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

Laminin subunit gamma-2

Gene

LAMC2

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

Functioni

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells.1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • epidermis development Source: ProtInc
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • hemidesmosome assembly Source: Reactome
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000058085-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-446107. Type I hemidesmosome assembly.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiQ13753.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-2
Alternative name(s):
Cell-scattering factor 140 kDa subunit
Short name:
CSF 140 kDa subunit
Epiligrin subunit gamma
Kalinin subunit gamma
Kalinin/nicein/epiligrin 100 kDa subunit
Ladsin 140 kDa subunit
Laminin B2t chain
Laminin-5 subunit gamma
Large adhesive scatter factor 140 kDa subunit
Nicein subunit gamma
Gene namesi
Name:LAMC2
Synonyms:LAMB2T, LAMNB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6493. LAMC2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa, junctional, Herlitz type (H-JEB)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.
See also OMIM:226700

Keywords - Diseasei

Epidermolysis bullosa

Organism-specific databases

DisGeNETi3918.
MalaCardsiLAMC2.
MIMi226700. phenotype.
OpenTargetsiENSG00000058085.
Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79405. Junctional epidermolysis bullosa inversa.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBiPA30281.

Protein family/group databases

Allergomei8331. Hom s Laminin gamma_2.

Chemistry databases

ChEMBLiCHEMBL2364187.

Polymorphism and mutation databases

BioMutaiLAMC2.
DMDMi90185107.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001707722 – 1193Laminin subunit gamma-2Add BLAST1172

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 37PROSITE-ProRule annotation
Disulfide bondi30 ↔ 53PROSITE-ProRule annotation
Disulfide bondi56 ↔ 65PROSITE-ProRule annotation
Disulfide bondi68 ↔ 81PROSITE-ProRule annotation
Disulfide bondi84 ↔ 96PROSITE-ProRule annotation
Disulfide bondi86 ↔ 102PROSITE-ProRule annotation
Disulfide bondi104 ↔ 113PROSITE-ProRule annotation
Disulfide bondi116 ↔ 128PROSITE-ProRule annotation
Disulfide bondi139 ↔ 150PROSITE-ProRule annotation
Disulfide bondi141 ↔ 155PROSITE-ProRule annotation
Disulfide bondi157 ↔ 166PROSITE-ProRule annotation
Disulfide bondi169 ↔ 184PROSITE-ProRule annotation
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi362N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi462 ↔ 470PROSITE-ProRule annotation
Disulfide bondi464 ↔ 481PROSITE-ProRule annotation
Disulfide bondi484 ↔ 493PROSITE-ProRule annotation
Disulfide bondi496 ↔ 514PROSITE-ProRule annotation
Disulfide bondi517 ↔ 531PROSITE-ProRule annotation
Disulfide bondi519 ↔ 538PROSITE-ProRule annotation
Disulfide bondi541 ↔ 550PROSITE-ProRule annotation
Disulfide bondi553 ↔ 570PROSITE-ProRule annotation
Disulfide bondi573 ↔ 585PROSITE-ProRule annotation
Disulfide bondi575 ↔ 591PROSITE-ProRule annotation
Disulfide bondi593 ↔ 602PROSITE-ProRule annotation
Disulfide bondi609InterchainCurated
Disulfide bondi612InterchainCurated
Glycosylationi942N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1033N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1184InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ13753.
MaxQBiQ13753.
PaxDbiQ13753.
PeptideAtlasiQ13753.
PRIDEiQ13753.

PTM databases

iPTMnetiQ13753.
PhosphoSitePlusiQ13753.

Miscellaneous databases

PMAP-CutDBQ13753.

Expressioni

Tissue specificityi

The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.

Gene expression databases

BgeeiENSG00000058085.
CleanExiHS_LAMC2.
GenevisibleiQ13753. HS.

Organism-specific databases

HPAiCAB004257.
HPA024638.

Interactioni

Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).

Protein-protein interaction databases

BioGridi110112. 5 interactors.
IntActiQ13753. 1 interactor.
MINTiMINT-4053464.
STRINGi9606.ENSP00000264144.

Structurei

3D structure databases

ProteinModelPortaliQ13753.
SMRiQ13753.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 83Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini84 – 130Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST47
Domaini139 – 186Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST48
Domaini187 – 196Laminin EGF-like 4; first partPROSITE-ProRule annotation10
Domaini213 – 381Laminin IV type APROSITE-ProRule annotationAdd BLAST169
Domaini382 – 415Laminin EGF-like 4; second partPROSITE-ProRule annotationAdd BLAST34
Domaini416 – 461Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST46
Domaini462 – 516Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST55
Domaini517 – 572Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST56
Domaini573 – 602Laminin EGF-like 8; truncatedPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni603 – 1193Domain II and IAdd BLAST591

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili611 – 718Sequence analysisAdd BLAST108
Coiled coili811 – 1076Sequence analysisAdd BLAST266
Coiled coili1117 – 1193Sequence analysisAdd BLAST77

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain IV is globular.

