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Protein

V-type proton ATPase subunit S1

Gene

ATP6AP1

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

Functioni

Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
  4. Rab GTPase binding Source: UniProtKB
  5. transporter activity Source: ProtInc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular iron ion homeostasis Source: Reactome
  3. establishment of organelle localization Source: UniProtKB
  4. insulin receptor signaling pathway Source: Reactome
  5. pH reduction Source: UniProtKB
  6. positive regulation of bone resorption Source: UniProtKB
  7. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  8. positive regulation of exocytosis Source: UniProtKB
  9. positive regulation of osteoblast differentiation Source: UniProtKB
  10. positive regulation of osteoclast development Source: UniProtKB
  11. proton transport Source: ProtInc
  12. transferrin transport Source: Reactome
  13. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01034-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_25283. Transferrin endocytosis and recycling.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit S1
Short name:
V-ATPase subunit S1
Alternative name(s):
Protein XAP-3
V-ATPase Ac45 subunit
V-ATPase S1 accessory protein
Vacuolar proton pump subunit S1
Gene namesi
Name:ATP6AP1
Synonyms:ATP6IP1, ATP6S1, VATPS1, XAP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:868. ATP6AP1.

Subcellular locationi

Vacuole membrane By similarity; Single-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 419378VacuolarSequence AnalysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence AnalysisAdd
BLAST
Topological domaini441 – 47030CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endosome membrane Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. proton-transporting two-sector ATPase complex Source: ProtInc
  5. proton-transporting V-type ATPase, V1 domain Source: InterPro
  6. vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Sequence AnalysisAdd
BLAST
Chaini42 – 470429V-type proton ATPase subunit S1PRO_0000002543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi261 – 2611N-linked (GlcNAc...)1 Publication
Glycosylationi273 – 2731N-linked (GlcNAc...)1 Publication
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ15904.
PaxDbiQ15904.
PRIDEiQ15904.

PTM databases

PhosphoSiteiQ15904.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ15904.
CleanExiHS_ATP6AP1.
ExpressionAtlasiQ15904. baseline and differential.
GenevestigatoriQ15904.

Organism-specific databases

HPAiCAB015218.

Interactioni

Subunit structurei

Composed of at least 10 subunits.

Protein-protein interaction databases

BioGridi107019. 14 interactions.
IntActiQ15904. 5 interactions.
MINTiMINT-4722342.
STRINGi9606.ENSP00000358777.

Structurei

3D structure databases

ProteinModelPortaliQ15904.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the vacuolar ATPase subunit S1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG322101.
GeneTreeiENSGT00530000063584.
HOGENOMiHOG000000706.
HOVERGENiHBG001090.
InParanoidiQ15904.
KOiK03662.
OMAiGHITSDM.
PhylomeDBiQ15904.
TreeFamiTF325819.

Family and domain databases

InterProiIPR008388. ATPase_V1-cplx_s1su.
IPR024722. BIG/ATPase_V1_suS1.
[Graphical view]
PANTHERiPTHR12471. PTHR12471. 1 hit.
PfamiPF05827. ATP-synt_S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q15904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAAMATARV RMGPRCAQAL WRMPWLPVFL SLAAAAAAAA AEQQVPLVLW
60 70 80 90 100
SSDRDLWAPA ADTHEGHITS DLQLSTYLDP ALELGPRNVL LFLQDKLSIE
110 120 130 140 150
DFTAYGGVFG NKQDSAFSNL ENALDLAPSS LVLPAVDWYA VSTLTTYLQE
160 170 180 190 200
KLGASPLHVD LATLRELKLN ASLPALLLIR LPYTASSGLM APREVLTGND
210 220 230 240 250
EVIGQVLSTL KSEDVPYTAA LTAVRPSRVA RDVAVVAGGL GRQLLQKQPV
260 270 280 290 300
SPVIHPPVSY NDTAPRILFW AQNFSVAYKD QWEDLTPLTF GVQELNLTGS
310 320 330 340 350
FWNDSFARLS LTYERLFGTT VTFKFILANR LYPVSARHWF TMERLEVHSN
360 370 380 390 400
GSVAYFNASQ VTGPSIYSFH CEYVSSLSKK GSLLVARTQP SPWQMMLQDF
410 420 430 440 450
QIQAFNVMGE QFSYASDCAS FFSPGIWMGL LTSLFMLFIF TYGLHMILSL
460 470
KTMDRFDDHK GPTISLTQIV
Length:470
Mass (Da):52,026
Last modified:January 11, 2001 - v2
Checksum:iA71C7EF0E90D0652
GO

Sequence cautioni

The sequence BAA03938.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB66785.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681I → V in BAC11520 (PubMed:16303743).Curated
Sequence conflicti74 – 741L → P in BAC11520 (PubMed:16303743).Curated
Sequence conflicti229 – 2291V → A in AK026519 (PubMed:14702039).Curated
Sequence conflicti307 – 3071A → T in AK026519 (PubMed:14702039).Curated
Sequence conflicti335 – 3351S → F in AK026519 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L44140 Genomic DNA. No translation available.
AL136851 mRNA. Translation: CAB66785.1. Different initiation.
AK026519 mRNA. No translation available.
AK289452 mRNA. Translation: BAF82141.1.
AK075284 mRNA. Translation: BAC11520.1.
BX936347, BX936385 Genomic DNA. Translation: CAI43213.3.
BX936385, BX936347 Genomic DNA. Translation: CAI95782.2.
CH471172 Genomic DNA. Translation: EAW72715.1.
BC000724 mRNA. Translation: AAH00724.1.
D16469 mRNA. Translation: BAA03938.1. Different initiation.
CCDSiCCDS35451.1.
RefSeqiNP_001174.2. NM_001183.5.
UniGeneiHs.633817.
Hs.6551.

Genome annotation databases

EnsembliENST00000369762; ENSP00000358777; ENSG00000071553.
GeneIDi537.
KEGGihsa:537.
UCSCiuc004flf.1. human.

Polymorphism databases

DMDMi12230759.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L44140 Genomic DNA. No translation available.
AL136851 mRNA. Translation: CAB66785.1. Different initiation.
AK026519 mRNA. No translation available.
AK289452 mRNA. Translation: BAF82141.1.
AK075284 mRNA. Translation: BAC11520.1.
BX936347, BX936385 Genomic DNA. Translation: CAI43213.3.
BX936385, BX936347 Genomic DNA. Translation: CAI95782.2.
CH471172 Genomic DNA. Translation: EAW72715.1.
BC000724 mRNA. Translation: AAH00724.1.
D16469 mRNA. Translation: BAA03938.1. Different initiation.
CCDSiCCDS35451.1.
RefSeqiNP_001174.2. NM_001183.5.
UniGeneiHs.633817.
Hs.6551.

3D structure databases

ProteinModelPortaliQ15904.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107019. 14 interactions.
IntActiQ15904. 5 interactions.
MINTiMINT-4722342.
STRINGi9606.ENSP00000358777.

Chemistry

BindingDBiQ15904.
ChEMBLiCHEMBL4790.

PTM databases

PhosphoSiteiQ15904.

Polymorphism databases

DMDMi12230759.

Proteomic databases

MaxQBiQ15904.
PaxDbiQ15904.
PRIDEiQ15904.

Protocols and materials databases

DNASUi537.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369762; ENSP00000358777; ENSG00000071553.
GeneIDi537.
KEGGihsa:537.
UCSCiuc004flf.1. human.

Organism-specific databases

CTDi537.
GeneCardsiGC0XP153657.
HGNCiHGNC:868. ATP6AP1.
HPAiCAB015218.
MIMi300197. gene.
neXtProtiNX_Q15904.
PharmGKBiPA25145.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG322101.
GeneTreeiENSGT00530000063584.
HOGENOMiHOG000000706.
HOVERGENiHBG001090.
InParanoidiQ15904.
KOiK03662.
OMAiGHITSDM.
PhylomeDBiQ15904.
TreeFamiTF325819.

Enzyme and pathway databases

BioCyciMetaCyc:HS01034-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSiATP6AP1. human.
GeneWikiiATP6AP1.
GenomeRNAii537.
NextBioi2227.
PROiQ15904.
SOURCEiSearch...

Gene expression databases

BgeeiQ15904.
CleanExiHS_ATP6AP1.
ExpressionAtlasiQ15904. baseline and differential.
GenevestigatoriQ15904.

Family and domain databases

InterProiIPR008388. ATPase_V1-cplx_s1su.
IPR024722. BIG/ATPase_V1_suS1.
[Graphical view]
PANTHERiPTHR12471. PTHR12471. 1 hit.
PfamiPF05827. ATP-synt_S1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
    Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
    Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  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].
  4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Kidney.
  8. "Isolation of expressed sequences encoded by the human Xq terminal portion using microclone probes generated by laser microdissection."
    Yokoi H., Hadano S., Kogi M., Kang X., Wakasa K., Ikeda J.
    Genomics 20:404-411(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-470.
    Tissue: Brain.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-273.
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVAS1_HUMAN
AccessioniPrimary (citable) accession number: Q15904
Secondary accession number(s): A6ZKI4, Q8NBT4, Q9H0C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: March 4, 2015
This is version 147 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. 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.