Q96TA2 (YMEL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent zinc metalloprotease YME1L1
EC=3.4.24.-

Alternative name(s):
ATP-dependent metalloprotease FtsH1
Meg-4
Presenilin-associated metalloprotease
Short name=PAMP
YME1-like protein 1

Gene names

Name:	YME1L1
Synonyms:	FTSH1, YME1L
ORF Names:	UNQ1868/PRO4304

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	773 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Putative ATP-dependent protease which plays a role in mitochondrial protein metabolism. Seems to act in the processing of OPA1. Ref.7
Cofactor	Binds 1 zinc ion per subunit Potential.
Subcellular location	Mitochondrion Ref.2.
Sequence similarities	In the N-terminal section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein catabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: InterPro mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96TA2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q96TA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     57-113: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 773	773	ATP-dependent zinc metalloprotease YME1L1		PRO_0000084667
Regions
	Nucleotide binding	379 – 386	8	ATP Potential
Sites
	Active site	600	1	By similarity
	Metal binding	599	1	Zinc; catalytic By similarity
	Metal binding	603	1	Zinc; catalytic By similarity
	Metal binding	677	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	237	1	N6-acetyllysine Ref.8
Natural variations
	Alternative sequence	57 – 113	57	Missing in isoform 2.		VSP_010017
Experimental info
	Sequence conflict	12	1	V → F in AAK57555. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: FB77990F4D7B3A58	FASTA	773	86,455
	10 20 30 40 50 60 MFSLSSTVQP QVTVPLSHLI NAFHTPKNTS VSLSGVSVSQ NQHRDVVPEH EAPSSECMFS 70 80 90 100 110 120 DFLTKLNIVS IGKGKIFEGY RSMFMEPAKR MKKSLDTTDN WHIRPEPFSL SIPPSLNLRD 130 140 150 160 170 180 LGLSELKIGQ IDQLVENLLP GFCKGKNISS HWHTSHVSAQ SFFENKYGNL DIFSTLRSSC 190 200 210 220 230 240 LYRHHSRALQ SICSDLQYWP VFIQSRGFKT LKSRTRRLQS TSERLAETQN IAPSFVKGFL 250 260 270 280 290 300 LRDRGSDVES LDKLMKTKNI PEAHQDAFKT GFAEGFLKAQ ALTQKTNDSL RRTRLILFVL 310 320 330 340 350 360 LLFGIYGLLK NPFLSVRFRT TTGLDSAVDP VQMKNVTFEH VKGVEEAKQE LQEVVEFLKN 370 380 390 400 410 420 PQKFTILGGK LPKGILLVGP PGTGKTLLAR AVAGEADVPF YYASGSEFDE MFVGVGASRI 430 440 450 460 470 480 RNLFREAKAN APCVIFIDEL DSVGGKRIES PMHPYSRQTI NQLLAEMDGF KPNEGVIIIG 490 500 510 520 530 540 ATNFPEALDN ALIRPGRFDM QVTVPRPDVK GRTEILKWYL NKIKFDQSVD PEIIARGTVG 550 560 570 580 590 600 FSGAELENLV NQAALKAAVD GKEMVTMKEL EFSKDKILMG PERRSVEIDN KNKTITAYHE 610 620 630 640 650 660 SGHAIIAYYT KDAMPINKAT IMPRGPTLGH VSLLPENDRW NETRAQLLAQ MDVSMGGRVA 670 680 690 700 710 720 EELIFGTDHI TTGASSDFDN ATKIAKRMVT KFGMSEKLGV MTYSDTGKLS PETQSAIEQE 730 740 750 760 770 IRILLRDSYE RAKHILKTHA KEHKNLAEAL LTYETLDAKE IQIVLEGKKL EVR
	Isoform 2 [UniParc]. Checksum: 17828316886DF7C5	FASTA	716	79,832
	10 20 30 40 50 60 MFSLSSTVQP QVTVPLSHLI NAFHTPKNTS VSLSGVSVSQ NQHRDVVPEH EAPSSEPSLN 70 80 90 100 110 120 LRDLGLSELK IGQIDQLVEN LLPGFCKGKN ISSHWHTSHV SAQSFFENKY GNLDIFSTLR 130 140 150 160 170 180 SSCLYRHHSR ALQSICSDLQ YWPVFIQSRG FKTLKSRTRR LQSTSERLAE TQNIAPSFVK 190 200 210 220 230 240 GFLLRDRGSD VESLDKLMKT KNIPEAHQDA FKTGFAEGFL KAQALTQKTN DSLRRTRLIL 250 260 270 280 290 300 FVLLLFGIYG LLKNPFLSVR FRTTTGLDSA VDPVQMKNVT FEHVKGVEEA KQELQEVVEF 310 320 330 340 350 360 LKNPQKFTIL GGKLPKGILL VGPPGTGKTL LARAVAGEAD VPFYYASGSE FDEMFVGVGA 370 380 390 400 410 420 SRIRNLFREA KANAPCVIFI DELDSVGGKR IESPMHPYSR QTINQLLAEM