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Protein

C-type mannose receptor 2

Gene

MRC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • collagen catabolic process Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • osteoblast differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Lectin

Enzyme and pathway databases

BioCyciZFISH:ENSG00000011028-MONOMER.
ReactomeiR-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:16875. MRC2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 1414ExtracellularSequence analysisAdd BLAST1384
Transmembranei1415 – 1435HelicalSequence analysisAdd BLAST21
Topological domaini1436 – 1479CytoplasmicSequence analysisAdd BLAST44

GO - Cellular componenti

  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi472N → D: Reduced sugar-binding activity. 1 Publication1
Mutagenesisi1452Y → A: No alteration of distribution and trafficking. 1 Publication1
Mutagenesisi1464E → A: Increased cell surface distribution. 1 Publication1
Mutagenesisi1468 – 1469LV → AA: Reduction of endocytotic activity; distribution almost restricted to the cell surface. 1 Publication2

Organism-specific databases

DisGeNETi9902.
OpenTargetsiENSG00000011028.
PharmGKBiPA134988161.

Polymorphism and mutation databases

BioMutaiMRC2.
DMDMi317373394.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000004607831 – 1479C-type mannose receptor 2Add BLAST1449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 68By similarity
Glycosylationi69N-linked (GlcNAc...) (complex)2 Publications1
Disulfide bondi93 ↔ 112By similarity
Glycosylationi140N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi187 ↔ 213By similarity
Disulfide bondi201 ↔ 228By similarity
Disulfide bondi266 ↔ 359By similarity
Disulfide bondi335 ↔ 351By similarity
Glycosylationi364N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi410 ↔ 504By similarity
Disulfide bondi481 ↔ 496By similarity
Glycosylationi588N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi618 ↔ 635By similarity
Disulfide bondi704 ↔ 808By similarity
Disulfide bondi785 ↔ 800By similarity
Disulfide bondi853 ↔ 950By similarity
Disulfide bondi927 ↔ 942By similarity
Glycosylationi954N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1029N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1078 ↔ 1098By similarity
Cross-linki1142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Disulfide bondi1220 ↔ 1234By similarity
Glycosylationi1350N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1369 ↔ 1384By similarity

Post-translational modificationi

N-glycosylated.3 Publications

Keywords - PTMi

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

Proteomic databases

EPDiQ9UBG0.
MaxQBiQ9UBG0.
PaxDbiQ9UBG0.
PeptideAtlasiQ9UBG0.
PRIDEiQ9UBG0.

PTM databases

iPTMnetiQ9UBG0.
PhosphoSitePlusiQ9UBG0.
SwissPalmiQ9UBG0.
UniCarbKBiQ9UBG0.

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

BgeeiENSG00000011028.
CleanExiHS_MRC2.
ExpressionAtlasiQ9UBG0. baseline and differential.
GenevisibleiQ9UBG0. HS.

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.By similarity1 Publication

GO - Molecular functioni

  • collagen binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115231. 25 interactors.
DIPiDIP-37631N.
IntActiQ9UBG0. 14 interactors.
STRINGi9606.ENSP00000307513.

