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Q9UBG0

- MRC2_HUMAN

UniProt

Q9UBG0 - MRC2_HUMAN

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Protein
C-type mannose receptor 2
Gene
MRC2, CLEC13E, ENDO180, KIAA0709, UPARAP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).2 Publications

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. collagen binding Source: UniProt
  3. protein binding Source: UniProt

GO - Biological processi

  1. collagen catabolic process Source: UniProt
  2. endocytosis Source: UniProtKB-KW
  3. osteoblast differentiation Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Lectin

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).

Protein family/group databases

MEROPSiI63.001.

Names & Taxonomyi

Protein namesi
Recommended name:
C-type mannose receptor 2
Alternative name(s):
C-type lectin domain family 13 member E
Endocytic receptor 180
Macrophage mannose receptor 2
Urokinase-type plasminogen activator receptor-associated protein
Short name:
UPAR-associated protein
Short name:
Urokinase receptor-associated protein
CD_antigen: CD280
Gene namesi
Name:MRC2
Synonyms:CLEC13E, ENDO180, KIAA0709, UPARAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:16875. MRC2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 14141384Extracellular Reviewed prediction
Add
BLAST
Transmembranei1415 – 143521Helical; Reviewed prediction
Add
BLAST
Topological domaini1436 – 147944Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi472 – 4721N → D: Reduced sugar-binding activity. 1 Publication
Mutagenesisi1452 – 14521Y → A: No alteration of distribution and trafficking. 1 Publication
Mutagenesisi1464 – 14641E → A: Increased cell surface distribution. 1 Publication
Mutagenesisi1468 – 14692LV → AA: Reduction of endocytotic activity; distribution almost restricted to the cell surface.

Organism-specific databases

PharmGKBiPA134988161.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030 Reviewed prediction
Add
BLAST
Chaini31 – 14791449C-type mannose receptor 2
PRO_0000046078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 68 By similarity
Glycosylationi69 – 691N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi93 ↔ 112 By similarity
Glycosylationi140 – 1401N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi187 ↔ 213 By similarity
Disulfide bondi201 ↔ 228 By similarity
Disulfide bondi266 ↔ 359 By similarity
Disulfide bondi335 ↔ 351 By similarity
Glycosylationi364 – 3641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi410 ↔ 504 By similarity
Disulfide bondi481 ↔ 496 By similarity
Glycosylationi588 – 5881N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi618 ↔ 635 By similarity
Disulfide bondi704 ↔ 808 By similarity
Disulfide bondi785 ↔ 800 By similarity
Disulfide bondi853 ↔ 950 By similarity
Disulfide bondi927 ↔ 942 By similarity
Glycosylationi954 – 9541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1029 – 10291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1078 ↔ 1098 By similarity
Cross-linki1142 – 1142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)1 Publication
Disulfide bondi1220 ↔ 1234 By similarity
Glycosylationi1350 – 13501N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1369 ↔ 1384 By similarity

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UBG0.
PaxDbiQ9UBG0.
PRIDEiQ9UBG0.

PTM databases

PhosphoSiteiQ9UBG0.

Expressioni

Tissue specificityi

Ubiquitous with low expression in brain, placenta, lung, kidney, pancreas, spleen, thymus and colon. Expressed in endothelial cells, fibroblasts and macrophages. Highly expressed in fetal lung and kidney.2 Publications

Gene expression databases

ArrayExpressiQ9UBG0.
BgeeiQ9UBG0.
CleanExiHS_MRC2.
GenevestigatoriQ9UBG0.

Organism-specific databases

HPAiHPA041991.

Interactioni

Subunit structurei

Interacts with C-terminal region of type I collagen/COL1A1 By similarity. Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a tri-molecular complex. Interacts with collagen V.1 Publication

Protein-protein interaction databases

BioGridi115231. 3 interactions.
IntActiQ9UBG0. 1 interaction.
STRINGi9606.ENSP00000307513.

Structurei

3D structure databases

ProteinModelPortaliQ9UBG0.
SMRiQ9UBG0. Positions 161-361, 381-645, 681-811, 828-952, 972-1109, 1132-1235, 1260-1396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 167127Ricin B-type lectin
Add
BLAST
Domaini182 – 23049Fibronectin type-II
Add
BLAST
Domaini244 – 360117C-type lectin 1
Add
BLAST
Domaini389 – 505117C-type lectin 2
Add
BLAST
Domaini528 – 644117C-type lectin 3
Add
BLAST
Domaini678 – 809132C-type lectin 4
Add
BLAST
Domaini832 – 951120C-type lectin 5
Add
BLAST
Domaini979 – 1107129C-type lectin 6
Add
BLAST
Domaini1132 – 1243112C-type lectin 7
Add
BLAST
Domaini1273 – 1393121C-type lectin 8
Add
BLAST

