Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitochondrial amidoxime reducing component 2

Gene

MARC2

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

Functioni

As a component of the benzamidoxime prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively.1 Publication

Cofactori

Mo-molybdopterin1 PublicationNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.1 Publication

Kineticsi

  1. KM=830 µM for benzamidoxime2 Publications
  2. KM=400 µM for benzamidoxime (at pH 6.0 and 37 degrees Celsius)1 Publication
  3. KM=3 mM for NOHA2 Publications
  4. KM=3.7 mM for NHAM2 Publications
  1. Vmax=307 nmol/min/mg enzyme toward benzamidoxime2 Publications
  2. Vmax=119 nmol/min/mg enzyme toward benzamidoxime (at pH 6.0 and 37 degrees Celsius)1 Publication
  3. Vmax=373 nmol/min/mg enzyme toward NOHA2 Publications
  4. Vmax=36.5 nmol/min/mg enzyme toward NHAM2 Publications

GO - Molecular functioni

  • molybdenum ion binding Source: UniProtKB
  • molybdopterin cofactor binding Source: UniProtKB
  • nitrate reductase activity Source: UniProtKB
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • detoxification of nitrogen compound Source: UniProtKB
  • nitrate metabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Molybdenum

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial amidoxime reducing component 2 (EC:1.-.-.-)
Short name:
mARC2
Alternative name(s):
Molybdenum cofactor sulfurase C-terminal domain-containing protein 2
Short name:
MOSC domain-containing protein 2
Short name:
Moco sulfurase C-terminal domain-containing protein 2
Gene namesi
Name:MARC2
Synonyms:MOSC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:26064. MARC2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671345.

Polymorphism and mutation databases

BioMutaiMARC2.
DMDMi74760692.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionSequence analysisAdd
BLAST
Chaini36 – 335300Mitochondrial amidoxime reducing component 2PRO_0000273340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki138 – 138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki144 – 144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei156 – 1561N6-acetyllysine; alternateBy similarity
Cross-linki156 – 156Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki166 – 166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki173 – 173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki187 – 187Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki287 – 287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki294 – 294Glycyl 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

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ969Z3.
MaxQBiQ969Z3.
PaxDbiQ969Z3.
PeptideAtlasiQ969Z3.
PRIDEiQ969Z3.

PTM databases

iPTMnetiQ969Z3.
PhosphoSiteiQ969Z3.

Expressioni

Gene expression databases

BgeeiQ969Z3.
CleanExiHS_MOSC2.
ExpressionAtlasiQ969Z3. baseline and differential.
GenevisibleiQ969Z3. HS.

Organism-specific databases

HPAiHPA015085.
HPA017572.

Interactioni

Subunit structurei

Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MARC2.By similarity

Protein-protein interaction databases

BioGridi120329. 3 interactions.
MINTiMINT-3050401.
STRINGi9606.ENSP00000355880.

Structurei

3D structure databases

ProteinModelPortaliQ969Z3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini188 – 334147MOSCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MOSC domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2362. Eukaryota.
COG3217. LUCA.
GeneTreeiENSGT00530000063150.
HOVERGENiHBG081982.
InParanoidiQ969Z3.
OMAiTRIEKKM.
PhylomeDBiQ969Z3.
TreeFamiTF316807.

Family and domain databases

InterProiIPR005302. MoCF_Sase_C.
IPR005303. MOSC_N.
IPR011037. Pyrv_Knase-like_insert_dom.
[Graphical view]
PfamiPF03473. MOSC. 1 hit.
PF03476. MOSC_N. 1 hit.
[Graphical view]
SUPFAMiSSF50800. SSF50800. 2 hits.
PROSITEiPS51340. MOSC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q969Z3-1) [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
MGASSSSALA RLGLPARPWP RWLGVAALGL AAVALGTVAW RRAWPRRRRR
60 70 80 90 100
LQQVGTVAKL WIYPVKSCKG VPVSEAECTA MGLRSGNLRD RFWLVIKEDG
110 120 130 140 150
HMVTARQEPR LVLISIIYEN NCLIFRAPDM DQLVLPSKQP SSNKLHNCRI
160 170 180 190 200
FGLDIKGRDC GNEAAKWFTN FLKTEAYRLV QFETNMKGRT SRKLLPTLDQ
210 220 230 240 250
NFQVAYPDYC PLLIMTDASL VDLNTRMEKK MKMENFRPNI VVTGCDAFEE
260 270 280 290 300
DTWDELLIGS VEVKKVMACP RCILTTVDPD TGVIDRKQPL DTLKSYRLCD
310 320 330
PSERELYKLS PLFGIYYSVE KIGSLRVGDP VYRMV
Length:335
Mass (Da):38,023
Last modified:December 1, 2001 - v1
Checksum:i4C6A9B8B9AC0F74D
GO
Isoform 2 (identifier: Q969Z3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     251-257: DTWDELL → ASATRRD
     258-335: Missing.

Note: No experimental confirmation available.
Show »
Length:257
Mass (Da):29,103
Checksum:i8938E1231A0ACB9B
GO

Sequence cautioni

The sequence BAA91287.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH70306.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH71880.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691T → A in CAL38507 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31A → S.1 Publication
Corresponds to variant rs72472370 [ dbSNP | Ensembl ].
VAR_062275
Natural varianti244 – 2441G → S Decreased catalytic efficiency toward benzamidoxime; no effect on affinity for benzamidoxime; no effect on binding of the molybdenum cofactor. 2 Publications
Corresponds to variant rs3795535 [ dbSNP | Ensembl ].
VAR_030133
Natural varianti245 – 2451C → W Decreased catalytic activity toward benzamidoxime; no effect on affinity for benzamidoxime; no effect on binding of the molybdenum cofactor. 1 Publication
Corresponds to variant rs76664695 [ dbSNP | Ensembl ].
VAR_070777

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei251 – 2577DTWDELL → ASATRRD in isoform 2. 1 PublicationVSP_022513
Alternative sequencei258 – 33578Missing in isoform 2. 1 PublicationVSP_022514Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136931 mRNA. Translation: CAB66865.1.
AM393631 mRNA. Translation: CAL38507.1.
EU567145 Genomic DNA. Translation: ACB21048.1.
AL606726, AL359353 Genomic DNA. Translation: CAH71878.1.
AL606726, AL359353 Genomic DNA. Translation: CAH71879.1.
AL606726, AL359353 Genomic DNA. Translation: CAH71880.1. Sequence problems.
AL359353, AL606726 Genomic DNA. Translation: CAH70303.1.
AL359353, AL606726 Genomic DNA. Translation: CAH70304.1.
AL359353, AL606726 Genomic DNA. Translation: CAH70306.1. Sequence problems.
CH471100 Genomic DNA. Translation: EAW93293.1.
CH471100 Genomic DNA. Translation: EAW93294.1.
BC011973 mRNA. Translation: AAH11973.1.
BC015829 mRNA. Translation: AAH15829.2.
BC016859 mRNA. Translation: AAH16859.1.
AK000612 mRNA. Translation: BAA91287.1. Different initiation.
CCDSiCCDS1525.1. [Q969Z3-1]
RefSeqiNP_001304267.1. NM_001317338.1. [Q969Z3-1]
NP_060368.2. NM_017898.4. [Q969Z3-1]
UniGeneiHs.369042.

Genome annotation databases

EnsembliENST00000359316; ENSP00000352266; ENSG00000117791. [Q969Z3-2]
ENST00000366913; ENSP00000355880; ENSG00000117791. [Q969Z3-1]
GeneIDi54996.
KEGGihsa:54996.
UCSCiuc001hmq.4. human. [Q969Z3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136931 mRNA. Translation: CAB66865.1.
AM393631 mRNA. Translation: CAL38507.1.
EU567145 Genomic DNA. Translation: ACB21048.1.
AL606726, AL359353 Genomic DNA. Translation: CAH71878.1.
AL606726, AL359353 Genomic DNA. Translation: CAH71879.1.
AL606726, AL359353 Genomic DNA. Translation: CAH71880.1. Sequence problems.
AL359353, AL606726 Genomic DNA. Translation: CAH70303.1.
AL359353, AL606726 Genomic DNA. Translation: CAH70304.1.
AL359353, AL606726 Genomic DNA. Translation: CAH70306.1. Sequence problems.
CH471100 Genomic DNA. Translation: EAW93293.1.
CH471100 Genomic DNA. Translation: EAW93294.1.
BC011973 mRNA. Translation: AAH11973.1.
BC015829 mRNA. Translation: AAH15829.2.
BC016859 mRNA. Translation: AAH16859.1.
AK000612 mRNA. Translation: BAA91287.1. Different initiation.
CCDSiCCDS1525.1. [Q969Z3-1]
RefSeqiNP_001304267.1. NM_001317338.1. [Q969Z3-1]
NP_060368.2. NM_017898.4. [Q969Z3-1]
UniGeneiHs.369042.

