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Protein

Microtubule-associated proteins 1A/1B light chain 3A

Gene

MAP1LC3A

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

Functioni

Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1212Cleavage; by ATG4BBy similarity

GO - Molecular functioni

  1. GABA receptor binding Source: GO_Central
  2. microtubule binding Source: GO_Central
  3. phosphatidylethanolamine binding Source: UniProtKB
  4. phospholipid binding Source: UniProtKB

GO - Biological processi

  1. autophagic vacuole assembly Source: UniProtKB
  2. cellular response to nitrogen starvation Source: GO_Central
  3. membrane fusion Source: GO_Central
  4. mitochondrion degradation Source: MGI
  5. nucleophagy Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Autophagy, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated proteins 1A/1B light chain 3A
Alternative name(s):
Autophagy-related protein LC3 A
Autophagy-related ubiquitin-like modifier LC3 A
MAP1 light chain 3-like protein 1
MAP1A/MAP1B light chain 3 A
Short name:
MAP1A/MAP1B LC3 A
Microtubule-associated protein 1 light chain 3 alpha
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:6838. MAP1LC3A.

Subcellular locationi

GO - Cellular componenti

  1. autophagic vacuole Source: UniProtKB
  2. autophagic vacuole membrane Source: GO_Central
  3. cytoplasmic vesicle Source: UniProtKB-KW
  4. cytosol Source: UniProtKB
  5. extrinsic component of membrane Source: GO_Central
  6. late endosome Source: Ensembl
  7. microtubule Source: UniProtKB-KW
  8. organelle membrane Source: UniProtKB
  9. pre-autophagosomal structure Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201G → A: No processing of precursor. 1 Publication

Organism-specific databases

PharmGKBiPA30582.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 120119Microtubule-associated proteins 1A/1B light chain 3APRO_0000017192Add
BLAST
Propeptidei121 – 1211Removed in mature formPRO_0000017193

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine; by PKA1 Publication
Lipidationi120 – 1201Phosphatidylethanolamine amidated glycine1 Publication

Post-translational modificationi

The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094).1 Publication
The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine.1 Publication
Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity.2 Publications

Keywords - PTMi

Lipoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9H492.
PaxDbiQ9H492.
PRIDEiQ9H492.

PTM databases

PhosphoSiteiQ9H492.

Miscellaneous databases

PMAP-CutDBQ9H492.

Expressioni

Tissue specificityi

Most abundant in heart, brain, liver, skeletal muscle and testis but absent in thymus and peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiQ9H492.
CleanExiHS_MAP1LC3A.
GenevestigatoriQ9H492.

Organism-specific databases

HPAiCAB037174.
HPA007649.
HPA052474.
HPA052484.

Interactioni

Subunit structurei

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity). Interacts with SQSTM1 (By similarity). Interacts with TP53INP1 and TP53INP2. Directly interacts with SQSTM1; this interaction leads to MAP1LC3A recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG13 and ULK1. Interacts with TBC1D5 (PubMed:22354992).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bnip3lQ9Z2F77EBI-720768,EBI-1774669From a different organism.
NBR1Q145965EBI-720768,EBI-742698
SQSTM1Q135017EBI-720768,EBI-307104
TOLLIPQ9H0E23EBI-720768,EBI-74615
UBQLN4Q9NRR53EBI-720768,EBI-711226

Protein-protein interaction databases

BioGridi124137. 110 interactions.
DIPiDIP-49052N.
IntActiQ9H492. 381 interactions.
MINTiMINT-1420598.
STRINGi9606.ENSP00000363970.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi7 – 104Combined sources
Helixi13 – 2614Combined sources
Beta strandi30 – 378Combined sources
Beta strandi42 – 443Combined sources
Beta strandi51 – 555Combined sources
Helixi60 – 7011Combined sources
Beta strandi80 – 834Combined sources
Turni84 – 863Combined sources
Beta strandi91 – 933Combined sources
Helixi95 – 1028Combined sources
Beta strandi109 – 1168Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ECIX-ray2.65A/B1-121[»]
3WALX-ray2.00A2-121[»]
3WANX-ray1.77A/B2-121[»]
ProteinModelPortaliQ9H492.
SMRiQ9H492. Positions 2-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H492.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATG8 family.Curated

Phylogenomic databases

eggNOGiNOG264390.
GeneTreeiENSGT00390000012937.
HOGENOMiHOG000232034.
HOVERGENiHBG051706.
InParanoidiQ9H492.
KOiK10435.
OMAiRTFADRC.
OrthoDBiEOG7XH6RV.
PhylomeDBiQ9H492.
TreeFamiTF312964.

