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UniProtKB - P36776 (LONM_HUMAN)

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Protein

Lon protease homolog, mitochondrial

Gene

LONP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters (PubMed:12198491, PubMed:15870080, PubMed:17420247, PubMed:8248235). Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein, helicase Twinkle (TWNK) and the large ribosomal subunit protein bL32m. bL32m is protected from degradation by LONP1 when it is bound to a nucleic acid (RNA), but TWNK is not (PubMed:17579211, PubMed:28377575).UniRule annotation6 Publications

Catalytic activityi

Hydrolysis of proteins in presence of ATP.UniRule annotation

Enzyme regulationi

Peptidase activity is subject to substrate inhibition by ATP.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei855UniRule annotation1
Active sitei898UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi523 – 530ATPUniRule annotation8

GO - Molecular functioni

  • ADP binding Source: UniProtKB
  • ATP binding Source: UniProtKB
  • ATP-dependent peptidase activity Source: UniProtKB
  • DNA polymerase binding Source: UniProtKB
  • G-quadruplex DNA binding Source: UniProtKB
  • mitochondrial promoter sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • serine-type endopeptidase activity Source: InterPro
  • single-stranded DNA binding Source: Ensembl
  • single-stranded RNA binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • aging Source: Ensembl
  • cellular protein-containing complex assembly Source: Ensembl
  • cellular response to oxidative stress Source: UniProtKB
  • mitochondrial DNA metabolic process Source: UniProtKB
  • mitochondrial genome maintenance Source: UniProtKB
  • mitochondrion organization Source: UniProtKB
  • oxidation-dependent protein catabolic process Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein quality control for misfolded or incompletely synthesized proteins Source: GO_Central
  • proteolysis involved in cellular protein catabolic process Source: UniProtKB
  • response to aluminum ion Source: Ensembl
  • response to hormone Source: Ensembl
  • response to hypoxia Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDNA-binding, Hydrolase, Protease, Serine protease
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.4.21.53 2681

Protein family/group databases

MEROPSiS16.002
MoonDBiP36776 Curated

Names & Taxonomyi

Protein namesi
Recommended name:
Lon protease homolog, mitochondrialUniRule annotation (EC:3.4.21.53UniRule annotation)
Alternative name(s):
LONHs
Lon protease-like proteinUniRule annotation
Short name:
LONPUniRule annotation
Mitochondrial ATP-dependent protease LonUniRule annotation
Serine protease 15UniRule annotation
Gene namesi
Name:LONP1UniRule annotation
Synonyms:PRSS15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000196365.11
HGNCiHGNC:9479 LONP1
MIMi605490 gene
neXtProtiNX_P36776

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

CODAS syndrome (CODASS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare syndrome characterized by the combination of cerebral, ocular, dental, auricular, and skeletal features. These include developmental delay, craniofacial anomalies, cataracts, ptosis, median nasal groove, delayed tooth eruption, hearing loss, short stature, delayed epiphyseal ossification, metaphyseal hip dysplasia, and vertebral coronal clefts.
See also OMIM:600373
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073338476E → A in CODASS. 1 Publication1
Natural variantiVAR_073339631S → Y in CODASS. 1 PublicationCorresponds to variant dbSNP:rs879255248EnsemblClinVar.1
Natural variantiVAR_073340670A → V in CODASS. 1 PublicationCorresponds to variant dbSNP:rs770036526Ensembl.1
Natural variantiVAR_073341672R → C in CODASS. 1 PublicationCorresponds to variant dbSNP:rs777009012Ensembl.1
Natural variantiVAR_073342676P → S in CODASS. 1 PublicationCorresponds to variant dbSNP:rs879255247EnsemblClinVar.1
Natural variantiVAR_073343679R → H in CODASS. 1 PublicationCorresponds to variant dbSNP:rs549574673EnsemblClinVar.1
Natural variantiVAR_073344721R → G in CODASS. 1 PublicationCorresponds to variant dbSNP:rs147588238Ensembl.1
Natural variantiVAR_073345724A → V in CODASS. 1 PublicationCorresponds to variant dbSNP:rs879255249EnsemblClinVar.1
Natural variantiVAR_073346749P → S in CODASS. 1 Publication1
Natural variantiVAR_073347767G → E in CODASS. 1 PublicationCorresponds to variant dbSNP:rs562553348Ensembl.1
Natural variantiVAR_073348927Missing in CODASS. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi529K → R: Abolishes ATPase activity, and presumably ATP-driven protein unfolding, but does not block access to the proteolytic active site or prevent a substrate from binding to it. 1 Publication1
Mutagenesisi770W → A: Has low basal, but normal stimulated ATPase activity, and retains peptidase activity. 1 Publication1
Mutagenesisi770W → P: Has normal basal, but low stimulated ATPase activity, and abolishes peptidase activity. 1 Publication1
Mutagenesisi855S → A: Lacks both ATPase and protease activity, but retains DNA binding activity. 2 Publications1
Mutagenesisi880T → V: Enhances the basal, but not the stimulated ATPase activity. 1 Publication1
Mutagenesisi893G → A: Has low basal, but normal stimulated ATPase activity, and retains peptidase activity. 1 Publication1
Mutagenesisi893G → P: Has normal basal, but low stimulated ATPase activity, and abolishes peptidase activity. 1 Publication1
Mutagenesisi894G → A or S: Enhances the basal, but not the stimulated ATPase activity, and retains peptidase activity. 1 Publication1
Mutagenesisi894G → P: Enhances the basal, but not the stimulated ATPase activity, and abolishes peptidase activity. 1 Publication1

