UniProt Accession

 STML2_HUMAN; Q9UJZ1; D3DRN3; O60376; Q53G29; Q96FY2; Q9P042 

Genbank Protein ID

 AF190167; AF282596; AK027405; AK223102; AL353795; AC004472; CH471071; CH471071; BC002442; BC003025; BC010152; BC014990; AF161458 

Genbank Nucleotide ID

 AAF09142.1; AAF91466.1; BAB55091.1; BAD96822.1; CAH70998.1; AAC07983.1; EAW58395.1; EAW58396.1; AAH02442.1; AAH03025.1; AAH10152.1; AAH14990.1; AAF29073.1 

Protein Name

 Stomatin-like protein 2, mitochondrial 

Protein Synonyms/Alias

 SLP-2; EPB72-like protein 2; Paraprotein target 7; Paratarg-7 

Gene Name

 STOML2 

Gene Synonyms/Alias

 SLP2; HSPC108 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
114	LRIMDPYKASYGVED	ubiquitination	[1]
140	TMRSELGKLSLDKVF	ubiquitination	[2, 3, 4]
145	LGKLSLDKVFRERES	acetylation	[5]
145	LGKLSLDKVFRERES	ubiquitination	[2, 3, 4, 6]
222	INVAEGKKQAQILAS	ubiquitination	[3]
233	ILASEAEKAEQINQA	acetylation	[5]
250	EASAVLAKAKAKAEA	ubiquitination	[1, 3]
252	SAVLAKAKAKAEAIR	ubiquitination	[3]

Reference

 [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] 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] 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]
 [4] 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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] 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] 

Functional Description

 Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation. 

Sequence Annotation

 MOD_RES 17 17 Phosphoserine; by PKC/PRKCZ.
 MOD_RES 124 124 Phosphotyrosine.
 MOD_RES 145 145 N6-acetyllysine.
 MOD_RES 233 233 N6-acetyllysine.  

Keyword

 Acetylation; Cell membrane; Coiled coil; Complete proteome; Direct protein sequencing; Lipid-binding; Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Polymorphism; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 356 AA 

Protein Sequence

Gene Ontology

 GO:0005856; C:cytoskeleton; TAS:ProtInc.
 GO:0019897; C:extrinsic to plasma membrane; IDA:UniProtKB.
 GO:0045121; C:membrane raft; IDA:UniProtKB.
 GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
 GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
 GO:1901612; F:cardiolipin binding; IDA:UniProtKB.
 GO:0005102; F:receptor binding; TAS:ProtInc.
 GO:0035710; P:CD4-positive, alpha-beta T cell activation; ISS:UniProtKB.
 GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
 GO:0032623; P:interleukin-2 production; ISS:UniProtKB.
 GO:0010876; P:lipid localization; ISS:UniProtKB.
 GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
 GO:0006851; P:mitochondrial calcium ion transport; IMP:UniProtKB.
 GO:0034982; P:mitochondrial protein processing; ISS:UniProtKB.
 GO:1900210; P:positive regulation of cardiolipin metabolic process; IMP:UniProtKB.
 GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:UniProtKB.
 GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:UniProtKB.
 GO:0051259; P:protein oligomerization; IDA:UniProtKB.
 GO:1990046; P:stress-induced mitochondrial fusion; ISS:UniProtKB.
 GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB. 

Interpro

 IPR001107; Band_7.
 IPR001972; Stomatin. 

Pfam

 PF01145; Band_7 

SMART

 SM00244; PHB 

PROSITE

  

PRINTS

 PR00721; STOMATIN.