UniProt Accession

 YMEL1_HUMAN; Q96TA2; B4DNM1; D3DRV8; D3DRV9; Q5T8D9; Q9H1Q0; Q9UMR9 

Genbank Protein ID

 AF151782; AJ132637; AY358484; AK297973; AL162272; AL162272; AL160291; AL160291; AL162272; AL160291; AL162272; CH471072; CH471072; CH471072; CH471072; CH471072; BC023507; BC024032 

Genbank Nucleotide ID

 AAK57555.1; CAB51858.1; AAQ88848.1; BAG60283.1; CAC19650.2; CAI12217.1; CAI12217.1; CAI16906.1; CAI16906.1; CAI16907.1; CAI16907.1; EAW86068.1; EAW86069.1; EAW86070.1; EAW86071.1; EAW86072.1; AAH23507.1; AAH24032.1 

Protein Name

 ATP-dependent zinc metalloprotease YME1L1 

Protein Synonyms/Alias

 ATP-dependent metalloprotease FtsH1; Meg-4; Presenilin-associated metalloprotease; PAMP; YME1-like protein 1 

Gene Name

 YME1L1 

Gene Synonyms/Alias

 FTSH1; YME1L; UNQ1868/PRO4304 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
144	NLLPGFCKGKNISSH	ubiquitination	[1]
146	LPGFCKGKNISSHWH	ubiquitination	[1]
237	NIAPSFVKGFLLRDR	acetylation	[2]
237	NIAPSFVKGFLLRDR	ubiquitination	[1, 3, 4, 5, 6]
253	SDVESLDKLMKTKNI	ubiquitination	[3, 6]
258	LDKLMKTKNIPEAHQ	ubiquitination	[1, 3, 4, 6]
269	EAHQDAFKTGFAEGF	ubiquitination	[3, 6]
278	GFAEGFLKAQALTQK	ubiquitination	[1, 4]
334	AVDPVQMKNVTFEHV	ubiquitination	[4]
363	EFLKNPQKFTILGGK	ubiquitination	[3, 6]
370	KFTILGGKLPKGILL	ubiquitination	[7]
385	VGPPGTGKTLLARAV	ubiquitination	[1, 3, 5, 6, 7]
446	ELDSVGGKRIESPMH	ubiquitination	[1, 8]
522	ILKWYLNKIKFDQSV	ubiquitination	[1]
524	KWYLNKIKFDQSVDP	ubiquitination	[1, 3, 4, 6]
556	LVNQAALKAAVDGKE	ubiquitination	[1, 4, 8, 9]
562	LKAAVDGKEMVTMKE	ubiquitination	[1]
568	GKEMVTMKELEFSKD	ubiquitination	[3, 6]
691	IAKRMVTKFGMSEKL	ubiquitination	[1]
708	MTYSDTGKLSPETQS	ubiquitination	[1, 4, 9]
744	KTHAKEHKNLAEALL	ubiquitination	[1]
768	IQIVLEGKKLEVR**	ubiquitination	[1]

Reference

 [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] 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]
 [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] 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] 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]
 [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] 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]
 [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] 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] 

Functional Description

 Putative ATP-dependent protease which plays a role in mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Requires to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1). Seems to act in the processing of OPA1. 

Sequence Annotation

 NP_BIND 379 386 ATP (Potential).
 ACT_SITE 600 600 By similarity.
 METAL 599 599 Zinc; catalytic (By similarity).
 METAL 603 603 Zinc; catalytic (By similarity).
 METAL 677 677 Zinc; catalytic (By similarity).  

Keyword

 Alternative splicing; ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 773 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0008283; P:cell proliferation; IMP:UniProtKB.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IMP:UniProtKB.
 GO:0007005; P:mitochondrion organization; IMP:UniProtKB. 

Interpro

 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR005936; FtsH.
 IPR027417; P-loop_NTPase.
 IPR000642; Peptidase_M41. 

Pfam

 PF00004; AAA
 PF01434; Peptidase_M41 

SMART

 SM00382; AAA 

PROSITE

 PS00674; AAA 

PRINTS