Domaini

C-type lectin domains 3 to 8 are not required for calcium-dependent binding of mannose, fucose and N-acetylglucosamine. C-type lectin domain 2 is responsible for sugar-binding in a calcium-dependent manner.2 Publications
Fibronectin type-II domain mediates collagen-binding.2 Publications
Ricin B-type lectin domain contacts with the second C-type lectin domain By similarity.2 Publications

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG288621.
HOGENOMiHOG000231191.
HOVERGENiHBG053606.
InParanoidiQ9UBG0.
KOiK06560.
OMAiMEMNEQQ.
OrthoDBiEOG7FFMQR.
PhylomeDBiQ9UBG0.
TreeFamiTF316663.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTiSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 3 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UBG0-1 [UniParc]FASTAAdd to Basket

« Hide

MGPGRPAPAP WPRHLLRCVL LLGCLHLGRP GAPGDAALPE PNVFLIFSHG     50
LQGCLEAQGG QVRVTPACNT SLPAQRWKWV SRNRLFNLGT MQCLGTGWPG 100
TNTTASLGMY ECDREALNLR WHCRTLGDQL SLLLGARTSN ISKPGTLERG 150
DQTRSGQWRI YGSEEDLCAL PYHEVYTIQG NSHGKPCTIP FKYDNQWFHG 200
CTSTGREDGH LWCATTQDYG KDERWGFCPI KSNDCETFWD KDQLTDSCYQ 250
FNFQSTLSWR EAWASCEQQG ADLLSITEIH EQTYINGLLT GYSSTLWIGL 300
NDLDTSGGWQ WSDNSPLKYL NWESDQPDNP SEENCGVIRT ESSGGWQNRD 350
CSIALPYVCK KKPNATAEPT PPDRWANVKV ECEPSWQPFQ GHCYRLQAEK 400
RSWQESKKAC LRGGGDLVSI HSMAELEFIT KQIKQEVEEL WIGLNDLKLQ 450
MNFEWSDGSL VSFTHWHPFE PNNFRDSLED CVTIWGPEGR WNDSPCNQSL 500
PSICKKAGQL SQGAAEEDHG CRKGWTWHSP SCYWLGEDQV TYSEARRLCT 550
DHGSQLVTIT NRFEQAFVSS LIYNWEGEYF WTALQDLNST GSFFWLSGDE 600
VMYTHWNRDQ PGYSRGGCVA LATGSAMGLW EVKNCTSFRA RYICRQSLGT 650
PVTPELPGPD PTPSLTGSCP QGWASDTKLR YCYKVFSSER LQDKKSWVQA 700
QGACQELGAQ LLSLASYEEE HFVANMLNKI FGESEPEIHE QHWFWIGLNR 750
RDPRGGQSWR WSDGVGFSYH NFDRSRHDDD DIRGCAVLDL ASLQWVAMQC 800
DTQLDWICKI PRGTDVREPD DSPQGRREWL RFQEAEYKFF EHHSTWAQAQ 850
RICTWFQAEL TSVHSQAELD FLSHNLQKFS RAQEQHWWIG LHTSESDGRF 900
RWTDGSIINF ISWAPGKPRP VGKDKKCVYM TASREDWGDQ RCLTALPYIC 950
KRSNVTKETQ PPDLPTTALG GCPSDWIQFL NKCFQVQGQE PQSRVKWSEA 1000
QFSCEQQEAQ LVTITNPLEQ AFITASLPNV TFDLWIGLHA SQRDFQWVEQ 1050
EPLMYANWAP GEPSGPSPAP SGNKPTSCAV VLHSPSAHFT GRWDDRSCTE 1100
ETHGFICQKG TDPSLSPSPA ALPPAPGTEL SYLNGTFRLL QKPLRWHDAL 1150
LLCESRNASL AYVPDPYTQA FLTQAARGLR TPLWIGLAGE EGSRRYSWVS 1200
EEPLNYVGWQ DGEPQQPGGC TYVDVDGAWR TTSCDTKLQG AVCGVSSGPP 1250
PPRRISYHGS CPQGLADSAW IPFREHCYSF HMELLLGHKE ARQRCQRAGG 1300
AVLSILDEME NVFVWEHLQS YEGQSRGAWL GMNFNPKGGT LVWQDNTAVN 1350
YSNWGPPGLG PSMLSHNSCY WIQSNSGLWR PGACTNITMG VVCKLPRAEQ 1400
SSFSPSALPE NPAALVVVLM AVLLLLALLT AALILYRRRQ SIERGAFEGA 1450
RYSRSSSSPT EATEKNILVS DMEMNEQQE 1479
Length:1,479
Mass (Da):166,674
Last modified:January 11, 2011 - v2
Checksum:iAAAA5286F91DF7E7
GO

Sequence cautioni

The sequence BAA31684.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431V → I.1 Publication
Corresponds to variant rs2014055 [ dbSNP | Ensembl ].
VAR_025304
Natural varianti1156 – 11561R → H.5 Publications
Corresponds to variant rs2429387 [ dbSNP | Ensembl ].
VAR_025305

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF107292 mRNA. Translation: AAF14192.1.
AF134838 mRNA. Translation: AAD30280.1.
AB014609 mRNA. Translation: BAA31684.2. Different initiation.
AC080038 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94341.1.
CH471109 Genomic DNA. Translation: EAW94342.1.
BC146647 mRNA. Translation: AAI46648.1.
BC150212 mRNA. Translation: AAI50213.1.
BC153884 mRNA. Translation: AAI53885.1.
CCDSiCCDS11634.1.
RefSeqiNP_006030.2. NM_006039.4.
UniGeneiHs.7835.

