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Protein

Activator of 90 kDa heat shock protein ATPase homolog 1

Gene

AHSA1

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

Functioni

Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking.By similarity

GO - Molecular functioni

  1. ATPase activator activity Source: MGI
  2. chaperone binding Source: MGI

GO - Biological processi

  1. positive regulation of ATPase activity Source: GOC
  2. response to stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Activator of 90 kDa heat shock protein ATPase homolog 1
Short name:
AHA1
Alternative name(s):
p38
Gene namesi
Name:AHSA1
Synonyms:C14orf3
ORF Names:HSPC322
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:1189. AHSA1.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Endoplasmic reticulum 1 Publication
Note: May transiently interact with the endoplasmic reticulum.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB-SubCell
  3. endoplasmic reticulum Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 338337Activator of 90 kDa heat shock protein ATPase homolog 1PRO_0000215820Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei3 – 31N6-acetyllysine1 Publication
Modified residuei193 – 1931Phosphoserine2 Publications
Modified residuei212 – 2121N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95433.
PaxDbiO95433.
PeptideAtlasiO95433.
PRIDEiO95433.

2D gel databases

REPRODUCTION-2DPAGEIPI00030706.

PTM databases

PhosphoSiteiO95433.

Expressioni

Tissue specificityi

Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.1 Publication

Inductioni

By heat shock and treatment with the HSP90 inhibitor 17-demethoxygeldanamycin (17AAG).1 Publication

Gene expression databases

BgeeiO95433.
CleanExiHS_AHSA1.
ExpressionAtlasiO95433. baseline and differential.
GenevestigatoriO95433.

Organism-specific databases

HPAiCAB006244.
HPA000903.

Interactioni

Subunit structurei

Interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatitis virus glycoprotein (VSV G). Interacts with GCH1. Interacts with SRPK1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GCH1P307933EBI-448610,EBI-958183
HSP90AA1P079004EBI-448610,EBI-296047
HSP90AB1P082383EBI-448610,EBI-352572

Protein-protein interaction databases

BioGridi115846. 34 interactions.
IntActiO95433. 24 interactions.
MINTiMINT-5002315.
STRINGi9606.ENSP00000216479.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi206 – 21712Combined sources
Helixi219 – 2257Combined sources
Helixi229 – 2357Combined sources
Turni253 – 2564Combined sources
Beta strandi261 – 2655Combined sources
Turni266 – 2683Combined sources
Beta strandi269 – 2768Combined sources
Beta strandi285 – 2906Combined sources
Beta strandi298 – 30811Combined sources
Helixi309 – 3179Combined sources
Turni318 – 3236Combined sources
Helixi324 – 3307Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X53NMR-A204-335[»]
ProteinModelPortaliO95433.
SMRiO95433. Positions 25-146, 204-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95433.

Family & Domainsi

Sequence similaritiesi

Belongs to the AHA1 family.Curated

Phylogenomic databases

eggNOGiCOG5580.
GeneTreeiENSGT00390000006429.
HOGENOMiHOG000242852.
HOVERGENiHBG065806.
InParanoidiO95433.
OMAiPEVSHEN.
PhylomeDBiO95433.
TreeFamiTF313680.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]
SMARTiSM01000. Aha1_N. 1 hit.
[Graphical view]
SUPFAMiSSF103111. SSF103111. 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. Align

Isoform 1 (identifier: O95433-1) [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
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ
60 70 80 90 100
NEEGKCEVTE VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK
110 120 130 140 150
GHVEIPNLSD ENSVDEVEIS VSLAKDEPDT NLVALMKEEG VKLLREAMGI
160 170 180 190 200
YISTLKTEFT QGMILPTMNG ESVDPVGQPA LKTEERKAKP APSKTQARPV
210 220 230 240 250
GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA TLEADRGGKF
260 270 280 290 300
HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL
310 320 330
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF
Length:338
Mass (Da):38,274
Last modified:May 1, 1999 - v1
Checksum:iE6B686DDD8D7D729
GO
Isoform 2 (identifier: O95433-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-338: HFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF → SHCHSG

Note: No experimental confirmation available.

Show »
Length:288
Mass (Da):32,340
Checksum:i4ACB777F0ED29F4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 682EA → CL in AAF29000. (PubMed:11042152)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei283 – 33856HFATI…GARLF → SHCHSG in isoform 2. 1 PublicationVSP_055797Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243310 mRNA. Translation: CAB45684.1.
AF164791 mRNA. Translation: AAF80755.1.
AK300766 mRNA. Translation: BAG62431.1.
AK313824 mRNA. Translation: BAG36559.1.
AF111168 Genomic DNA. Translation: AAD09623.1.
CH471061 Genomic DNA. Translation: EAW81291.1.
BC000321 mRNA. Translation: AAH00321.1.
BC007398 mRNA. Translation: AAH07398.2.
AF161440 mRNA. Translation: AAF29000.1.
CCDSiCCDS9863.1. [O95433-1]
PIRiJC7769.
RefSeqiNP_036243.1. NM_012111.2. [O95433-1]
UniGeneiHs.204041.

Genome annotation databases

EnsembliENST00000216479; ENSP00000216479; ENSG00000100591. [O95433-1]
ENST00000535854; ENSP00000440108; ENSG00000100591. [O95433-2]
GeneIDi10598.
KEGGihsa:10598.
UCSCiuc001xtw.3. human. [O95433-1]
uc010tvk.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243310 mRNA. Translation: CAB45684.1.
AF164791 mRNA. Translation: AAF80755.1.
AK300766 mRNA. Translation: BAG62431.1.
AK313824 mRNA. Translation: BAG36559.1.
AF111168 Genomic DNA. Translation: AAD09623.1.
CH471061 Genomic DNA. Translation: EAW81291.1.
BC000321 mRNA. Translation: AAH00321.1.
BC007398 mRNA. Translation: AAH07398.2.
AF161440 mRNA. Translation: AAF29000.1.
CCDSiCCDS9863.1. [O95433-1]
PIRiJC7769.
RefSeqiNP_036243.1. NM_012111.2. [O95433-1]
UniGeneiHs.204041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X53NMR-A204-335[»]
ProteinModelPortaliO95433.
SMRiO95433. Positions 25-146, 204-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115846. 34 interactions.
IntActiO95433. 24 interactions.
MINTiMINT-5002315.
STRINGi9606.ENSP00000216479.

PTM databases

PhosphoSiteiO95433.

2D gel databases

REPRODUCTION-2DPAGEIPI00030706.

Proteomic databases

MaxQBiO95433.
PaxDbiO95433.
PeptideAtlasiO95433.
PRIDEiO95433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216479; ENSP00000216479; ENSG00000100591. [O95433-1]
ENST00000535854; ENSP00000440108; ENSG00000100591. [O95433-2]
GeneIDi10598.
KEGGihsa:10598.
UCSCiuc001xtw.3. human. [O95433-1]
uc010tvk.1. human.

Organism-specific databases

CTDi10598.
GeneCardsiGC14P077924.
HGNCiHGNC:1189. AHSA1.
HPAiCAB006244.
HPA000903.
MIMi608466. gene.
neXtProtiNX_O95433.
PharmGKBiPA25515.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5580.
GeneTreeiENSGT00390000006429.
HOGENOMiHOG000242852.
HOVERGENiHBG065806.
InParanoidiO95433.
OMAiPEVSHEN.
PhylomeDBiO95433.
TreeFamiTF313680.

Miscellaneous databases

ChiTaRSiAHSA1. human.
EvolutionaryTraceiO95433.
GeneWikiiAHSA1.
GenomeRNAii10598.
NextBioi35475259.
PROiO95433.
SOURCEiSearch...

Gene expression databases

BgeeiO95433.
CleanExiHS_AHSA1.
ExpressionAtlasiO95433. baseline and differential.
GenevestigatoriO95433.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]
SMARTiSM01000. Aha1_N. 1 hit.
[Graphical view]
SUPFAMiSSF103111. SSF103111. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a novel gene underexpressed in Down syndrome."
    Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E., Scott H.S.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Ovary.
  7. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-338 (ISOFORM 1).
    Tissue: Umbilical cord blood.
  8. "p38: a novel protein that associates with the vesicular stomatitis virus glycoprotein."
    Sevier C.S., Machamer C.E.
    Biochem. Biophys. Res. Commun. 287:574-582(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VSV G, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. Cited for: INTERACTION WITH HSPCA, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
  10. "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."
    Lotz G.P., Lin H., Harst A., Obermann W.M.J.
    J. Biol. Chem. 278:17228-17235(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPCA.
  11. "A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions."
    Swick L., Kapatos G.
    J. Neurochem. 97:1447-1455(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCH1.
  12. "Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones."
    Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.
    Genes Dev. 23:482-495(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRPK1.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-3 AND LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "The solution structure of the C-terminal domain of human activator of 90 kDa heat shock protein ATPase homolog 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 204-335.

Entry informationi

Entry nameiAHSA1_HUMAN
AccessioniPrimary (citable) accession number: O95433
Secondary accession number(s): B2R9L2
, B4DUR9, Q96IL6, Q9P060
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 136 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 14
    Human chromosome 14: 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.