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P51884 (LUM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lumican
Alternative name(s):
Keratan sulfate proteoglycan lumican
Short name=KSPG lumican
Gene names
Name:LUM
Synonyms:LDC, SLRR2D
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Binds to laminin By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Cornea and other tissues.

Developmental stage

Present in the extracellular matrix of human articular cartilage at all ages, although its abundance is far greater in the adult. In the adult cartilage lumican exists predominantly in a glycoprotein form lacking keratan sulfate, whereas the juvenile form of the molecule is a proteoglycan.

Post-translational modification

Sulfated on tyrosine residue(s).

Sequence similarities

Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily.

Contains 11 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainLeucine-rich repeat
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Proteoglycan
Pyrrolidone carboxylic acid
Sulfation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cartilage development

Inferred from electronic annotation. Source: Ensembl

collagen fibril organization

Non-traceable author statement PubMed 10892350. Source: UniProtKB

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

keratan sulfate biosynthetic process

Traceable author statement. Source: Reactome

keratan sulfate catabolic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

response to growth factor

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

visual perception

Traceable author statement PubMed 10802664. Source: ProtInc

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

fibrillar collagen trimer

Inferred from direct assay PubMed 10734230. Source: UniProtKB

lysosomal lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functioncollagen binding

Inferred from direct assay PubMed 10892350. Source: UniProtKB

extracellular matrix structural constituent

Non-traceable author statement PubMed 10892350. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 338320Lumican
PRO_0000032733

Regions

Domain28 – 6639LRRNT
Repeat67 – 8822LRR 1
Repeat91 – 11424LRR 2
Repeat117 – 13721LRR 3
Repeat138 – 15922LRR 4
Repeat160 – 18122LRR 5
Repeat185 – 20521LRR 6
Repeat206 – 22722LRR 7
Repeat230 – 25324LRR 8
Repeat255 – 27622LRR 9
Repeat277 – 29620LRR 10
Repeat305 – 32622LRR 11
Compositional bias37 – 5317Cys-rich

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid
Modified residue201Sulfotyrosine By similarity
Modified residue211Sulfotyrosine By similarity
Modified residue231Sulfotyrosine By similarity
Modified residue301Sulfotyrosine By similarity
Glycosylation881N-linked (GlcNAc...) (keratan sulfate) Ref.8 Ref.9 Ref.10
Glycosylation1271N-linked (GlcNAc...) (keratan sulfate) Potential
Glycosylation1601N-linked (GlcNAc...) (keratan sulfate) Ref.8 Ref.9 Ref.10
Glycosylation2521N-linked (GlcNAc...) (keratan sulfate) Potential
Disulfide bond295 ↔ 328 By similarity

Natural variations

Natural variant1991L → P Found in patients with amyotrophic lateral sclerosis. Ref.11
Corresponds to variant rs147975710 [ dbSNP | Ensembl ].
VAR_065763

Experimental info

Sequence conflict271L → P in AAA85268. Ref.1
Sequence conflict1011L → V in AAA85268. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51884 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 905D2EBD370CC59D

FASTA33838,429
        10         20         30         40         50         60 
MSLSAFTLFL ALIGGTSGQY YDYDFPLSIY GQSSPNCAPE CNCPESYPSA MYCDELKLKS 

        70         80         90        100        110        120 
VPMVPPGIKY LYLRNNQIDH IDEKAFENVT DLQWLILDHN LLENSKIKGR VFSKLKQLKK 

       130        140        150        160        170        180 
LHINHNNLTE SVGPLPKSLE DLQLTHNKIT KLGSFEGLVN LTFIHLQHNR LKEDAVSAAF 

       190        200        210        220        230        240 
KGLKSLEYLD LSFNQIARLP SGLPVSLLTL YLDNNKISNI PDEYFKRFNA LQYLRLSHNE 

       250        260        270        280        290        300 
LADSGIPGNS FNVSSLVELD LSYNKLKNIP TVNENLENYY LEVNQLEKFD IKSFCKILGP 

       310        320        330 
LSYSKIKHLR LDGNRISETS LPPDMYECLR VANEVTLN 

« Hide

References

« Hide 'large scale' references
[1]"The human lumican gene. Organization, chromosomal location, and expression in articular cartilage."
Grover J., Chen X.-N., Korenberg J.R., Roughley P.J.
J. Biol. Chem. 270:21942-21949(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cartilage, Intestine and Placenta.
[2]"Primary structure of human lumican (keratan sulfate proteoglycan) and localization of the gene (LUM) to chromosome 12q21.3-q22."
Chakravarti S., Stallings R.L., Sundar-Raj N., Cornuet P.K., Hassell J.R.
Genomics 27:481-488(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Cornea.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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. expand/collapse author list , 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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: Lung and Prostate.
[7]"Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry."
Onnerfjord P., Heathfield T.F., Heinegaard D.
J. Biol. Chem. 279:26-33(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION, PYROGLUTAMATE FORMATION AT GLN-19, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88 AND ASN-160.
Tissue: Plasma.
[9]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88; ASN-127; ASN-160 AND ASN-252.
Tissue: Plasma.
[10]"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-88; ASN-127; ASN-160 AND ASN-252.
Tissue: Liver.
[11]"Resequencing of 29 candidate genes in patients with familial and sporadic amyotrophic lateral sclerosis."
Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D., Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A., Rouleau G.A.
Arch. Neurol. 68:587-593(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-199.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18728 mRNA. Translation: AAA85268.1.
U21128 mRNA. Translation: AAA91639.1.
BT006707 mRNA. Translation: AAP35353.1.
AK312682 mRNA. Translation: BAG35562.1.
CH471054 Genomic DNA. Translation: EAW97449.1.
BC007038 mRNA. Translation: AAH07038.1.
BC035997 mRNA. Translation: AAH35997.1.
CCDSCCDS9038.1.
RefSeqNP_002336.1. NM_002345.3.
UniGeneHs.406475.

3D structure databases

ProteinModelPortalP51884.
SMRP51884. Positions 37-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110238. 3 interactions.
IntActP51884. 2 interactions.
MINTMINT-1422554.
STRING9606.ENSP00000266718.

PTM databases

PhosphoSiteP51884.

Polymorphism databases

DMDM20141464.

Proteomic databases

MaxQBP51884.
PaxDbP51884.
PeptideAtlasP51884.
PRIDEP51884.

Protocols and materials databases

DNASU4060.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266718; ENSP00000266718; ENSG00000139329.
GeneID4060.
KEGGhsa:4060.
UCSCuc001tbm.3. human.

Organism-specific databases

CTD4060.
GeneCardsGC12M091430.
HGNCHGNC:6724. LUM.
HPACAB022193.
HPA001522.
MIM600616. gene.
neXtProtNX_P51884.
PharmGKBPA30486.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000234447.
HOVERGENHBG108061.
InParanoidP51884.
KOK08122.
OMAKKLHINY.
OrthoDBEOG75F4DF.
PhylomeDBP51884.
TreeFamTF334562.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeP51884.
CleanExHS_LUM.
GenevestigatorP51884.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR027219. Lumican.
[Graphical view]
PANTHERPTHR24371:SF54. PTHR24371:SF54. 1 hit.
PfamPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLUM. human.
GeneWikiLUM.
GenomeRNAi4060.
NextBio15912.
PMAP-CutDBP51884.
PROP51884.
SOURCESearch...

Entry information

Entry nameLUM_HUMAN
AccessionPrimary (citable) accession number: P51884
Secondary accession number(s): B2R6R5, Q96QM7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM