEIH	ubiquitination	[1]
50	CLREEIHKDLLVTGA	ubiquitination	[1]
75	GGLRSHLKITDSAGH	ubiquitination	[1, 2, 3]
87	AGHILYSKEDATKGK	ubiquitination	[1, 2, 3, 4]
94	KEDATKGKFAFTTED	ubiquitination	[1]
127	QLVILDMKHGVEAKN	ubiquitination	[1, 3, 4]
133	MKHGVEAKNYEEIAK	ubiquitination	[1, 3]
140	KNYEEIAKVEKLKPL	ubiquitination	[1, 3]
143	EEIAKVEKLKPLEVE	ubiquitination	[1]
145	IAKVEKLKPLEVELR	ubiquitination	[1, 3, 5]
169	VNDFAYMKKREEEMR	ubiquitination	[1, 3, 4]
170	NDFAYMKKREEEMRD	ubiquitination	[1]

[1] 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]
[2] 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]
[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] 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]
[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]

Functional Description

Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act togther with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1 (By similarity). In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus.

DOMAIN 41 193 GOLD.
REGION 1 142 Required for interaction with STX17.
REGION 147 178 Required for TMED10 and TMED2 cis-Golgi
REGION 204 219 Interaction with COPG1.
REGION 207 219 Interaction with ARF1.
MOTIF 211 219 COPI vesicle coat-binding.
MOTIF 211 212 COPII vesicle coat-binding.
MOD_RES 171 171 Omega-N-methylated arginine (By
MOD_RES 176 176 Omega-N-methylated arginine (By
CARBOHYD 179 179 N-linked (GlcNAc...) (Potential).

Cell membrane; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport; Glycoprotein; Golgi apparatus; Membrane; Methylation; Polymorphism; Protein transport; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005801; C:cis-Golgi network; ISS:HGNC.
GO:0030137; C:COPI-coated vesicle; ISS:UniProtKB.
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:0070765; C:gamma-secretase complex; IDA:UniProtKB.
GO:0016021; C:integral to membrane; ISS:HGNC.
GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO:0042589; C:zymogen granule membrane; ISS:HGNC.
GO:0034205; P:beta-amyloid formation; IMP:UniProtKB.
GO:0035459; P:cargo loading into vesicle; TAS:UniProtKB.
GO:0048205; P:COPI coating of Golgi vesicle; TAS:UniProtKB.
GO:0048208; P:COPII vesicle coating; TAS:UniProtKB.
GO:0007030; P:Golgi organization; IEA:Compara.
GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
GO:0001822; P:kidney development; IEA:Compara.
GO:0051259; P:protein oligomerization; IEA:Compara.
GO:0045055; P:regulated secretory pathway; ISS:HGNC.
GO:0001101; P:response to acid; IEA:Compara.
GO:0043279; P:response to alkaloid; IEA:Compara.
GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISS:UniProtKB.

PF01105; EMP24_GP25L