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Protein

Amphiphysin

Gene

AMPH

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

Functioni

May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.

GO - Molecular functioni

  • phospholipid binding Source: FlyBase

GO - Biological processi

  • endocytosis Source: ProtInc
  • learning Source: Ensembl
  • synaptic transmission Source: ProtInc
  • synaptic vesicle endocytosis Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Amphiphysin
Gene namesi
Name:AMPH
Synonyms:AMPH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:471. AMPH.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • cell junction Source: UniProtKB-KW
  • leading edge membrane Source: FlyBase
  • synaptic vesicle Source: ProtInc
  • synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24779.

Polymorphism and mutation databases

BioMutaiAMPH.
DMDMi1351924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 695695AmphiphysinPRO_0000192947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei506 – 5061PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49418.
PaxDbiP49418.
PRIDEiP49418.

PTM databases

PhosphoSiteiP49418.

Miscellaneous databases

PMAP-CutDBP49418.

Expressioni

Tissue specificityi

Neurons, certain endocrine cell types and spermatocytes.

Gene expression databases

BgeeiP49418.
CleanExiHS_AMPH.
ExpressionAtlasiP49418. baseline and differential.
GenevisibleiP49418. HS.

Organism-specific databases

HPAiCAB008559.
HPA019828.
HPA019829.

Interactioni

Subunit structurei

Heterodimer with BIN1. Binds SH3GLB1 and AP2A2 (By similarity). Interacts with AP2B1. Interacts with REPS1 and SGIP1; may be involved in clathrin-mediated endocytosis.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARL16Q0P5N63EBI-7121510,EBI-10186132
CCDC67Q05D603EBI-7121510,EBI-748597
CltaP080813EBI-7121510,EBI-916140From a different organism.
Necap1P696823EBI-7121510,EBI-7592718From a different organism.
Necap1Q9CR956EBI-7121510,EBI-7592476From a different organism.
PPP3CCP484543EBI-7121510,EBI-2827192
Tfap2aP581972EBI-7121510,EBI-7069641From a different organism.

Protein-protein interaction databases

BioGridi106770. 44 interactions.
DIPiDIP-40729N.
IntActiP49418. 11 interactions.
MINTiMINT-109264.
STRINGi9606.ENSP00000348602.

Structurei

Secondary structure

1
695
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 223Combined sources
Helixi24 – 8461Combined sources
Helixi92 – 11524Combined sources
Helixi117 – 12610Combined sources
Helixi128 – 15629Combined sources
Helixi163 – 19634Combined sources
Helixi198 – 23740Combined sources
Helixi382 – 3843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KY7X-ray2.15P322-330[»]
1UTCX-ray2.30P/Q379-387[»]
3SOGX-ray2.30A34-236[»]
4ATMX-ray1.78A1-242[»]
ProteinModelPortaliP49418.
SMRiP49418. Positions 19-239, 618-694.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49418.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 240217BARPROSITE-ProRule annotationAdd
BLAST
Domaini622 – 69574SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili10 – 8374Sequence AnalysisAdd
BLAST
Coiled coili144 – 19148Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 BAR domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG264615.
GeneTreeiENSGT00390000017588.
HOVERGENiHBG004224.
InParanoidiP49418.
KOiK12562.
OMAiMICNLAE.
OrthoDBiEOG7XWPND.
PhylomeDBiP49418.
TreeFamiTF313542.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003017. Amphiphysin_1.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR01251. AMPHIPHYSIN.
PR01252. AMPHIPHYSIN1.
PR00452. SH3DOMAIN.
SMARTiSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50002. SH3. 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: P49418-1) [UniParc]FASTAAdd to basket

Also known as: 128 kDa

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
MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE
60 70 80 90 100
AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE
110 120 130 140 150
KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH
160 170 180 190 200
HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG
210 220 230 240 250
FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFTIQGAPS
260 270 280 290 300
DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG
310 320 330 340 350
PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET
360 370 380 390 400
LLDLDFDPFK PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF
410 420 430 440 450
NGFTQPQDTS LFTMQTDQSM ICNLAESEQA PPTEPKAEEP LAAVTPAVGL
460 470 480 490 500
DLGMDTRAEE PVEEAVIIPG ADADAAVGTL VSAAEGAPGE EAEAEKATVP
510 520 530 540 550
AGEGVSLEEA KIGTETTEGA ESAQPEAEEL EATVPQEKVI PSVVIEPASN
560 570 580 590 600
HEEEGENEIT IGAEPKETTE DAAPPGPTSE TPELATEQKP IQDPQPTPSA
610 620 630 640 650
PAMGAADQLA SAREASQELP PGFLYKVETL HDFEAANSDE LTLQRGDVVL
660 670 680 690
VVPSDSEADQ DAGWLVGVKE SDWLQYRDLA TYKGLFPENF TRRLD
Length:695
Mass (Da):76,257
Last modified:February 1, 1996 - v1
Checksum:i78B4F75AB75BA357
GO
Isoform 2 (identifier: P49418-2) [UniParc]FASTAAdd to basket

Also known as: 108 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     425-466: Missing.

Show »
Length:653
Mass (Da):71,929
Checksum:i44C1115E3E70B6A9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti218 – 2181K → E.
Corresponds to variant rs35166354 [ dbSNP | Ensembl ].
VAR_053004
Natural varianti376 – 3761M → I.
Corresponds to variant rs17171345 [ dbSNP | Ensembl ].
VAR_053005
Natural varianti496 – 4961K → T.1 Publication
Corresponds to variant rs35024632 [ dbSNP | Ensembl ].
VAR_053006

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei425 – 46642Missing in isoform 2. 1 PublicationVSP_000245Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07616 mRNA. Translation: AAA21865.1.
X81438 mRNA. Translation: CAA57197.1.
AF034996 mRNA. Translation: AAC02977.1.
AC011309 Genomic DNA. Translation: AAS07391.1.
AC012490 Genomic DNA. Translation: AAS07563.1.
AC007245 Genomic DNA. Translation: AAS07541.1.
CH236951 Genomic DNA. Translation: EAL23989.1.
CH236951 Genomic DNA. Translation: EAL23990.1.
CH471073 Genomic DNA. Translation: EAW94110.1.
CH471073 Genomic DNA. Translation: EAW94111.1.
BC034376 mRNA. Translation: AAH34376.1.
CCDSiCCDS47574.1. [P49418-2]
CCDS5456.1. [P49418-1]
PIRiS62400.
RefSeqiNP_001626.1. NM_001635.3. [P49418-1]
NP_647477.1. NM_139316.2. [P49418-2]
UniGeneiHs.592182.

Genome annotation databases

EnsembliENST00000325590; ENSP00000317441; ENSG00000078053. [P49418-2]
ENST00000356264; ENSP00000348602; ENSG00000078053. [P49418-1]
GeneIDi273.
KEGGihsa:273.
UCSCiuc003tgu.3. human. [P49418-1]
uc003tgv.3. human. [P49418-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07616 mRNA. Translation: AAA21865.1.
X81438 mRNA. Translation: CAA57197.1.
AF034996 mRNA. Translation: AAC02977.1.
AC011309 Genomic DNA. Translation: AAS07391.1.
AC012490 Genomic DNA. Translation: AAS07563.1.
AC007245 Genomic DNA. Translation: AAS07541.1.
CH236951 Genomic DNA. Translation: EAL23989.1.
CH236951 Genomic DNA. Translation: EAL23990.1.
CH471073 Genomic DNA. Translation: EAW94110.1.
CH471073 Genomic DNA. Translation: EAW94111.1.
BC034376 mRNA. Translation: AAH34376.1.
CCDSiCCDS47574.1. [P49418-2]
CCDS5456.1. [P49418-1]
PIRiS62400.
RefSeqiNP_001626.1. NM_001635.3. [P49418-1]
NP_647477.1. NM_139316.2. [P49418-2]
UniGeneiHs.592182.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KY7X-ray2.15P322-330[»]
1UTCX-ray2.30P/Q379-387[»]
3SOGX-ray2.30A34-236[»]
4ATMX-ray1.78A1-242[»]
ProteinModelPortaliP49418.
SMRiP49418. Positions 19-239, 618-694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106770. 44 interactions.
DIPiDIP-40729N.
IntActiP49418. 11 interactions.
MINTiMINT-109264.
STRINGi9606.ENSP00000348602.

PTM databases

PhosphoSiteiP49418.

Polymorphism and mutation databases

BioMutaiAMPH.
DMDMi1351924.

Proteomic databases

MaxQBiP49418.
PaxDbiP49418.
PRIDEiP49418.

Protocols and materials databases

DNASUi273.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325590; ENSP00000317441; ENSG00000078053. [P49418-2]
ENST00000356264; ENSP00000348602; ENSG00000078053. [P49418-1]
GeneIDi273.
KEGGihsa:273.
UCSCiuc003tgu.3. human. [P49418-1]
uc003tgv.3. human. [P49418-2]

Organism-specific databases

CTDi273.
GeneCardsiGC07M038423.
HGNCiHGNC:471. AMPH.
HPAiCAB008559.
HPA019828.
HPA019829.
MIMi600418. gene.
neXtProtiNX_P49418.
PharmGKBiPA24779.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264615.
GeneTreeiENSGT00390000017588.
HOVERGENiHBG004224.
InParanoidiP49418.
KOiK12562.
OMAiMICNLAE.
OrthoDBiEOG7XWPND.
PhylomeDBiP49418.
TreeFamiTF313542.

Miscellaneous databases

ChiTaRSiAMPH. human.
EvolutionaryTraceiP49418.
GeneWikiiAmphiphysin.
GenomeRNAii273.
NextBioi1081.
PMAP-CutDBP49418.
PROiP49418.
SOURCEiSearch...

Gene expression databases

BgeeiP49418.
CleanExiHS_AMPH.
ExpressionAtlasiP49418. baseline and differential.
GenevisibleiP49418. HS.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003017. Amphiphysin_1.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR01251. AMPHIPHYSIN.
PR01252. AMPHIPHYSIN1.
PR00452. SH3DOMAIN.
SMARTiSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Autoimmunity in stiff-man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161."
    David C., Solimena M., de Camilli P.
    FEBS Lett. 351:73-79(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cerebellum.
  2. "Primary structure of human amphiphysin, the dominant autoantigen of paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to chromosome 7p13-p14."
    Yamamoto R., Li X., Winter S., Francke U., Kilimann M.W.
    Hum. Mol. Genet. 4:265-268(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Expression of amphiphysin I, an autoantigen of paraneoplastic neurological syndromes, in breast cancer."
    Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.
    Mol. Med. 4:29-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Mammary gland.
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    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], VARIANT THR-496.
    Tissue: Brain.
  8. "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
    Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
    PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2B1.
  9. "Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits."
    Dergai O., Novokhatska O., Dergai M., Skrypkina I., Tsyba L., Moreau J., Rynditch A.
    Biochem. Biophys. Res. Commun. 402:408-413(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REPS1 AND SGIP1.
  10. "Accessory protein recruitment motifs in clathrin-mediated endocytosis."
    Brett T.J., Traub L.M., Fremont D.H.
    Structure 10:797-809(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 322-330 IN COMPLEX WITH AP2A2.

Entry informationi

Entry nameiAMPH_HUMAN
AccessioniPrimary (citable) accession number: P49418
Secondary accession number(s): A4D1X8
, A4D1X9, O43538, Q75MJ8, Q75MK5, Q75MM3, Q8N4G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 148 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

Miscellaneous

Antibodies against AMPH are detected in patients with stiff-man syndrome, a rare disease of the central nervous system characterized by progressive rigidity of the body musculature with superimposed painful spasms.

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. 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.