DGFKPNEGVI 430 440 450 460 470 480 IIGATNFPEA LDNALIRPGR FDMQVTVPRP DVKGRTEILK WYLNKIKFDQ SVDPEIIARG 490 500 510 520 530 540 TVGFSGAELE NLVNQAALKA AVDGKEMVTM KELEFSKDKI LMGPERRSVE IDNKNKTITA 550 560 570 580 590 600 YHESGHAIIA YYTKDAMPIN KATIMPRGPT LGHVSLLPEN DRWNETRAQL LAQMDVSMGG 610 620 630 640 650 660 RVAEELIFGT DHITTGASSD FDNATKIAKR MVTKFGMSEK LGVMTYSDTG KLSPETQSAI 670 680 690 700 710 EQEIRILLRD SYERAKHILK THAKEHKNLA EALLTYETLD AKEIQIVLEG KKLEVR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human ATP-dependent metalloprotease (FtsH1) homolog mRNA." Miyata T., Inagi R., Yasuda Y., Kurokawa K. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Identification and characterization of YME1L1, a novel paraplegin-related gene." Coppola M., Pizzigoni A., Banfi S., Bassi M.T., Casari G., Incerti B. Genomics 66:48-54(2000) [PubMed: 10843804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION. Tissue: Fetal brain.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Muscle and Placenta.
[7]	"Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential." Guillery O., Malka F., Landes T., Guillou E., Blackstone C., Lombes A., Belenguer P., Arnoult D., Rojo M. Biol. Cell 100:315-325(2008) [PubMed: 18076378] [Abstract] Cited for: FUNCTION IN PROCESSING OF OPA1.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF151782 mRNA. Translation: AAK57555.1. AJ132637 mRNA. Translation: CAB51858.1. AY358484 mRNA. Translation: AAQ88848.1. AL162272 Genomic DNA. Translation: CAC19650.2. AL162272, AL160291 Genomic DNA. Translation: CAI12217.1. AL160291, AL162272 Genomic DNA. Translation: CAI16906.1. AL160291, AL162272 Genomic DNA. Translation: CAI16907.1. CH471072 Genomic DNA. Translation: EAW86068.1. CH471072 Genomic DNA. Translation: EAW86069.1. CH471072 Genomic DNA. Translation: EAW86070.1. CH471072 Genomic DNA. Translation: EAW86072.1. BC023507 mRNA. Translation: AAH23507.1. BC024032 mRNA. Translation: AAH24032.1.
IPI	IPI00045946. IPI00099529.
RefSeq	NP_055078.1. NM_014263.2. NP_647473.1. NM_139312.1.
UniGene	Hs.499145. Hs.74647.
3D structure databases
ProteinModelPortal	Q96TA2.
SMR	Q96TA2. Positions 332-766.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96TA2. 5 interactions.
STRING	Q96TA2.
PTM databases
PhosphoSite	Q96TA2.
Polymorphism databases
DMDM	46397258.
Proteomic databases
PRIDE	Q96TA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326799; ENSP00000318480; ENSG00000136758.
GeneID	10730.
KEGG	hsa:10730.
UCSC	uc001iti.1. human. uc001itj.1. human.
Organism-specific databases
CTD	10730.
GeneCards	GC10M027439.
H-InvDB	HIX0008725.
HGNC	HGNC:12843. YME1L1.
MIM	607472. gene.
neXtProt	NX_Q96TA2.
PharmGKB	PA37434.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG724153.
HOVERGEN	HBG057127.
InParanoid	Q96TA2.
OMA	VSAQSFF.
PhylomeDB	Q96TA2.
Gene expression databases
ArrayExpress	Q96TA2.
Bgee	Q96TA2.
CleanEx	HS_YME1L1.
Genevestigator	Q96TA2.
GermOnline	ENSG00000136758. Homo sapiens.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR005936. Pept_M41_FtsH. IPR000642. Peptidase_M41. [Graphical view]
KO	K08955.
Pfam	PF00004. AAA. 1 hit. PF01434. Peptidase_M41. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
TIGRFAMs	TIGR01241. FtsH_fam. 1 hit.
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	40734.
SOURCE	Search...

Entry information

Entry name

YMEL1_HUMAN

Accession

Primary (citable) accession number: Q96TA2
Secondary accession number(s): D3DRV8 , D3DRV9, Q5T8D9, Q9H1Q0, Q9UMR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.