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Protein

Mitochondrial ubiquitin ligase activator of NFKB 1

Gene

MUL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its ability to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.6 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri302 – 34039RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • signal transducer activity Source: UniProtKB
  • SUMO transferase activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • activation of JUN kinase activity Source: UniProtKB
  • cellular response to exogenous dsRNA Source: UniProtKB
  • mitochondrial fission Source: UniProtKB
  • mitochondrion localization Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of chemokine (C-C motif) ligand 5 production Source: UniProtKB
  • negative regulation of defense response to virus by host Source: UniProtKB
  • negative regulation of innate immune response Source: UniProtKB
  • negative regulation of mitochondrial fusion Source: UniProtKB
  • negative regulation of protein kinase B signaling Source: UniProtKB
  • negative regulation of type I interferon-mediated signaling pathway Source: UniProtKB
  • positive regulation of dendrite extension Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of mitochondrial fission Source: UniProtKB
  • positive regulation of protein sumoylation Source: UniProtKB
  • protein destabilization Source: ParkinsonsUK-UCL
  • protein stabilization Source: UniProtKB
  • protein sumoylation Source: UniProtKB-UniPathway
  • protein ubiquitination Source: UniProtKB
  • regulation of mitochondrial membrane potential Source: Ensembl
  • regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
  • regulation of mitochondrion organization Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
UniPathwayiUPA00143.
UPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial ubiquitin ligase activator of NFKB 1 (EC:6.3.2.-)
Alternative name(s):
E3 SUMO-protein ligase MUL1
E3 ubiquitin-protein ligase MUL1
Growth inhibition and death E3 ligase
Mitochondrial-anchored protein ligase
Short name:
MAPL
Putative NF-kappa-B-activating protein 266
RING finger protein 218
Gene namesi
Name:MUL1
Synonyms:C1orf166, GIDE, MAPL, MULAN, RNF218
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25762. MUL1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysis
Transmembranei9 – 2921HelicalSequence analysisAdd
BLAST
Topological domaini30 – 238209Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Topological domaini260 – 35293CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: ParkinsonsUK-UCL
  • cytoplasm Source: HPA
  • integral component of mitochondrial outer membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: LIFEdb
  • neuronal cell body Source: ParkinsonsUK-UCL
  • nucleoplasm Source: HPA
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi260 – 2601R → A: Protein is targeted to the ER; when associated with A-261. 1 Publication
Mutagenesisi261 – 2611K → A: Protein is targeted to the ER; when associated with A-260. 1 Publication
Mutagenesisi319 – 3191H → A: Abolishes ligase activity. No effect on mitochondrial localization. 1 Publication
Mutagenesisi339 – 3391C → A: Abolishes ligase activity. 1 Publication

Organism-specific databases

PharmGKBiPA162396329.

Polymorphism and mutation databases

BioMutaiMUL1.
DMDMi74760689.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Mitochondrial ubiquitin ligase activator of NFKB 1PRO_0000277660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki52 – 52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki273 – 273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki299 – 299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ969V5.
MaxQBiQ969V5.
PaxDbiQ969V5.
PRIDEiQ969V5.

PTM databases

iPTMnetiQ969V5.
PhosphoSiteiQ969V5.

Expressioni

Tissue specificityi

Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus.2 Publications

Gene expression databases

BgeeiQ969V5.
CleanExiHS_MUL1.
ExpressionAtlasiQ969V5. baseline and differential.
GenevisibleiQ969V5. HS.

Organism-specific databases

HPAiHPA017681.
HPA026827.

Interactioni

Subunit structurei

Homooligomer. Interacts with MAP3K7/TAK1. Interacts with UBC9. Interacts with MAVS.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-744120,EBI-743771
TRIM9Q9C0263EBI-744120,EBI-720828

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122734. 46 interactions.
IntActiQ969V5. 16 interactions.
MINTiMINT-1464078.
STRINGi9606.ENSP00000264198.

Structurei

3D structure databases

ProteinModelPortaliQ969V5.
SMRiQ969V5. Positions 300-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The zinc finger domain is required for E3 ligase activity.

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri302 – 34039RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1571. Eukaryota.
ENOG410YF4M. LUCA.
GeneTreeiENSGT00390000012141.
HOGENOMiHOG000007562.
HOVERGENiHBG106376.
InParanoidiQ969V5.
KOiK15688.
OMAiVCSCAEC.
OrthoDBiEOG7B31N9.
PhylomeDBiQ969V5.
TreeFamiTF325195.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR022170. MULAN.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF12483. GIDE. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q969V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESGGRPSLC QFILLGTTSV VTAALYSVYR QKARVSQELK GAKKVHLGED
60 70 80 90 100
LKSILSEAPG KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLTLQEHK
110 120 130 140 150
MVWNRTTHLW NDCSKIIHQR TNTVPFDLVP HEDGVDVAVR VLKPLDSVDL
160 170 180 190 200
GLETVYEKFH PSIQSFTDVI GHYISGERPK GIQETEEMLK VGATLTGVGE
210 220 230 240 250
LVLDNNSVRL QPPKQGMQYY LSSQDFDSLL QRQESSVRLW KVLALVFGFA
260 270 280 290 300
TCATLFFILR KQYLQRQERL RLKQMQEEFQ EHEAQLLSRA KPEDRESLKS
310 320 330 340 350
ACVVCLSSFK SCVFLECGHV CSCTECYRAL PEPKKCPICR QAITRVIPLY