Keywords - Diseasei

Cataract, Deafness, Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi9361
MalaCardsiLONP1
MIMi600373 phenotype
OpenTargetsiENSG00000196365
PharmGKBiPA162394145

Polymorphism and mutation databases

DMDMi12644239

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 67MitochondrionUniRule annotationCombined sourcesAdd BLAST67
ChainiPRO_000002673468 – 959Lon protease homolog, mitochondrialAdd BLAST892

Proteomic databases

EPDiP36776
MaxQBiP36776
PaxDbiP36776
PeptideAtlasiP36776
PRIDEiP36776
ProteomicsDBi55221

PTM databases

iPTMnetiP36776
PhosphoSitePlusiP36776
SwissPalmiP36776

Expressioni

Tissue specificityi

Duodenum, heart, lung and liver, but not thymus.

Gene expression databases

BgeeiENSG00000196365
CleanExiHS_LONP1
ExpressionAtlasiP36776 baseline and differential
GenevisibleiP36776 HS

Organism-specific databases

HPAiHPA002034
HPA002192

Interactioni

Subunit structurei

Homohexamer (PubMed:14739292, PubMed:25369343, PubMed:20222013). Organized in a ring with a central cavity (PubMed:25369343, PubMed:20222013). The ATP-binding and proteolytic domains (AP-domain) form a hexameric chamber, while the N-terminal domain is arranged as a trimer of dimers (PubMed:27632940). DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with TWNK and mitochondrial DNA polymerase subunit POLG (PubMed:14739292).UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSN2P026666EBI-357448,EBI-5260183From Bos taurus.

GO - Molecular functioni

  • DNA polymerase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi114762, 68 interactors
IntActiP36776, 45 interactors
MINTiP36776
STRINGi9606.ENSP00000353826

Structurei

Secondary structure

1959
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi764 – 786Combined sources23
Beta strandi799 – 804Combined sources6
Helixi808 – 828Combined sources21
Helixi834 – 837Combined sources4
Beta strandi839 – 843Combined sources5
Turni850 – 852Combined sources3
Helixi853 – 856Combined sources4
Helixi857 – 869Combined sources13
Beta strandi877 – 879Combined sources3
Beta strandi887 – 890Combined sources4
Helixi895 – 904Combined sources10
Beta strandi909 – 913Combined sources5
Helixi914 – 916Combined sources3
Helixi917 – 921Combined sources5
Helixi925 – 928Combined sources4
Beta strandi932 – 938Combined sources7
Helixi939 – 946Combined sources8

3D structure databases

ProteinModelPortaliP36776
SMRiP36776
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36776

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini124 – 368Lon N-terminalPROSITE-ProRule annotationAdd BLAST245
Domaini759 – 949Lon proteolyticPROSITE-ProRule annotationAdd BLAST191

Domaini

The Lon N-terminal domains are crucial for the overall structure of the protein, maintaining it in a conformation allowing its proper functioning.1 Publication
The AP-domain (ATP-binding and proteolytic domains) has a closed-ring conformation in the presence of AMP-PNP and its N-terminal entry gate appears closed. Upon ADP binding, it switches to a lock-washer conformation and its N-terminal gate opens.1 Publication
The proteolytic site is connected to the ATP binding site through the GG loop (Gly-893 and Gly-894) and the loop containing Trp-770. Binding of a protein substrate such as beta-casein appears to trigger movement of both these loops as part of the conformational changes which lead to enhanced ATPase and peptidase activities.1 Publication

Sequence similaritiesi

Belongs to the peptidase S16 family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2004 Eukaryota
COG0466 LUCA
GeneTreeiENSGT00530000063553
HOGENOMiHOG000261409
HOVERGENiHBG000798
InParanoidiP36776
KOiK08675
OMAiRSAENFG
OrthoDBiEOG091G01TN
PhylomeDBiP36776
TreeFamiTF105001

Family and domain databases

Gene3Di3.30.230.10, 1 hit
HAMAPiMF_03120 lonm_euk, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR004815 Lon_bac/euk-typ
IPR008269 Lon_proteolytic
IPR027065 Lon_Prtase
IPR003111 Lon_substr-bd
IPR027503 Lonm_euk
IPR027417 P-loop_NTPase
IPR008268 Peptidase_S16_AS
IPR015947 PUA-like_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
PANTHERiPTHR43718 PTHR43718, 1 hit
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF05362 Lon_C, 1 hit
PF02190 LON_substr_bdg, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SM00464 LON, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF54211 SSF54211, 1 hit
SSF88697 SSF88697, 1 hit
TIGRFAMsiTIGR00763 lon, 1 hit
PROSITEiView protein in PROSITE
PS51787 LON_N, 1 hit
PS51786 LON_PROTEOLYTIC, 1 hit
PS01046 LON_SER, 1 hit

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P36776-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAASTGYVRL WGAARCWVLR RPMLAAAGGR VPTAAGAWLL RGQRTCDASP 
        60         70         80         90        100
PWALWGRGPA IGGQWRGFWE ASSRGGGAFS GGEDASEGGA EEGAGGAGGS 
       110        120        130        140        150
AGAGEGPVIT ALTPMTIPDV FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV 
       160        170        180        190        200
ELLRRKVRLA QPYVGVFLKR DDSNESDVVE SLDEIYHTGT FAQIHEMQDL 
       210        220        230        240        250
GDKLRMIVMG HRRVHISRQL EVEPEEPEAE NKHKPRRKSK RGKKEAEDEL 
       260        270        280        290        300
SARHPAELAM EPTPELPAEV LMVEVENVVH EDFQVTEEVK ALTAEIVKTI 
       310        320        330        340        350
RDIIALNPLY RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL 
       360        370        380        390        400
EETNIPKRLY KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL 
       410        420        430        440        450
KIIKKELGLE KDDKDAIEEK FRERLKELVV PKHVMDVVDE ELSKLGLLDN 
       460        470        480        490        500
HSSEFNVTRN YLDWLTSIPW GKYSNENLDL ARAQAVLEED HYGMEDVKKR 
       510        520        530        540        550
ILEFIAVSQL RGSTQGKILC FYGPPGVGKT SIARSIARAL NREYFRFSVG 
       560        570        580        590        600
GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLILID EVDKIGRGYQ 
       610        620        630        640        650
GDPSSALLEL LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR 
       660        670        680        690        700
DRMEMINVSG YVAQEKLAIA ERYLVPQARA LCGLDESKAK LSSDVLTLLI 
       710        720        730        740        750
KQYCRESGVR NLQKQVEKVL RKSAYKIVSG EAESVEVTPE NLQDFVGKPV 
       760        770        780        790        800
FTVERMYDVT PPGVVMGLAW TAMGGSTLFV ETSLRRPQDK DAKGDKDGSL 
       810        820        830        840        850
EVTGQLGEVM KESARIAYTF ARAFLMQHAP ANDYLVTSHI HLHVPEGATP 
       860        870        880        890        900
KDGPSAGCTI VTALLSLAMG RPVRQNLAMT GEVSLTGKIL PVGGIKEKTI 
       910        920        930        940        950
AAKRAGVTCI VLPAENKKDF YDLAAFITEG LEVHFVEHYR EIFDIAFPDE 