Genome annotation databases

EnsembliENST00000303375; ENSP00000307513; ENSG00000011028.
GeneIDi9902.
KEGGihsa:9902.
UCSCiuc002jad.4. human.

Polymorphism databases

DMDMi317373394.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Endo180

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF107292 mRNA. Translation: AAF14192.1 .
AF134838 mRNA. Translation: AAD30280.1 .
AB014609 mRNA. Translation: BAA31684.2 . Different initiation.
AC080038 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94341.1 .
CH471109 Genomic DNA. Translation: EAW94342.1 .
BC146647 mRNA. Translation: AAI46648.1 .
BC150212 mRNA. Translation: AAI50213.1 .
BC153884 mRNA. Translation: AAI53885.1 .
CCDSi CCDS11634.1.
RefSeqi NP_006030.2. NM_006039.4.
UniGenei Hs.7835.

3D structure databases

ProteinModelPortali Q9UBG0.
SMRi Q9UBG0. Positions 161-361, 381-645, 681-811, 828-952, 972-1109, 1132-1235, 1260-1396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115231. 3 interactions.
IntActi Q9UBG0. 1 interaction.
STRINGi 9606.ENSP00000307513.

Protein family/group databases

MEROPSi I63.001.

PTM databases

PhosphoSitei Q9UBG0.

Polymorphism databases

DMDMi 317373394.

Proteomic databases

MaxQBi Q9UBG0.
PaxDbi Q9UBG0.
PRIDEi Q9UBG0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303375 ; ENSP00000307513 ; ENSG00000011028 .
GeneIDi 9902.
KEGGi hsa:9902.
UCSCi uc002jad.4. human.

Organism-specific databases

CTDi 9902.
GeneCardsi GC17P060704.
H-InvDB HIX0018596.
HIX0027238.
HGNCi HGNC:16875. MRC2.
HPAi HPA041991.
MIMi 612264. gene.
neXtProti NX_Q9UBG0.
PharmGKBi PA134988161.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG288621.
HOGENOMi HOG000231191.
HOVERGENi HBG053606.
InParanoidi Q9UBG0.
KOi K06560.
OMAi MEMNEQQ.
OrthoDBi EOG7FFMQR.
PhylomeDBi Q9UBG0.
TreeFami TF316663.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).

Miscellaneous databases

ChiTaRSi MRC2. human.
GenomeRNAii 9902.
NextBioi 37337.
PROi Q9UBG0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBG0.
Bgeei Q9UBG0.
CleanExi HS_MRC2.
Genevestigatori Q9UBG0.

Family and domain databases

Gene3Di 2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view ]
SMARTi SM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEi PS00615. C_TYPE_LECTIN_1. 3 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A urokinase receptor-associated protein with specific collagen binding properties."
    Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.
    J. Biol. Chem. 275:1993-2002(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 350-360, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, VARIANT HIS-1156.
  2. "Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor."
    Sheikh H., Yarwood H., Ashworth A., Isacke C.M.
    J. Cell Sci. 113:1021-1032(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, GLYCOSYLATION, TISSUE SPECIFICITY, VARIANTS ILE-43 AND HIS-1156.
  3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-1156.
    Tissue: Brain.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-1156.
  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], VARIANT HIS-1156.
  7. "Characterization of a novel member of the macrophage mannose receptor type C lectin family."
    Wu K., Yuan J., Lasky L.A.
    J. Biol. Chem. 271:21323-21330(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "The C-type lectin receptor Endo180 displays internalization and recycling properties distinct from other members of the mannose receptor family."
    Howard M.J., Isacke C.M.
    J. Biol. Chem. 277:32320-32331(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-1452; GLU-1464 AND 1468-LEU-VAL-1469.
  9. "Characterization of sugar binding by the mannose receptor family member, Endo180."
    East L., Rushton S., Taylor M.E., Isacke C.M.
    J. Biol. Chem. 277:50469-50475(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF ASN-472.
  10. "Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor."
    Wienke D., MacFadyen J.R., Isacke C.M.
    Mol. Biol. Cell 14:3592-3604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
    Tissue: Liver.
  12. Cited for: GLYCOSYLATION AT ASN-69.
  13. "In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
    Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
    J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-1142.
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiMRC2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBG0
Secondary accession number(s): A6H8K4
, D3DU08, Q7LGE7, Q9Y5P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 105 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi