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Protein

AP-1 complex subunit sigma-1A

Gene

AP1S1

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

Functioni

Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.1 Publication

GO - Molecular functioni

  1. protein transporter activity Source: InterPro

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. intracellular protein transport Source: InterPro
  3. membrane organization Source: Reactome
  4. post-Golgi vesicle-mediated transport Source: Reactome
  5. receptor-mediated endocytosis Source: UniProtKB
  6. regulation of defense response to virus by virus Source: Reactome
  7. response to virus Source: UniProtKB
  8. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_121399. MHC class II antigen presentation.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1 complex subunit sigma-1A
Alternative name(s):
Adaptor protein complex AP-1 subunit sigma-1A
Adaptor-related protein complex 1 subunit sigma-1A
Clathrin assembly protein complex 1 sigma-1A small chain
Clathrin coat assembly protein AP19
Golgi adaptor HA1/AP1 adaptin sigma-1A subunit
HA1 19 kDa subunit
Sigma 1a subunit of AP-1 clathrin
Sigma-adaptin 1A
Sigma1A-adaptin
Gene namesi
Name:AP1S1
Synonyms:AP19, CLAPS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:559. AP1S1.

Subcellular locationi

Golgi apparatus 1 Publication. Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Membraneclathrin-coated pit 1 Publication
Note: Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.

GO - Cellular componenti

  1. AP-1 adaptor complex Source: UniProtKB
  2. coated pit Source: UniProtKB-SubCell
  3. cytoplasmic vesicle membrane Source: Reactome
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
  6. Golgi membrane Source: Reactome
  7. lysosomal membrane Source: Reactome
  8. membrane Source: UniProtKB
  9. trans-Golgi network membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Mental retardation, enteropathy, deafness, peripheral neuropathy, ichthyosis, and keratoderma (MEDNIK)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by erythematous skin lesions and hyperkeratosis, severe psychomotor retardation, peripheral neuropathy, sensorineural hearing loss, together with elevated very-long-chain fatty acids and severe congenital diarrhea.

See also OMIM:609313

Keywords - Diseasei

Deafness, Ichthyosis, Mental retardation, Neuropathy

Organism-specific databases

MIMi609313. phenotype.
Orphaneti171851. MEDNIK syndrome.
PharmGKBiPA24850.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158AP-1 complex subunit sigma-1APRO_0000193797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP61966.
PaxDbiP61966.
PRIDEiP61966.

PTM databases

PhosphoSiteiP61966.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Up-regulated in response to enterovirus 71 (EV71) infection.1 Publication

Gene expression databases

BgeeiP61966.
CleanExiHS_AP1S1.
ExpressionAtlasiP61966. baseline and differential.
GenevestigatoriP61966.

Organism-specific databases

HPAiHPA060945.

Interactioni

Subunit structurei

Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3).

Protein-protein interaction databases

BioGridi107588. 14 interactions.
MINTiMINT-5006039.
STRINGi9606.ENSP00000336666.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Beta strandi14 – 218Combined sources
Helixi25 – 4016Combined sources
Beta strandi48 – 525Combined sources
Beta strandi55 – 628Combined sources
Beta strandi65 – 717Combined sources
Helixi77 – 9519Combined sources
Helixi100 – 1056Combined sources
Helixi107 – 11711Combined sources
Beta strandi122 – 1243Combined sources
Helixi128 – 14619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P6ZX-ray3.00S1-158[»]
ProteinModelPortaliP61966.
SMRiP61966. Positions 1-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5030.
GeneTreeiENSGT00530000062839.
HOVERGENiHBG050517.
InParanoidiP61966.
KOiK12394.
OrthoDBiEOG7S7SGC.
PhylomeDBiP61966.
TreeFamiTF312921.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P61966-1) [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
MMRFMLLFSR QGKLRLQKWY LATSDKERKK MVRELMQVVL ARKPKMCSFL
60 70 80 90 100
EWRDLKVVYK RYASLYFCCA IEGQDNELIT LELIHRYVEL LDKYFGSVCE
110 120 130 140 150
LDIIFNFEKA YFILDEFLMG GDVQDTSKKS VLKAIEQADL LQEEDESPRS

VLEEMGLA
Length:158
Mass (Da):18,733
Last modified:June 6, 2004 - v1
Checksum:iE461937790406D8B
GO
Isoform 2 (identifier: P61966-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-158: KKSVLKAIEQADLLQEEDESPRSVLEEMGLA → TFPFSH

Show »
Length:133
Mass (Da):16,011
Checksum:i3FB1FD64446EBFD6
GO

Sequence cautioni

The sequence AAD45829.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei128 – 15831KKSVL…EMGLA → TFPFSH in isoform 2. 2 PublicationsVSP_000171Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015319 mRNA. Translation: BAA33391.1.
BT006779 mRNA. Translation: AAP35425.1.
AK312151 mRNA. Translation: BAG35085.1.
AC004876 Genomic DNA. Translation: AAD45829.1. Different initiation.
CH471197 Genomic DNA. Translation: EAW50199.1.
BC003561 mRNA. Translation: AAH03561.1.
CCDSiCCDS47669.1.
RefSeqiNP_001274.1. NM_001283.3. [P61966-1]
UniGeneiHs.489365.

Genome annotation databases

EnsembliENST00000337619; ENSP00000336666; ENSG00000106367. [P61966-1]
ENST00000443943; ENSP00000410780; ENSG00000106367. [P61966-1]
GeneIDi1174.
KEGGihsa:1174.
UCSCiuc003uxv.4. human.

Polymorphism databases

DMDMi48428719.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015319 mRNA. Translation: BAA33391.1.
BT006779 mRNA. Translation: AAP35425.1.
AK312151 mRNA. Translation: BAG35085.1.
AC004876 Genomic DNA. Translation: AAD45829.1. Different initiation.
CH471197 Genomic DNA. Translation: EAW50199.1.
BC003561 mRNA. Translation: AAH03561.1.
CCDSiCCDS47669.1.
RefSeqiNP_001274.1. NM_001283.3. [P61966-1]
UniGeneiHs.489365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P6ZX-ray3.00S1-158[»]
ProteinModelPortaliP61966.
SMRiP61966. Positions 1-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107588. 14 interactions.
MINTiMINT-5006039.
STRINGi9606.ENSP00000336666.

PTM databases

PhosphoSiteiP61966.

Polymorphism databases

DMDMi48428719.

Proteomic databases

MaxQBiP61966.
PaxDbiP61966.
PRIDEiP61966.

Protocols and materials databases

DNASUi1174.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337619; ENSP00000336666; ENSG00000106367. [P61966-1]
ENST00000443943; ENSP00000410780; ENSG00000106367. [P61966-1]
GeneIDi1174.
KEGGihsa:1174.
UCSCiuc003uxv.4. human.

Organism-specific databases

CTDi1174.
GeneCardsiGC07P100797.
HGNCiHGNC:559. AP1S1.
HPAiHPA060945.
MIMi603531. gene.
609313. phenotype.
neXtProtiNX_P61966.
Orphaneti171851. MEDNIK syndrome.
PharmGKBiPA24850.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5030.
GeneTreeiENSGT00530000062839.
HOVERGENiHBG050517.
InParanoidiP61966.
KOiK12394.
OrthoDBiEOG7S7SGC.
PhylomeDBiP61966.
TreeFamiTF312921.

Enzyme and pathway databases

ReactomeiREACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_121399. MHC class II antigen presentation.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiAP1S1. human.
GeneWikiiAP1S1.
GenomeRNAii1174.
NextBioi4850.
PROiP61966.
SOURCEiSearch...

Gene expression databases

BgeeiP61966.
CleanExiHS_AP1S1.
ExpressionAtlasiP61966. baseline and differential.
GenevestigatoriP61966.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of novel clathrin adaptor-related proteins."
    Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.
    J. Biol. Chem. 273:24693-24700(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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 2).
  3. "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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Caudate nucleus.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 2).
    Tissue: Placenta.
  7. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Disruption of AP1S1, causing a novel neurocutaneous syndrome, perturbs development of the skin and spinal cord."
    Montpetit A., Cote S., Brustein E., Drouin C.A., Lapointe L., Boudreau M., Meloche C., Drouin R., Hudson T.J., Drapeau P., Cossette P.
    PLoS Genet. 4:E1000296-E1000296(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MEDNIK.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAP1S1_HUMAN
AccessioniPrimary (citable) accession number: P61966
Secondary accession number(s): B2R5D8
, P82267, Q00382, Q53YA7, Q9BTN4, Q9UDW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2004
Last sequence update: June 6, 2004
Last modified: March 3, 2015
This is version 108 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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.