Sequence similaritiesi

Contains 8 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IP6C. Eukaryota.
ENOG4110QI9. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG062127.
InParanoidiQ13753.
KOiK06246.
OMAiTEEVVCN.
OrthoDBiEOG091G005L.
PhylomeDBiQ13753.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 7 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 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 Long (identifier: Q13753-1) [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
MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG
60 70 80 90 100
FRCLNCNDNT DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG
110 120 130 140 150
RCSCKPGVTG ARCDRCLPGF HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC
160 170 180 190 200
DAGRCVCKPA VTGERCDRCR SGYYNLDGGN PEGCTQCFCY GHSASCRSSA
210 220 230 240 250
EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF SSAQRLDPVY
260 270 280 290 300
FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL
310 320 330 340 350
MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA
360 370 380 390 400
TYGEYSTGYI DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY
410 420 430 440 450
KRDSARLGPF GTCIPCNCQG GGACDPDTGD CYSGDENPDI ECADCPIGFY
460 470 480 490 500
NDPHDPRSCK PCPCHNGFSC SVMPETEEVV CNNCPPGVTG ARCELCADGY
510 520 530 540 550
FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK CIHNTAGIYC
560 570 580 590 600
DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP
610 620 630 640 650
NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE
660 670 680 690 700
GRMQQAEQAL QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM
710 720 730 740 750
TVERVRALGS QYQNRVRDTH RLITQMQLSL AESEASLGNT NIPASDHYVG
760 770 780 790 800
PNGFKSLAQE ATRLAESHVE SASNMEQLTR ETEDYSKQAL SLVRKALHEG
810 820 830 840 850
VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE ADRSYQHSLR
860 870 880 890 900
LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG
910 920 930 940 950
NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES
960 970 980 990 1000
ILKNLREFDL QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA
1010 1020 1030 1040 1050
AADAQRAKNG AGEALEISSE IEQEIGSLNL EANVTADGAL AMEKGLASLK
1060 1070 1080 1090 1100
SEMREVEGEL ERKELEFDTN MDAVQMVITE AQKVDTRAKN AGVTIQDTLN
1110 1120 1130 1140 1150
TLDGLLHLMD QPLSVDEEGL VLLEQKLSRA KTQINSQLRP MMSELEERAR
1160 1170 1180 1190
QQRGHLHLLE TSIDGILADV KNLENIRDNL PPGCYNTQAL EQQ
Length:1,193
Mass (Da):130,976
Last modified:March 7, 2006 - v2
Checksum:i0BBE1A56516C5C9A
GO
Isoform Short (identifier: Q13753-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1110-1193: DQPLSVDEEG...CYNTQALEQQ → GM

Show »
Length:1,111
Mass (Da):121,604
Checksum:i7762993F3D7F89DF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12F → L in CAA52108 (PubMed:8306988).Curated1
Sequence conflicti473M → I in CAA78728 (PubMed:1383240).Curated1
Sequence conflicti473M → I in CAA78729 (PubMed:1383240).Curated1
Sequence conflicti521N → S in CAA78728 (PubMed:1383240).Curated1
Sequence conflicti521N → S in CAA78729 (PubMed:1383240).Curated1
Sequence conflicti857R → P in CAA78728 (PubMed:1383240).Curated1
Sequence conflicti857R → P in CAA78729 (PubMed:1383240).Curated1
Sequence conflicti883S → T in AAC50457 (PubMed:8786121).Curated1
Sequence conflicti883S → T in AAC50456 (PubMed:8786121).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050081111A → P.Corresponds to variant rs12065473dbSNPEnsembl.1
Natural variantiVAR_050082115R → Q.Corresponds to variant rs17481405dbSNPEnsembl.1
Natural variantiVAR_050083124T → M.Corresponds to variant rs11586699dbSNPEnsembl.1
Natural variantiVAR_050084136D → V.Corresponds to variant rs12037099dbSNPEnsembl.1
Natural variantiVAR_022017247D → E.Corresponds to variant rs2296306dbSNPEnsembl.1
Natural variantiVAR_050085608S → I.Corresponds to variant rs4373715dbSNPEnsembl.1
Natural variantiVAR_020304733S → T.Corresponds to variant rs2296303dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0030401110 – 1193DQPLS…ALEQQ → GM in isoform Short. 1 PublicationAdd BLAST84