QAEALAVER
Length:959
Mass (Da):106,489
Last modified:December 1, 2000 - v2
Checksum:iB5E03D9C27C220FF
GO
Isoform 2 (identifier: P36776-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     42-105: Missing.

Note: No experimental confirmation available.
Show »
Length:895
Mass (Da):100,397
Checksum:iEF213C4E36C69AE1
GO
Isoform 3 (identifier: P36776-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: Missing.

Note: No experimental confirmation available.
Show »
Length:763
Mass (Da):85,642
Checksum:i3FEBB8DEEA651D7A
GO

Sequence cautioni

The sequence CAA52291 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 55MAAST…PWALW → MAGLWRRALATCDCGERRGA GCCGGRCWPRRGAGSHCSRS VVAPRPADLRRLSSLGTV in AAA61616 (PubMed:8248235).CuratedAdd BLAST55
Sequence conflicti65 – 66WR → CG in AAA61616 (PubMed:8248235).Curated2
Sequence conflicti257 – 258EL → DV in AAA61616 (PubMed:8248235).Curated2
Sequence conflicti423E → G in BAG51690 (PubMed:14702039).Curated1
Sequence conflicti456N → D in AAA61616 (PubMed:8248235).Curated1
Sequence conflicti501I → V in BAG51690 (PubMed:14702039).Curated1
Sequence conflicti556A → T in AAA61616 (PubMed:8248235).Curated1
Sequence conflicti842L → P in AAA61616 (PubMed:8248235).Curated1
Sequence conflicti859T → A in AAA61616 (PubMed:8248235).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05156487E → D. Corresponds to variant dbSNP:rs34413649Ensembl.1
Natural variantiVAR_051565241R → Q. Corresponds to variant dbSNP:rs11085147Ensembl.1
Natural variantiVAR_073338476E → A in CODASS. 1 Publication1
Natural variantiVAR_073339631S → Y in CODASS. 1 PublicationCorresponds to variant dbSNP:rs879255248EnsemblClinVar.1
Natural variantiVAR_073340670A → V in CODASS. 1 PublicationCorresponds to variant dbSNP:rs770036526Ensembl.1
Natural variantiVAR_073341672R → C in CODASS. 1 PublicationCorresponds to variant dbSNP:rs777009012Ensembl.1
Natural variantiVAR_073342676P → S in CODASS. 1 PublicationCorresponds to variant dbSNP:rs879255247EnsemblClinVar.1
Natural variantiVAR_073343679R → H in CODASS. 1 PublicationCorresponds to variant dbSNP:rs549574673EnsemblClinVar.1
Natural variantiVAR_073344721R → G in CODASS. 1 PublicationCorresponds to variant dbSNP:rs147588238Ensembl.1
Natural variantiVAR_073345724A → V in CODASS. 1 PublicationCorresponds to variant dbSNP:rs879255249EnsemblClinVar.1
Natural variantiVAR_073346749P → S in CODASS. 1 Publication1
Natural variantiVAR_073347767G → E in CODASS. 1 PublicationCorresponds to variant dbSNP:rs562553348Ensembl.1
Natural variantiVAR_067708829A → T. Corresponds to variant dbSNP:rs35804229Ensembl.1
Natural variantiVAR_067709911V → I2 PublicationsCorresponds to variant dbSNP:rs1062373Ensembl.1
Natural variantiVAR_073348927Missing in CODASS. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0553101 – 196Missing in isoform 3. 1 PublicationAdd BLAST196
Alternative sequenceiVSP_05461742 – 105Missing in isoform 2. 1 PublicationAdd BLAST64

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02389 mRNA Translation: AAA61616.1
HQ204946 Genomic DNA Translation: ADP90374.1
HQ204947 Genomic DNA Translation: ADP90375.1
HQ204948 Genomic DNA Translation: ADP90376.1
HQ204949 Genomic DNA Translation: ADP90377.1
HQ204950 Genomic DNA Translation: ADP90378.1
HQ204951 Genomic DNA Translation: ADP90379.1
HQ204952 Genomic DNA Translation: ADP90380.1
HQ204953 Genomic DNA Translation: ADP90381.1
HQ204954 Genomic DNA Translation: ADP90382.1
HQ204955 Genomic DNA Translation: ADP90383.1
HQ204956 Genomic DNA Translation: ADP90384.1
HQ204957 Genomic DNA Translation: ADP90385.1
HQ204958 Genomic DNA Translation: ADP90386.1
HQ204959 Genomic DNA Translation: ADP90387.1
HQ204960 Genomic DNA Translation: ADP90388.1
HQ204961 Genomic DNA Translation: ADP90389.1
HQ204962 Genomic DNA Translation: ADP90390.1
HQ204963 Genomic DNA Translation: ADP90391.1
HQ204964 Genomic DNA Translation: ADP90392.1
HQ204965 Genomic DNA Translation: ADP90393.1
HQ204966 Genomic DNA Translation: ADP90394.1
HQ204968 Genomic DNA Translation: ADP90396.1
HQ204969 Genomic DNA Translation: ADP90397.1
HQ204970 Genomic DNA Translation: ADP90398.1
HQ204971 Genomic DNA Translation: ADP90399.1
HQ204972 Genomic DNA Translation: ADP90400.1
HQ204973 Genomic DNA Translation: ADP90401.1
HQ204974 Genomic DNA Translation: ADP90402.1
HQ204975 Genomic DNA Translation: ADP90403.1
HQ204976 Genomic DNA Translation: ADP90404.1
HQ204977 Genomic DNA Translation: ADP90405.1
HQ204978 Genomic DNA Translation: ADP90406.1
HQ204979 Genomic DNA Translation: ADP90407.1
HQ204980 Genomic DNA Translation: ADP90408.1
HQ204981 Genomic DNA Translation: ADP90409.1
HQ204982 Genomic DNA Translation: ADP90410.1
HQ204983 Genomic DNA Translation: ADP90411.1
HQ204984 Genomic DNA Translation: ADP90412.1
HQ204985 Genomic DNA Translation: ADP90413.1
AF059309
, AF059296, AF059297, AF059298, AF059299, AF059300, AF059301, AF059302, AF059303, AF059304, AF059305, AF059306, AF059307, AF059308 Genomic DNA Translation: AAD24414.1
AK056366 mRNA Translation: BAG51690.1
AK096626 mRNA Translation: BAC04829.1
AC011499 Genomic DNA No translation available.
CH471139 Genomic DNA Translation: EAW69151.1
CH471139 Genomic DNA Translation: EAW69154.1
BC000235 mRNA Translation: AAH00235.1
X74215 mRNA Translation: CAA52291.1 Different initiation.
X76040 mRNA Translation: CAA53625.1
CCDSiCCDS12148.1 [P36776-1]
CCDS62507.1 [P36776-3]
CCDS62508.1 [P36776-2]
PIRiS42366
S57342
RefSeqiNP_001263408.1, NM_001276479.1 [P36776-2]
NP_001263409.1, NM_001276480.1 [P36776-3]
NP_004784.2, NM_004793.3 [P36776-1]
UniGeneiHs.350265

Genome annotation databases

EnsembliENST00000360614; ENSP00000353826; ENSG00000196365 [P36776-1]
ENST00000540670; ENSP00000441523; ENSG00000196365 [P36776-3]
ENST00000593119; ENSP00000468541; ENSG00000196365 [P36776-2]
GeneIDi9361
KEGGihsa:9361
UCSCiuc002mcx.5 human [P36776-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLONM_HUMAN
AccessioniPrimary (citable) accession number: P36776
Secondary accession number(s): B3KPH8
, D6W635, E5KMH8, F5GZ27, P36777, Q8N8K8, Q9UQ95
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: July 18, 2018
This is version 184 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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