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 beta-3

Gene

LAMB3

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:G66-33215-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.
SIGNORiQ13751.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-3
Alternative name(s):
Epiligrin subunit bata
Kalinin B1 chain
Kalinin subunit beta
Laminin B1k chain
Laminin-5 subunit beta
Nicein subunit beta
Gene namesi
Name:LAMB3
Synonyms:LAMNB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6490. LAMB3.

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)1 Publication
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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004171679P → L in H-JEB. 1 PublicationCorresponds to variant rs201223111dbSNPEnsembl.1
Generalized atrophic benign epidermolysis bullosa (GABEB)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities.
See also OMIM:226650
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037310199G → A in GABEB; somatic second-site mutation. 1 PublicationCorresponds to variant rs121912486dbSNPEnsembl.1
Natural variantiVAR_037311207K → Q in GABEB; somatic second-site mutation. 1 PublicationCorresponds to variant rs121912487dbSNPEnsembl.1
Natural variantiVAR_004170210E → K in GABEB. 2 PublicationsCorresponds to variant rs121912482dbSNPEnsembl.1
Amelogenesis imperfecta 1A (AI1A)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of amelogenesis imperfecta, a disorder characterized by defective enamel formation. The enamel may be hypoplastic, hypomineralized or both, and affected teeth may be discoloured, sensitive or prone to disintegration.
See also OMIM:104530

Keywords - Diseasei

Amelogenesis imperfecta, Disease mutation, Epidermolysis bullosa

Organism-specific databases

DisGeNETi3914.
MalaCardsiLAMB3.
MIMi104530. phenotype.
226650. phenotype.
226700. phenotype.
OpenTargetsiENSG00000196878.
Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
100031. Hypoplastic amelogenesis imperfecta.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBiPA30278.

Chemistry databases

ChEMBLiCHEMBL2364187.

Polymorphism and mutation databases

BioMutaiLAMB3.
DMDMi2497600.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000001707118 – 1172Laminin subunit beta-3Add BLAST1155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi220N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi250 ↔ 259PROSITE-ProRule annotation
Disulfide bondi252 ↔ 279PROSITE-ProRule annotation
Disulfide bondi281 ↔ 290PROSITE-ProRule annotation
Disulfide bondi293 ↔ 313PROSITE-ProRule annotation
Disulfide bondi316 ↔ 325PROSITE-ProRule annotation
Disulfide bondi318 ↔ 343PROSITE-ProRule annotation
Disulfide bondi346 ↔ 355PROSITE-ProRule annotation
Disulfide bondi358 ↔ 376PROSITE-ProRule annotation
Disulfide bondi379 ↔ 392PROSITE-ProRule annotation
Disulfide bondi381 ↔ 399PROSITE-ProRule annotation
Disulfide bondi401 ↔ 410PROSITE-ProRule annotation
Disulfide bondi413 ↔ 428PROSITE-ProRule annotation
Disulfide bondi431 ↔ 444PROSITE-ProRule annotation
Disulfide bondi433 ↔ 451PROSITE-ProRule annotation
Disulfide bondi453 ↔ 462PROSITE-ProRule annotation
Disulfide bondi465 ↔ 478PROSITE-ProRule annotation
Disulfide bondi481 ↔ 493PROSITE-ProRule annotation
Disulfide bondi483 ↔ 500PROSITE-ProRule annotation
Disulfide bondi502 ↔ 511PROSITE-ProRule annotation
Disulfide bondi519 ↔ 531PROSITE-ProRule annotation
Disulfide bondi534 ↔ 546PROSITE-ProRule annotation
Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
Disulfide bondi555 ↔ 564PROSITE-ProRule annotation
Disulfide bondi567 ↔ 578PROSITE-ProRule annotation
Disulfide bondi581InterchainCurated
Disulfide bondi584InterchainCurated
Glycosylationi604N-linked (GlcNAc...)Sequence analysis1
Glycosylationi810N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1171InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ13751.
MaxQBiQ13751.
PaxDbiQ13751.
PeptideAtlasiQ13751.
PRIDEiQ13751.

PTM databases

iPTMnetiQ13751.
PhosphoSitePlusiQ13751.
SwissPalmiQ13751.

Miscellaneous databases

PMAP-CutDBQ13751.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

BgeeiENSG00000196878.
CleanExiHS_LAMB3.
ExpressionAtlasiQ13751. baseline and differential.
GenevisibleiQ13751. HS.

Organism-specific databases

HPAiHPA008069.

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. Beta-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1.1 Publication

Protein-protein interaction databases

BioGridi110108. 22 interactors.
IntActiQ13751. 21 interactors.
MINTiMINT-4053402.
STRINGi9606.ENSP00000348384.

Structurei

3D structure databases

ProteinModelPortaliQ13751.
SMRiQ13751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 249Laminin N-terminalPROSITE-ProRule annotationAdd BLAST228
Domaini250 – 315Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST66
Domaini316 – 378Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST63
Domaini379 – 430Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST52
Domaini431 – 480Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST50
Domaini481 – 533Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST53
Domaini534 – 580Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni579 – 785Domain IIAdd BLAST207
Regioni786 – 816Domain alphaAdd BLAST31
Regioni817 – 1170Domain IAdd BLAST354

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili723 – 757Sequence analysisAdd BLAST35
Coiled coili831 – 884Sequence analysisAdd BLAST54
Coiled coili948 – 1133Sequence analysisAdd BLAST186

Domaini

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

Sequence similaritiesi

Contains 6 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000113279.
HOVERGENiHBG052302.
InParanoidiQ13751.
KOiK06244.
OMAiRVLYYAT.
OrthoDBiEOG091G019I.
PhylomeDBiQ13751.
TreeFamiTF352481.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR002049. Laminin_EGF.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 5 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q13751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPFFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LRASSTCGLT
60 70 80 90 100
KPETYCTQYG EWQMKCCKCD SRQPHNYYSH RVENVASSSG PMRWWQSQND
110 120 130 140 150
VNPVSLQLDL DRRFQLQEVM MEFQGPMPAG MLIERSSDFG KTWRVYQYLA
160 170 180 190 200
ADCTSTFPRV RQGRPQSWQD VRCQSLPQRP NARLNGGKVQ LNLMDLVSGI
210 220 230 240 250
PATQSQKIQE VGEITNLRVN FTRLAPVPQR GYHPPSAYYA VSQLRLQGSC
260 270 280 290 300
FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR
310 320 330 340 350
PWRPAEGQDA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT
360 370 380 390 400
EGKNCERCQL HYFRNRRPGA SIQETCISCE CDPDGAVPGA PCDPVTGQCV
410 420 430 440 450
CKEHVQGERC DLCKPGFTGL TYANPQGCHR CDCNILGSRR DMPCDEESGR
460 470 480 490 500
CLCLPNVVGP KCDQCAPYHW KLASGQGCEP CACDPHNSLS PQCNQFTGQC
510 520 530 540 550
PCREGFGGLM CSAAAIRQCP DRTYGDVATG CRACDCDFRG TEGPGCDKAS
560 570 580 590 600
GRCLCRPGLT GPRCDQCQRG YCNRYPVCVA CHPCFQTYDA DLREQALRFG
610 620 630 640 650
RLRNATASLW SGPGLEDRGL ASRILDAKSK IEQIRAVLSS PAVTEQEVAQ
660 670 680 690 700
VASAILSLRR TLQGLQLDLP LEEETLSLPR DLESLDRSFN GLLTMYQRKR
710 720 730 740 750
EQFEKISSAD PSGAFRMLST AYEQSAQAAQ QVSDSSRLLD QLRDSRREAE
760 770 780 790 800
RLVRQAGGGG GTGSPKLVAL RLEMSSLPDL TPTFNKLCGN SRQMACTPIS
810 820 830 840 850
CPGELCPQDN GTACGSRCRG VLPRAGGAFL MAGQVAEQLR GFNAQLQRTR
860 870 880 890 900
QMIRAAEESA SQIQSSAQRL ETQVSASRSQ MEEDVRRTRL LIQQVRDFLT
910 920 930 940 950
DPDTDAATIQ EVSEAVLALW LPTDSATVLQ KMNEIQAIAA RLPNVDLVLS
960 970 980 990 1000
QTKQDIARAR RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT
1010 1020 1030 1040 1050
MQGTSRSLRL IQDRVAEVQQ VLRPAEKLVT SMTKQLGDFW TRMEELRHQA
1060 1070 1080 1090 1100
RQQGAEAVQA QQLAEGASEQ ALSAQEGFER IKQKYAELKD RLGQSSMLGE
1110 1120 1130 1140 1150
QGARIQSVKT EAEELFGETM EMMDRMKDME LELLRGSQAI MLRSADLTGL
1160 1170
EKRVEQIRDH INGRVLYYAT CK
Length:1,172
Mass (Da):129,572
Last modified:November 1, 1996 - v1
Checksum:i61BC1A60BBD4FA05
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti124Q → R in AAA61834 (PubMed:7512558).Curated1
Sequence conflicti269Missing in AAA61834 (PubMed:7512558).Curated1
Sequence conflicti388P → A in AAA61834 (PubMed:7512558).Curated1
Sequence conflicti426 – 427QG → RR in AAA61834 (PubMed:7512558).Curated2
Sequence conflicti440 – 441RD → E in AAA61834 (PubMed:7512558).Curated2
Sequence conflicti489 – 500LSPQC…FTGQC → PQPTVQPVHRAV in BAA22263 (PubMed:8530036).CuratedAdd BLAST12
Sequence conflicti603R → P in AAA61834 (PubMed:7512558).Curated1
Sequence conflicti815G → A in AAA61834 (PubMed:7512558).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037309181N → D.Corresponds to variant rs2235542dbSNPEnsembl.1
Natural variantiVAR_037310199G → A in GABEB; somatic second-site mutation. 1 PublicationCorresponds to variant rs121912486dbSNPEnsembl.1
Natural variantiVAR_037311207K → Q in GABEB; somatic second-site mutation. 1 PublicationCorresponds to variant rs121912487dbSNPEnsembl.1
Natural variantiVAR_004170210E → K in GABEB. 2 PublicationsCorresponds to variant rs121912482dbSNPEnsembl.1
Natural variantiVAR_037312292R → L.Corresponds to variant rs12091253dbSNPEnsembl.1
Natural variantiVAR_034060438S → T.Corresponds to variant rs2229468dbSNPEnsembl.1
Natural variantiVAR_035820450R → C in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs200895463dbSNPEnsembl.1
Natural variantiVAR_037313527V → M.Corresponds to variant rs2076349dbSNPEnsembl.1
Natural variantiVAR_004171679P → L in H-JEB. 1 PublicationCorresponds to variant rs201223111dbSNPEnsembl.1
Natural variantiVAR_034061690N → S.Corresponds to variant rs2229466dbSNPEnsembl.1
Natural variantiVAR_034062852M → L.1 PublicationCorresponds to variant rs12748250dbSNPEnsembl.1
Natural variantiVAR_037314926A → D.Corresponds to variant rs2076222dbSNPEnsembl.1
Natural variantiVAR_034063988R → W.Corresponds to variant rs2229467dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25541 mRNA. Translation: AAA61834.1.
U17760
, U17745, U17746, U17747, U17748, U17749, U17750, U17751, U17752, U17753, U17754, U17755, U17756, U17757, U17758, U17759 Genomic DNA. Translation: AAC51352.1.
D37766 mRNA. Translation: BAA22263.1.
AY035783 mRNA. Translation: AAK61364.1.
AL023754 Genomic DNA. Translation: CAA19297.2.
AL023754, AL031316 Genomic DNA. Translation: CAI19989.1.
AL031316, AL023754 Genomic DNA. Translation: CAI20062.1.
CH471100 Genomic DNA. Translation: EAW93448.1.
CH471100 Genomic DNA. Translation: EAW93449.1.
BC075838 mRNA. Translation: AAH75838.1.
CCDSiCCDS1487.1.
PIRiA53612.
RefSeqiNP_000219.2. NM_000228.2.
NP_001017402.1. NM_001017402.1.
NP_001121113.1. NM_001127641.1.
XP_005273181.1. XM_005273124.4.
UniGeneiHs.497636.

Genome annotation databases

EnsembliENST00000356082; ENSP00000348384; ENSG00000196878.
ENST00000367030; ENSP00000355997; ENSG00000196878.
ENST00000391911; ENSP00000375778; ENSG00000196878.
GeneIDi3914.
KEGGihsa:3914.
UCSCiuc001hhg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25541 mRNA. Translation: AAA61834.1.
U17760
, U17745, U17746, U17747, U17748, U17749, U17750, U17751, U17752, U17753, U17754, U17755, U17756, U17757, U17758, U17759 Genomic DNA. Translation: AAC51352.1.
D37766 mRNA. Translation: BAA22263.1.
AY035783 mRNA. Translation: AAK61364.1.
AL023754 Genomic DNA. Translation: CAA19297.2.
AL023754, AL031316 Genomic DNA. Translation: CAI19989.1.
AL031316, AL023754 Genomic DNA. Translation: CAI20062.1.
CH471100 Genomic DNA. Translation: EAW93448.1.
CH471100 Genomic DNA. Translation: EAW93449.1.
BC075838 mRNA. Translation: AAH75838.1.
CCDSiCCDS1487.1.
PIRiA53612.
RefSeqiNP_000219.2. NM_000228.2.
NP_001017402.1. NM_001017402.1.
NP_001121113.1. NM_001127641.1.
XP_005273181.1. XM_005273124.4.
UniGeneiHs.497636.

3D structure databases

ProteinModelPortaliQ13751.
SMRiQ13751.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110108. 22 interactors.
IntActiQ13751. 21 interactors.
MINTiMINT-4053402.
STRINGi9606.ENSP00000348384.

Chemistry databases

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiQ13751.
PhosphoSitePlusiQ13751.
SwissPalmiQ13751.

Polymorphism and mutation databases

BioMutaiLAMB3.
DMDMi2497600.

Proteomic databases

EPDiQ13751.
MaxQBiQ13751.
PaxDbiQ13751.
PeptideAtlasiQ13751.
PRIDEiQ13751.

Protocols and materials databases

DNASUi3914.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356082; ENSP00000348384; ENSG00000196878.
ENST00000367030; ENSP00000355997; ENSG00000196878.
ENST00000391911; ENSP00000375778; ENSG00000196878.
GeneIDi3914.
KEGGihsa:3914.
UCSCiuc001hhg.4. human.

Organism-specific databases

CTDi3914.
DisGeNETi3914.
GeneCardsiLAMB3.
GeneReviewsiLAMB3.
HGNCiHGNC:6490. LAMB3.
HPAiHPA008069.
MalaCardsiLAMB3.
MIMi104530. phenotype.
150310. gene.
226650. phenotype.
226700. phenotype.
neXtProtiNX_Q13751.
OpenTargetsiENSG00000196878.
Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
100031. Hypoplastic amelogenesis imperfecta.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBiPA30278.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000113279.
HOVERGENiHBG052302.
InParanoidiQ13751.
KOiK06244.
OMAiRVLYYAT.
OrthoDBiEOG091G019I.
PhylomeDBiQ13751.
TreeFamiTF352481.

Enzyme and pathway databases

BioCyciZFISH:G66-33215-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.
SIGNORiQ13751.

Miscellaneous databases

ChiTaRSiLAMB3. human.
GeneWikiiLaminin,_beta_3.
GenomeRNAii3914.
PMAP-CutDBQ13751.
PROiQ13751.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196878.
CleanExiHS_LAMB3.
ExpressionAtlasiQ13751. baseline and differential.
GenevisibleiQ13751. HS.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR002049. Laminin_EGF.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 5 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMB3_HUMAN
AccessioniPrimary (citable) accession number: Q13751
Secondary accession number(s): D3DT88
, O14947, Q14733, Q9UJK4, Q9UJL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 171 of the entry and version 1 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 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.