NS
Length:352
Mass (Da):39,800
Last modified:December 1, 2001 - v1
Checksum:i6EF2B8BBFCE1801F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti240 – 2401W → C in BAB14317 (PubMed:14702039).Curated
Sequence conflicti349 – 3491L → P in ACH72645 (PubMed:18591963).Curated
Sequence conflicti349 – 3491L → P in BAC77368 (PubMed:12761501).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU935008 mRNA. Translation: ACH72645.1.
AB097015 mRNA. Translation: BAC77368.1.
AK022937 mRNA. Translation: BAB14317.1.
AL833889 mRNA. Translation: CAD38745.1.
AL391357 Genomic DNA. Translation: CAH73470.1.
BC010101 mRNA. Translation: AAH10101.1.
BC014010 mRNA. Translation: AAH14010.1.
CCDSiCCDS208.1.
RefSeqiNP_078820.2. NM_024544.2.
UniGeneiHs.10101.

Genome annotation databases

EnsembliENST00000264198; ENSP00000264198; ENSG00000090432.
GeneIDi79594.
KEGGihsa:79594.
UCSCiuc001bdi.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU935008 mRNA. Translation: ACH72645.1.
AB097015 mRNA. Translation: BAC77368.1.
AK022937 mRNA. Translation: BAB14317.1.
AL833889 mRNA. Translation: CAD38745.1.
AL391357 Genomic DNA. Translation: CAH73470.1.
BC010101 mRNA. Translation: AAH10101.1.
BC014010 mRNA. Translation: AAH14010.1.
CCDSiCCDS208.1.
RefSeqiNP_078820.2. NM_024544.2.
UniGeneiHs.10101.

3D structure databases

ProteinModelPortaliQ969V5.
SMRiQ969V5. Positions 300-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122734. 46 interactions.
IntActiQ969V5. 16 interactions.
MINTiMINT-1464078.
STRINGi9606.ENSP00000264198.

PTM databases

iPTMnetiQ969V5.
PhosphoSiteiQ969V5.

Polymorphism and mutation databases

BioMutaiMUL1.
DMDMi74760689.

Proteomic databases

EPDiQ969V5.
MaxQBiQ969V5.
PaxDbiQ969V5.
PRIDEiQ969V5.

Protocols and materials databases

DNASUi79594.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264198; ENSP00000264198; ENSG00000090432.
GeneIDi79594.
KEGGihsa:79594.
UCSCiuc001bdi.5. human.

Organism-specific databases

CTDi79594.
GeneCardsiMUL1.
HGNCiHGNC:25762. MUL1.
HPAiHPA017681.
HPA026827.
MIMi612037. gene.
neXtProtiNX_Q969V5.
PharmGKBiPA162396329.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1571. Eukaryota.
ENOG410YF4M. LUCA.
GeneTreeiENSGT00390000012141.
HOGENOMiHOG000007562.
HOVERGENiHBG106376.
InParanoidiQ969V5.
KOiK15688.
OMAiVCSCAEC.
OrthoDBiEOG7B31N9.
PhylomeDBiQ969V5.
TreeFamiTF325195.

Enzyme and pathway databases

UniPathwayiUPA00143.
UPA00886.
BRENDAi6.3.2.19. 2681.

Miscellaneous databases

GenomeRNAii79594.
NextBioi68610.
PROiQ969V5.
SOURCEiSearch...

Gene expression databases

BgeeiQ969V5.
CleanExiHS_MUL1.
ExpressionAtlasiQ969V5. baseline and differential.
GenevisibleiQ969V5. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR022170. MULAN.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF12483. GIDE. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and slows growth."
    Zhang B., Huang J., Li H.-L., Liu T., Wang Y.-Y., Waterman P., Mao A.-P., Xu L.-G., Zhai Z., Liu D., Marrack P., Shu H.-B.
    Cell Res. 18:900-910(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH MAP3K7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-319.
  2. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
    Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
    Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Melanoma.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Skin.
  7. "Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers."
    Neuspiel M., Schauss A.C., Braschi E., Zunino R., Rippstein P., Rachubinski R.A., Andrade-Navarro M.A., McBride H.M.
    Curr. Biol. 18:102-108(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.
  8. "Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling."
    Li W., Bengtson M.H., Ulbrich A., Matsuda A., Reddy V.A., Orth A., Chanda S.K., Batalov S., Joazeiro C.A.P.
    PLoS ONE 3:E1487-E1487(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOPOLOGY, MUTAGENESIS OF ARG-260; LYS-261 AND CYS-339.
  9. "MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission."
    Braschi E., Zunino R., McBride H.M.
    EMBO Rep. 10:748-754(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SUMO LIGASE, INTERACTION WITH UBC9 AND DNM1L.
  10. Cited for: FUNCTION IN UBIQUITINATION OF AKT1.
  11. Cited for: FUNCTION, INTERACTION WITH MAVS.
  12. "USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria."
    Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M., Kirkpatrick D.S., Bingol B., Corn J.E.
    Nat. Cell Biol. 17:160-169(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-52; LYS-273 AND LYS-299.

Entry informationi

Entry nameiMUL1_HUMAN
AccessioniPrimary (citable) accession number: Q969V5
Secondary accession number(s): B5M497, Q7Z431, Q9H9B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.