Family and domain databases

InterProiIPR004241. Atg8_like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10969. PTHR10969. 1 hit.
PfamiPF02991. Atg8. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.

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 1 (identifier: Q9H492-1) [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
MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT
60 70 80 90 100
KFLVPDHVNM SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE
110 120
QEKDEDGFLY MVYASQETFG F
Length:121
Mass (Da):14,272
Last modified:May 10, 2005 - v2
Checksum:i48C1FBE8F7892AF3
GO
Isoform 2 (identifier: Q9H492-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MPSDRPFKQRRSF → MKMRFFSSPCGKAAVDP

Note: No experimental confirmation available.

Show »
Length:125
Mass (Da):14,493
Checksum:i097697B5424FC425
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313MPSDR…QRRSF → MKMRFFSSPCGKAAVDP in isoform 2. CuratedVSP_013660Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF276658 mRNA. Translation: AAK35151.1.
BT007452 mRNA. Translation: AAP36120.1.
AL833855 mRNA. Translation: CAD38714.1.
AL118520 Genomic DNA. Translation: CAC14078.1.
AL118520 Genomic DNA. Translation: CAI40290.1.
CH471077 Genomic DNA. Translation: EAW76263.1.
CH471077 Genomic DNA. Translation: EAW76264.1.
CH471077 Genomic DNA. Translation: EAW76265.1.
CH471077 Genomic DNA. Translation: EAW76266.1.
BC015810 mRNA. Translation: AAH15810.1.
CCDSiCCDS13237.1. [Q9H492-2]
CCDS13238.1. [Q9H492-1]
RefSeqiNP_115903.1. NM_032514.3. [Q9H492-1]
NP_852610.1. NM_181509.2. [Q9H492-2]
XP_005260634.1. XM_005260577.1. [Q9H492-1]
UniGeneiHs.632273.

Genome annotation databases

EnsembliENST00000360668; ENSP00000353886; ENSG00000101460. [Q9H492-1]
ENST00000374837; ENSP00000363970; ENSG00000101460. [Q9H492-2]
ENST00000397709; ENSP00000380821; ENSG00000101460. [Q9H492-1]
GeneIDi84557.
KEGGihsa:84557.
UCSCiuc002xap.2. human. [Q9H492-2]
uc002xaq.2. human. [Q9H492-1]

Polymorphism databases

DMDMi85701362.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF276658 mRNA. Translation: AAK35151.1.
BT007452 mRNA. Translation: AAP36120.1.
AL833855 mRNA. Translation: CAD38714.1.
AL118520 Genomic DNA. Translation: CAC14078.1.
AL118520 Genomic DNA. Translation: CAI40290.1.
CH471077 Genomic DNA. Translation: EAW76263.1.
CH471077 Genomic DNA. Translation: EAW76264.1.
CH471077 Genomic DNA. Translation: EAW76265.1.
CH471077 Genomic DNA. Translation: EAW76266.1.
BC015810 mRNA. Translation: AAH15810.1.
CCDSiCCDS13237.1. [Q9H492-2]
CCDS13238.1. [Q9H492-1]
RefSeqiNP_115903.1. NM_032514.3. [Q9H492-1]
NP_852610.1. NM_181509.2. [Q9H492-2]
XP_005260634.1. XM_005260577.1. [Q9H492-1]
UniGeneiHs.632273.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ECIX-ray2.65A/B1-121[»]
3WALX-ray2.00A2-121[»]
3WANX-ray1.77A/B2-121[»]
ProteinModelPortaliQ9H492.
SMRiQ9H492. Positions 2-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124137. 110 interactions.
DIPiDIP-49052N.
IntActiQ9H492. 381 interactions.
MINTiMINT-1420598.
STRINGi9606.ENSP00000363970.