Structurei

Secondary structure

11479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi46 – 48Combined sources3
Turni49 – 52Combined sources4
Beta strandi53 – 58Combined sources6
Beta strandi61 – 67Combined sources7
Helixi73 – 75Combined sources3
Beta strandi77 – 80Combined sources4
Turni81 – 83Combined sources3
Beta strandi84 – 87Combined sources4
Turni88 – 91Combined sources4
Beta strandi92 – 96Combined sources5
Beta strandi108 – 110Combined sources3
Beta strandi116 – 118Combined sources3
Turni123 – 125Combined sources3
Helixi126 – 134Combined sources9
Beta strandi158 – 160Combined sources3
Turni161 – 163Combined sources3
Turni180 – 184Combined sources5
Beta strandi189 – 193Combined sources5
Beta strandi196 – 200Combined sources5
Beta strandi212 – 218Combined sources7
Helixi219 – 222Combined sources4
Beta strandi225 – 227Combined sources3
Turni236 – 238Combined sources3
Beta strandi240 – 242Combined sources3
Turni243 – 245Combined sources3
Beta strandi248 – 257Combined sources10
Helixi259 – 267Combined sources9
Turni268 – 270Combined sources3
Helixi279 – 288Combined sources10
Turni289 – 291Combined sources3
Beta strandi295 – 301Combined sources7
Beta strandi303 – 305Combined sources3
Beta strandi309 – 311Combined sources3
Beta strandi330 – 332Combined sources3
Beta strandi335 – 339Combined sources5
Turni340 – 343Combined sources4
Beta strandi344 – 349Combined sources6
Beta strandi355 – 361Combined sources7
Beta strandi387 – 389Combined sources3
Beta strandi392 – 401Combined sources10
Helixi403 – 412Combined sources10
Helixi423 – 432Combined sources10
Turni433 – 436Combined sources4
Beta strandi439 – 445Combined sources7
Beta strandi447 – 449Combined sources3
Beta strandi452 – 455Combined sources4
Turni474 – 476Combined sources3
Beta strandi478 – 485Combined sources8
Turni486 – 489Combined sources4
Beta strandi490 – 495Combined sources6
Beta strandi500 – 507Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AO5X-ray2.48A/B35-511[»]
5AO6X-ray3.36A/B35-511[»]
5E4KX-ray2.58A31-510[»]
5E4LX-ray2.44A/B31-510[»]
5EW6X-ray2.29A31-510[»]
ProteinModelPortaliQ9UBG0.
SMRiQ9UBG0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 167Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST127
Domaini182 – 230Fibronectin type-IIPROSITE-ProRule annotationAdd BLAST49
Domaini244 – 360C-type lectin 1PROSITE-ProRule annotationAdd BLAST117
Domaini389 – 505C-type lectin 2PROSITE-ProRule annotationAdd BLAST117
Domaini528 – 644C-type lectin 3PROSITE-ProRule annotationAdd BLAST117
Domaini678 – 809C-type lectin 4PROSITE-ProRule annotationAdd BLAST132
Domaini832 – 951C-type lectin 5PROSITE-ProRule annotationAdd BLAST120
Domaini979 – 1107C-type lectin 6PROSITE-ProRule annotationAdd BLAST129
Domaini1132 – 1243C-type lectin 7PROSITE-ProRule annotationAdd BLAST112
Domaini1273 – 1393C-type lectin 8PROSITE-ProRule annotationAdd BLAST121

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.
Fibronectin type-II domain mediates collagen-binding.
Ricin B-type lectin domain contacts with the second C-type lectin domain.By similarity

Sequence similaritiesi

Contains 8 C-type lectin domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IS43. Eukaryota.
ENOG410XQ89. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000231191.
HOVERGENiHBG053606.
InParanoidiQ9UBG0.
KOiK06560.
OMAiIGLHASQ.
OrthoDBiEOG091G0EGC.
PhylomeDBiQ9UBG0.
TreeFamiTF316663.

Family and domain databases

CDDicd00062. FN2. 1 hit.
Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_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

