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Protein

Laminin subunit gamma-3

Gene

LAMC3

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.

GO - Molecular functioni

  • structural molecule activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:ENSG00000050555-MONOMER.
ReactomeiR-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-3
Alternative name(s):
Laminin-12 subunit gamma
Laminin-14 subunit gamma
Laminin-15 subunit gamma
Gene namesi
Name:LAMC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:6494. LAMC3.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB-SubCell
  • extracellular region Source: Reactome
  • membrane Source: ProtInc
  • proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Cortical malformations occipital (OCCM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease in which affected individuals develop seizures, sometimes associated with transient visual changes. Brain MRI shows both pachygyria and polymicrogyria restricted to the lateral occipital lobes.
See also OMIM:614115
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066404350G → R in OCCM. 1 PublicationCorresponds to variant rs571785750dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10319.
MalaCardsiLAMC3.
MIMi614115. phenotype.
OpenTargetsiENSG00000050555.
Orphaneti280640. Occipital pachygyria and polymicrogyria.
PharmGKBiPA30282.

Chemistry databases

ChEMBLiCHEMBL2364187.

Polymorphism and mutation databases

BioMutaiLAMC3.
DMDMi308153586.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001707920 – 1575Laminin subunit gamma-3Add BLAST1556

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi87N-linked (GlcNAc...)Sequence analysis1
Glycosylationi119N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi271 ↔ 280PROSITE-ProRule annotation
Disulfide bondi273 ↔ 290PROSITE-ProRule annotation
Disulfide bondi292 ↔ 301PROSITE-ProRule annotation
Glycosylationi295N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi304 ↔ 324PROSITE-ProRule annotation
Disulfide bondi327 ↔ 336PROSITE-ProRule annotation
Glycosylationi328N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi329 ↔ 352PROSITE-ProRule annotation
Disulfide bondi355 ↔ 364PROSITE-ProRule annotation
Disulfide bondi367 ↔ 380PROSITE-ProRule annotation
Disulfide bondi383 ↔ 395PROSITE-ProRule annotation
Disulfide bondi385 ↔ 401PROSITE-ProRule annotation
Disulfide bondi403 ↔ 412PROSITE-ProRule annotation
Disulfide bondi415 ↔ 427PROSITE-ProRule annotation
Disulfide bondi430 ↔ 441PROSITE-ProRule annotation
Disulfide bondi432 ↔ 448PROSITE-ProRule annotation
Disulfide bondi450 ↔ 459PROSITE-ProRule annotation
Disulfide bondi462 ↔ 477PROSITE-ProRule annotation
Glycosylationi631N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi707 ↔ 715PROSITE-ProRule annotation
Disulfide bondi709 ↔ 722PROSITE-ProRule annotation
Disulfide bondi724 ↔ 733PROSITE-ProRule annotation
Disulfide bondi736 ↔ 752PROSITE-ProRule annotation
Disulfide bondi755 ↔ 763PROSITE-ProRule annotation
Disulfide bondi757 ↔ 774PROSITE-ProRule annotation
Disulfide bondi777 ↔ 786PROSITE-ProRule annotation
Disulfide bondi789 ↔ 807PROSITE-ProRule annotation
Disulfide bondi810 ↔ 824PROSITE-ProRule annotation
Disulfide bondi812 ↔ 831PROSITE-ProRule annotation
Disulfide bondi834 ↔ 843PROSITE-ProRule annotation
Glycosylationi837N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi846 ↔ 863PROSITE-ProRule annotation
Disulfide bondi866 ↔ 880PROSITE-ProRule annotation
Disulfide bondi868 ↔ 887PROSITE-ProRule annotation
Disulfide bondi889 ↔ 898PROSITE-ProRule annotation
Disulfide bondi901 ↔ 914PROSITE-ProRule annotation
Disulfide bondi917 ↔ 929PROSITE-ProRule annotation
Disulfide bondi919 ↔ 936PROSITE-ProRule annotation
Disulfide bondi938 ↔ 947PROSITE-ProRule annotation
Disulfide bondi950 ↔ 962PROSITE-ProRule annotation
Disulfide bondi965 ↔ 977PROSITE-ProRule annotation
Disulfide bondi967 ↔ 983PROSITE-ProRule annotation
Glycosylationi980N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi985 ↔ 994PROSITE-ProRule annotation
Disulfide bondi997 ↔ 1010PROSITE-ProRule annotation
Glycosylationi1185N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9Y6N6.
MaxQBiQ9Y6N6.
PaxDbiQ9Y6N6.
PeptideAtlasiQ9Y6N6.
PRIDEiQ9Y6N6.

PTM databases

iPTMnetiQ9Y6N6.
PhosphoSitePlusiQ9Y6N6.

Expressioni

Tissue specificityi

Broadly expressed in: skin, heart, lung, and the reproductive tracts.

Gene expression databases

BgeeiENSG00000050555.
CleanExiHS_LAMC3.
ExpressionAtlasiQ9Y6N6. baseline and differential.
GenevisibleiQ9Y6N6. HS.

Organism-specific databases

HPAiHPA022814.

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-3 is a subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and laminin-15 (laminin-523).

Protein-protein interaction databases

BioGridi115603. 20 interactors.
IntActiQ9Y6N6. 27 interactors.
MINTiMINT-7034525.
STRINGi9606.ENSP00000354360.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6N6.
SMRiQ9Y6N6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 270Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini271 – 326Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini327 – 382Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini383 – 429Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Domaini430 – 479Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST50
Domaini480 – 489Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini499 – 672Laminin IV type APROSITE-ProRule annotationAdd BLAST174
Domaini673 – 706Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST34
Domaini707 – 754Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST48
Domaini755 – 809Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST55
Domaini810 – 865Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST56
Domaini866 – 916Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST51
Domaini917 – 964Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST48
Domaini965 – 1013Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST49

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1014 – 1575Domain II and IAdd BLAST562

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1073 – 1134Sequence analysisAdd BLAST62
Coiled coili1201 – 1228Sequence analysisAdd BLAST28
Coiled coili1410 – 1492Sequence analysisAdd BLAST83
Coiled coili1523 – 1567Sequence analysisAdd BLAST45

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1059 – 1061Cell attachment siteSequence analysis3

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 11 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IP68. Eukaryota.
ENOG4111F9V. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ9Y6N6.
KOiK06247.
OMAiAGCSSCF.
OrthoDBiEOG091G005L.
PhylomeDBiQ9Y6N6.
TreeFamiTF352481.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Y6N6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA
60 70 80 90 100
SHTCGSPPED FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES
110 120 130 140 150
TWWQSPSMAF GVQYPTSVNI TLRLGKAYEI TYVRLKFHTS RPESFAIYKR
160 170 180 190 200
SRADGPWEPY QFYSASCQKT YGRPEGQYLR PGEDERVAFC TSEFSDISPL
210 220 230 240 250
SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR LNTFGDDIFK
260 270 280 290 300
DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD
310 320 330 340 350
CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG
360 370 380 390 400
RCHHCRDHTA GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT
410 420 430 440 450
CACKPTVTGW KCDRCLPGFH SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC
460 470 480 490 500
KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC FCYGHSKVCA STAQFQVHHI
510 520 530 540 550
LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL TAPEKFLGDQ
560 570 580 590 600
RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP
610 620 630 640 650
REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF
660 670 680 690 700
LTEVRLTSAR PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP
710 720 730 740 750
YASCVPCTCN QHGTCDPNTG ICVCSHHTEG PSCERCLPGF YGNPFAGQAD
760 770 780 790 800
DCQPCPCPGQ SACTTIPESR EVVCTHCPPG QRGRRCEVCD DGFFGDPLGL
810 820 830 840 850
FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG DHCEHCQEGF
860 870 880 890 900
YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR
910 920 930 940 950
CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC
960 970 980 990 1000
QLGFFGFSIK GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN
1010 1020 1030 1040 1050
FFLTADGTHC QQCPSCYALV KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL
1060 1070 1080 1090 1100
DILLGEAPRG DVYQGHHLLP GAREAFLEQM MSLEGAVKAA REQLQRLNKG
1110 1120 1130 1140 1150
ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE IPQEGPSQPT
1160 1170 1180 1190 1200
KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA
1210 1220 1230 1240 1250
LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL
1260 1270 1280 1290 1300
ALLASPGALP QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT
1310 1320 1330 1340 1350
LRQTEPLTKL HQEARAALTQ ASSSVQAATV TVMGARTLLA DLEGMKLQFP
1360 1370 1380 1390 1400
RPKDQAALQR KADSVSDRLL ADTRKKTKQA ERMLGNAAPL SSSAKKKGRE
1410 1420 1430 1440 1450
AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA SQQVLASEAR
1460 1470 1480 1490 1500
RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA
1510 1520 1530 1540 1550
PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL
1560 1570
AEIRADKQNL EAILHSLPEN CASWQ
Length:1,575
Mass (Da):171,227
Last modified:October 5, 2010 - v3
Checksum:iD09DAFB3A900E1BD
GO

Sequence cautioni

The sequence AAD36991 differs from that shown. Reason: Frameshift at positions 598 and 609.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti957F → S in AAD36991 (PubMed:10225960).Curated1
Sequence conflicti979E → Y in AAD36991 (PubMed:10225960).Curated1
Sequence conflicti999D → Y in AAD36991 (PubMed:10225960).Curated1
Sequence conflicti1024A → T in AAD36991 (PubMed:10225960).Curated1
Sequence conflicti1157T → I in AAD36991 (PubMed:10225960).Curated1
Sequence conflicti1309K → KARSRLTATSASQ in CAH69983 (PubMed:15164053).Curated1
Sequence conflicti1309K → MARSRLTATFASQ in AAD36991 (PubMed:10225960).Curated1
Sequence conflicti1313E → G in AAD36991 (PubMed:10225960).Curated1
Sequence conflicti1433T → M in BAD92124 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066404350G → R in OCCM. 1 PublicationCorresponds to variant rs571785750dbSNPEnsembl.1
Natural variantiVAR_056145522P → S.1 PublicationCorresponds to variant rs869457dbSNPEnsembl.1
Natural variantiVAR_056146544E → G.2 PublicationsCorresponds to variant rs10901333dbSNPEnsembl.1
Natural variantiVAR_056147770R → G.2 PublicationsCorresponds to variant rs3739510dbSNPEnsembl.1
Natural variantiVAR_0561481082S → G.2 PublicationsCorresponds to variant rs2275140dbSNPEnsembl.1
Natural variantiVAR_0561491264R → W.Corresponds to variant rs11244275dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041835 mRNA. Translation: AAD36991.1. Frameshift.
AL583807, AL355872 Genomic DNA. Translation: CAH69983.1.
AL583807, AL355872 Genomic DNA. Translation: CAH69984.3.
AL355872, AL583807 Genomic DNA. Translation: CAX14981.1.
AB208887 mRNA. Translation: BAD92124.1.
CCDSiCCDS6938.1.
RefSeqiNP_006050.3. NM_006059.3.
UniGeneiHs.201805.

Genome annotation databases

EnsembliENST00000361069; ENSP00000354360; ENSG00000050555.
GeneIDi10319.
KEGGihsa:10319.
UCSCiuc004caa.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041835 mRNA. Translation: AAD36991.1. Frameshift.
AL583807, AL355872 Genomic DNA. Translation: CAH69983.1.
AL583807, AL355872 Genomic DNA. Translation: CAH69984.3.
AL355872, AL583807 Genomic DNA. Translation: CAX14981.1.
AB208887 mRNA. Translation: BAD92124.1.
CCDSiCCDS6938.1.
RefSeqiNP_006050.3. NM_006059.3.
UniGeneiHs.201805.

3D structure databases

ProteinModelPortaliQ9Y6N6.
SMRiQ9Y6N6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115603. 20 interactors.
IntActiQ9Y6N6. 27 interactors.
MINTiMINT-7034525.
STRINGi9606.ENSP00000354360.

Chemistry databases

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiQ9Y6N6.
PhosphoSitePlusiQ9Y6N6.

Polymorphism and mutation databases

BioMutaiLAMC3.
DMDMi308153586.

Proteomic databases

EPDiQ9Y6N6.
MaxQBiQ9Y6N6.
PaxDbiQ9Y6N6.
PeptideAtlasiQ9Y6N6.
PRIDEiQ9Y6N6.

Protocols and materials databases

DNASUi10319.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361069; ENSP00000354360; ENSG00000050555.
GeneIDi10319.
KEGGihsa:10319.
UCSCiuc004caa.2. human.

Organism-specific databases

CTDi10319.
DisGeNETi10319.
GeneCardsiLAMC3.
H-InvDBHIX0008477.
HGNCiHGNC:6494. LAMC3.
HPAiHPA022814.
MalaCardsiLAMC3.
MIMi604349. gene.
614115. phenotype.
neXtProtiNX_Q9Y6N6.
OpenTargetsiENSG00000050555.
Orphaneti280640. Occipital pachygyria and polymicrogyria.
PharmGKBiPA30282.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IP68. Eukaryota.
ENOG4111F9V. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ9Y6N6.
KOiK06247.
OMAiAGCSSCF.
OrthoDBiEOG091G005L.
PhylomeDBiQ9Y6N6.
TreeFamiTF352481.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000050555-MONOMER.
ReactomeiR-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-8874081. MET activates PTK2 signaling.

Miscellaneous databases

ChiTaRSiLAMC3. human.
GeneWikiiLAMC3.
GenomeRNAii10319.
PROiQ9Y6N6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000050555.
CleanExiHS_LAMC3.
ExpressionAtlasiQ9Y6N6. baseline and differential.
GenevisibleiQ9Y6N6. HS.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMC3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6N6
Secondary accession number(s): B1APX9, B1APY0, Q59H72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 153 of the entry and version 3 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 9
    Human chromosome 9: 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.