PTM databases

PhosphoSiteiQ9H492.

Polymorphism databases

DMDMi85701362.

Proteomic databases

MaxQBiQ9H492.
PaxDbiQ9H492.
PRIDEiQ9H492.

Protocols and materials databases

DNASUi84557.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360668; ENSP00000353886; ENSG00000101460. [Q9H492-1]
ENST00000374837; ENSP00000363970; ENSG00000101460. [Q9H492-2]
ENST00000397709; ENSP00000380821; ENSG00000101460. [Q9H492-1]
GeneIDi84557.
KEGGihsa:84557.
UCSCiuc002xap.2. human. [Q9H492-2]
uc002xaq.2. human. [Q9H492-1]

Organism-specific databases

CTDi84557.
GeneCardsiGC20P033134.
HGNCiHGNC:6838. MAP1LC3A.
HPAiCAB037174.
HPA007649.
HPA052474.
HPA052484.
MIMi601242. gene.
neXtProtiNX_Q9H492.
PharmGKBiPA30582.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264390.
GeneTreeiENSGT00390000012937.
HOGENOMiHOG000232034.
HOVERGENiHBG051706.
InParanoidiQ9H492.
KOiK10435.
OMAiRTFADRC.
OrthoDBiEOG7XH6RV.
PhylomeDBiQ9H492.
TreeFamiTF312964.

Miscellaneous databases

ChiTaRSiMAP1LC3A. human.
EvolutionaryTraceiQ9H492.
GeneWikiiMAP1LC3A.
GenomeRNAii84557.
NextBioi74441.
PMAP-CutDBQ9H492.
PROiQ9H492.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H492.
CleanExiHS_MAP1LC3A.
GenevestigatoriQ9H492.

Family and domain databases

InterProiIPR004241. Atg8_like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10969. PTHR10969. 1 hit.
PfamiPF02991. Atg8. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B."
    He H., Dang Y., Dai F., Guo Z., Wu J., She X., Pei Y., Chen Y., Ling W., Wu C., Zhao S., Liu J.O., Yu L.
    J. Biol. Chem. 278:29278-29287(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-120.
  2. "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 (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
  5. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  7. "The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3."
    Tanida I., Tanida-Miyake E., Ueno T., Kominami E.
    J. Biol. Chem. 276:1701-1706(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG7.
  8. "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p."
    Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.
    J. Biol. Chem. 277:13739-13744(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG3.
  9. "HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates."
    Tanida I., Sou Y.-S., Ezaki J., Minematsu-Ikeguchi N., Ueno T., Kominami E.
    J. Biol. Chem. 279:36268-36276(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPIDATION AT GLY-120, CLEAVAGE BY APG4B.
  10. "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
    Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
    J. Biol. Chem. 282:24131-24145(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
  11. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53INP2.
  12. Cited for: PHOSPHORYLATION AT SER-12 BY PKA, FUNCTION.
  13. "TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death."
    Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.
    Cell Death Differ. 19:1525-1535(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs."
    Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.
    J. Biol. Chem. 287:39275-39290(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG13 AND ULK1.
  15. "Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers."
    Popovic D., Akutsu M., Novak I., Harper J.W., Behrends C., Dikic I.
    Mol. Cell. Biol. 32:1733-1744(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TBC1D5.
  16. "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription."
    Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M., Johansen T., Zorzano A.
    PLoS ONE 7:E34034-E34034(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53INP1 AND TP53INP2.
  17. "The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation."
    Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J., Roy C.R.
    Science 338:1072-1076(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DECONJUGATION BY LEGIONELLA RAVZ.

Entry informationi

Entry nameiMLP3A_HUMAN
AccessioniPrimary (citable) accession number: Q9H492
Secondary accession number(s): E1P5P4, E1P5P5, Q9BXW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 10, 2005
Last modified: April 1, 2015
This is version 123 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, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.