3D structure databases

ProteinModelPortaliQ969Z3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120329. 3 interactions.
MINTiMINT-3050401.
STRINGi9606.ENSP00000355880.

PTM databases

iPTMnetiQ969Z3.
PhosphoSiteiQ969Z3.

Polymorphism and mutation databases

BioMutaiMARC2.
DMDMi74760692.

Proteomic databases

EPDiQ969Z3.
MaxQBiQ969Z3.
PaxDbiQ969Z3.
PeptideAtlasiQ969Z3.
PRIDEiQ969Z3.

Protocols and materials databases

DNASUi54996.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359316; ENSP00000352266; ENSG00000117791. [Q969Z3-2]
ENST00000366913; ENSP00000355880; ENSG00000117791. [Q969Z3-1]
GeneIDi54996.
KEGGihsa:54996.
UCSCiuc001hmq.4. human. [Q969Z3-1]

Organism-specific databases

CTDi54996.
GeneCardsiMARC2.
HGNCiHGNC:26064. MARC2.
HPAiHPA015085.
HPA017572.
MIMi614127. gene.
neXtProtiNX_Q969Z3.
PharmGKBiPA142671345.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2362. Eukaryota.
COG3217. LUCA.
GeneTreeiENSGT00530000063150.
HOVERGENiHBG081982.
InParanoidiQ969Z3.
OMAiTRIEKKM.
PhylomeDBiQ969Z3.
TreeFamiTF316807.

Miscellaneous databases

ChiTaRSiMARC2. human.
GeneWikiiMOSC2.
GenomeRNAii54996.
PROiQ969Z3.
SOURCEiSearch...

Gene expression databases

BgeeiQ969Z3.
CleanExiHS_MOSC2.
ExpressionAtlasiQ969Z3. baseline and differential.
GenevisibleiQ969Z3. HS.

Family and domain databases

InterProiIPR005302. MoCF_Sase_C.
IPR005303. MOSC_N.
IPR011037. Pyrv_Knase-like_insert_dom.
[Graphical view]
PfamiPF03473. MOSC. 1 hit.
PF03476. MOSC_N. 1 hit.
[Graphical view]
SUPFAMiSSF50800. SSF50800. 2 hits.
PROSITEiPS51340. MOSC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Uterus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. NIEHS SNPs program
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-3 AND SER-244.
  4. "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].
  5. 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: Cervix, Colon and Lung.
  7. "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] OF 193-335.
    Tissue: Carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Reduction of N(omega)-hydroxy-L-arginine by the mitochondrial amidoxime reducing component (mARC)."
    Kotthaus J., Wahl B., Havemeyer A., Kotthaus J., Schade D., Garbe-Schonberg D., Mendel R., Bittner F., Clement B.
    Biochem. J. 433:383-391(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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-59; LYS-138; LYS-144; LYS-156; LYS-166; LYS-173; LYS-187; LYS-287 AND LYS-294.
  12. "Functional characterization of protein variants encoded by non-synonymous SNPs in MARC1 and MARC2 in healthy Caucasians."
    Ott G., Reichmann D., Boerger C., Cascorbi I., Bittner F., Mendel R.R., Kunze T., Clement B., Havemeyer A.
    Drug Metab. Dispos. 42:718-725(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-244 AND TRP-245, CHARACTERIZATION OF VARIANTS SER-244 AND TRP-245, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.

Entry informationi

Entry nameiMARC2_HUMAN
AccessioniPrimary (citable) accession number: Q969Z3
Secondary accession number(s): B2D0R5
, D3DTB3, Q0JSK7, Q5VT67, Q5VXC7, Q7L317, Q9H066, Q9NWU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 118 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. 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. 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.