        10         20         30         40         50
MGPGRPAPAP WPRHLLRCVL LLGCLHLGRP GAPGDAALPE PNVFLIFSHG
60 70 80 90 100
LQGCLEAQGG QVRVTPACNT SLPAQRWKWV SRNRLFNLGT MQCLGTGWPG
110 120 130 140 150
TNTTASLGMY ECDREALNLR WHCRTLGDQL SLLLGARTSN ISKPGTLERG
160 170 180 190 200
DQTRSGQWRI YGSEEDLCAL PYHEVYTIQG NSHGKPCTIP FKYDNQWFHG
210 220 230 240 250
CTSTGREDGH LWCATTQDYG KDERWGFCPI KSNDCETFWD KDQLTDSCYQ
260 270 280 290 300
FNFQSTLSWR EAWASCEQQG ADLLSITEIH EQTYINGLLT GYSSTLWIGL
310 320 330 340 350
NDLDTSGGWQ WSDNSPLKYL NWESDQPDNP SEENCGVIRT ESSGGWQNRD
360 370 380 390 400
CSIALPYVCK KKPNATAEPT PPDRWANVKV ECEPSWQPFQ GHCYRLQAEK
410 420 430 440 450
RSWQESKKAC LRGGGDLVSI HSMAELEFIT KQIKQEVEEL WIGLNDLKLQ
460 470 480 490 500
MNFEWSDGSL VSFTHWHPFE PNNFRDSLED CVTIWGPEGR WNDSPCNQSL
510 520 530 540 550
PSICKKAGQL SQGAAEEDHG CRKGWTWHSP SCYWLGEDQV TYSEARRLCT
560 570 580 590 600
DHGSQLVTIT NRFEQAFVSS LIYNWEGEYF WTALQDLNST GSFFWLSGDE
610 620 630 640 650
VMYTHWNRDQ PGYSRGGCVA LATGSAMGLW EVKNCTSFRA RYICRQSLGT
660 670 680 690 700
PVTPELPGPD PTPSLTGSCP QGWASDTKLR YCYKVFSSER LQDKKSWVQA
710 720 730 740 750
QGACQELGAQ LLSLASYEEE HFVANMLNKI FGESEPEIHE QHWFWIGLNR
760 770 780 790 800
RDPRGGQSWR WSDGVGFSYH NFDRSRHDDD DIRGCAVLDL ASLQWVAMQC
810 820 830 840 850
DTQLDWICKI PRGTDVREPD DSPQGRREWL RFQEAEYKFF EHHSTWAQAQ
860 870 880 890 900
RICTWFQAEL TSVHSQAELD FLSHNLQKFS RAQEQHWWIG LHTSESDGRF
910 920 930 940 950
RWTDGSIINF ISWAPGKPRP VGKDKKCVYM TASREDWGDQ RCLTALPYIC
960 970 980 990 1000
KRSNVTKETQ PPDLPTTALG GCPSDWIQFL NKCFQVQGQE PQSRVKWSEA
1010 1020 1030 1040 1050
QFSCEQQEAQ LVTITNPLEQ AFITASLPNV TFDLWIGLHA SQRDFQWVEQ
1060 1070 1080 1090 1100
EPLMYANWAP GEPSGPSPAP SGNKPTSCAV VLHSPSAHFT GRWDDRSCTE
1110 1120 1130 1140 1150
ETHGFICQKG TDPSLSPSPA ALPPAPGTEL SYLNGTFRLL QKPLRWHDAL
1160 1170 1180 1190 1200
LLCESRNASL AYVPDPYTQA FLTQAARGLR TPLWIGLAGE EGSRRYSWVS
1210 1220 1230 1240 1250
EEPLNYVGWQ DGEPQQPGGC TYVDVDGAWR TTSCDTKLQG AVCGVSSGPP
1260 1270 1280 1290 1300
PPRRISYHGS CPQGLADSAW IPFREHCYSF HMELLLGHKE ARQRCQRAGG
1310 1320 1330 1340 1350
AVLSILDEME NVFVWEHLQS YEGQSRGAWL GMNFNPKGGT LVWQDNTAVN
1360 1370 1380 1390 1400
YSNWGPPGLG PSMLSHNSCY WIQSNSGLWR PGACTNITMG VVCKLPRAEQ
1410 1420 1430 1440 1450
SSFSPSALPE NPAALVVVLM AVLLLLALLT AALILYRRRQ SIERGAFEGA
1460 1470
RYSRSSSSPT EATEKNILVS DMEMNEQQE
Length:1,479
Mass (Da):166,674
Last modified:January 11, 2011 - v2
Checksum:iAAAA5286F91DF7E7
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02530443V → I.1 PublicationCorresponds to variant rs2014055dbSNPEnsembl.1
Natural variantiVAR_0253051156R → H.5 PublicationsCorresponds to variant rs2429387dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Endo180

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AO5X-ray2.48A/B35-511[»]
5AO6X-ray3.36A/B35-511[»]
5E4KX-ray2.58A31-510[»]
5E4LX-ray2.44A/B31-510[»]
5EW6X-ray2.29A31-510[»]
ProteinModelPortaliQ9UBG0.
SMRiQ9UBG0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115231. 25 interactors.
DIPiDIP-37631N.
IntActiQ9UBG0. 14 interactors.
STRINGi9606.ENSP00000307513.

PTM databases

iPTMnetiQ9UBG0.
PhosphoSitePlusiQ9UBG0.
SwissPalmiQ9UBG0.
UniCarbKBiQ9UBG0.

Polymorphism and mutation databases

BioMutaiMRC2.
DMDMi317373394.

Proteomic databases

EPDiQ9UBG0.
MaxQBiQ9UBG0.
PaxDbiQ9UBG0.
PeptideAtlasiQ9UBG0.
PRIDEiQ9UBG0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303375; ENSP00000307513; ENSG00000011028.
GeneIDi9902.
KEGGihsa:9902.
UCSCiuc002jad.5. human.

Organism-specific databases

CTDi9902.
DisGeNETi9902.
GeneCardsiMRC2.
H-InvDBHIX0018596.
HIX0027238.
HGNCiHGNC:16875. MRC2.
HPAiHPA041991.
MIMi612264. gene.
neXtProtiNX_Q9UBG0.
OpenTargetsiENSG00000011028.
PharmGKBiPA134988161.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IS43. Eukaryota.
ENOG410XQ89. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000231191.
HOVERGENiHBG053606.
InParanoidiQ9UBG0.
KOiK06560.
OMAiIGLHASQ.
OrthoDBiEOG091G0EGC.
PhylomeDBiQ9UBG0.
TreeFamiTF316663.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000011028-MONOMER.
ReactomeiR-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).

Miscellaneous databases

ChiTaRSiMRC2. human.
GenomeRNAii9902.
PROiQ9UBG0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000011028.
CleanExiHS_MRC2.
ExpressionAtlasiQ9UBG0. baseline and differential.
GenevisibleiQ9UBG0. HS.

Family and domain databases

CDDicd00062. FN2. 1 hit.
Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_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]
ProtoNetiSearch...

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: November 30, 2016
This is version 127 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.