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15008 mRNA. Translation: CAA78728.1.
Z15009 mRNA. Translation: CAA78729.1.
X73902 mRNA. Translation: CAA52108.1.
U31201
, U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198, U31199 Genomic DNA. Translation: AAC50457.1.
U31200
, U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198 Genomic DNA. Translation: AAC50456.1.
AL354953 Genomic DNA. Translation: CAH70980.1.
CH471067 Genomic DNA. Translation: EAW91146.1.
BC112286 mRNA. Translation: AAI12287.1.
BC113378 mRNA. Translation: AAI13379.1.
CCDSiCCDS1352.1. [Q13753-1]
CCDS44285.1. [Q13753-2]
PIRiA44018.
RefSeqiNP_005553.2. NM_005562.2. [Q13753-1]
NP_061486.2. NM_018891.2. [Q13753-2]
UniGeneiHs.591484.

Genome annotation databases

EnsembliENST00000264144; ENSP00000264144; ENSG00000058085. [Q13753-1]
ENST00000493293; ENSP00000432063; ENSG00000058085. [Q13753-2]
GeneIDi3918.
KEGGihsa:3918.
UCSCiuc001gpz.5. human. [Q13753-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15008 mRNA. Translation: CAA78728.1.
Z15009 mRNA. Translation: CAA78729.1.
X73902 mRNA. Translation: CAA52108.1.
U31201
, U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198, U31199 Genomic DNA. Translation: AAC50457.1.
U31200
, U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198 Genomic DNA. Translation: AAC50456.1.
AL354953 Genomic DNA. Translation: CAH70980.1.
CH471067 Genomic DNA. Translation: EAW91146.1.
BC112286 mRNA. Translation: AAI12287.1.
BC113378 mRNA. Translation: AAI13379.1.
CCDSiCCDS1352.1. [Q13753-1]
CCDS44285.1. [Q13753-2]
PIRiA44018.
RefSeqiNP_005553.2. NM_005562.2. [Q13753-1]
NP_061486.2. NM_018891.2. [Q13753-2]
UniGeneiHs.591484.

3D structure databases

ProteinModelPortaliQ13753.
SMRiQ13753.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110112. 5 interactors.
IntActiQ13753. 1 interactor.
MINTiMINT-4053464.
STRINGi9606.ENSP00000264144.

Chemistry databases

ChEMBLiCHEMBL2364187.

Protein family/group databases

Allergomei8331. Hom s Laminin gamma_2.

PTM databases

iPTMnetiQ13753.
PhosphoSitePlusiQ13753.

Polymorphism and mutation databases

BioMutaiLAMC2.
DMDMi90185107.

Proteomic databases

EPDiQ13753.
MaxQBiQ13753.
PaxDbiQ13753.
PeptideAtlasiQ13753.
PRIDEiQ13753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264144; ENSP00000264144; ENSG00000058085. [Q13753-1]
ENST00000493293; ENSP00000432063; ENSG00000058085. [Q13753-2]
GeneIDi3918.
KEGGihsa:3918.
UCSCiuc001gpz.5. human. [Q13753-1]

Organism-specific databases

CTDi3918.
DisGeNETi3918.
GeneCardsiLAMC2.
GeneReviewsiLAMC2.
HGNCiHGNC:6493. LAMC2.
HPAiCAB004257.
HPA024638.
MalaCardsiLAMC2.
MIMi150292. gene.
226700. phenotype.
neXtProtiNX_Q13753.
OpenTargetsiENSG00000058085.
Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79405. Junctional epidermolysis bullosa inversa.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBiPA30281.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IP6C. Eukaryota.
ENOG4110QI9. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG062127.
InParanoidiQ13753.
KOiK06246.
OMAiTEEVVCN.
OrthoDBiEOG091G005L.
PhylomeDBiQ13753.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000058085-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-446107. Type I hemidesmosome assembly.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiQ13753.

Miscellaneous databases

ChiTaRSiLAMC2. human.
GeneWikiiLaminin,_gamma_2.
GenomeRNAii3918.
PMAP-CutDBQ13753.
PROiQ13753.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000058085.
CleanExiHS_LAMC2.
GenevisibleiQ13753. HS.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 7 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMC2_HUMAN
AccessioniPrimary (citable) accession number: Q13753
Secondary accession number(s): Q02536
, Q02537, Q13752, Q14941, Q14DF7, Q2M1N2, Q5VYE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 7, 2006
Last modified: November 30, 2016
This is version 174 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

Miscellaneous

Binds heparin.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.