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Protein

Wiskott-Aldrich syndrome protein family member 2

Gene

WASF2

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

Functioni

Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex.2 Publications

GO - Molecular functioni

  • actin binding Source: ProtInc
  • protein complex binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiQ9Y6W5.

Names & Taxonomyi

Protein namesi
Recommended name:
Wiskott-Aldrich syndrome protein family member 2
Short name:
WASP family protein member 2
Alternative name(s):
Protein WAVE-2
Verprolin homology domain-containing protein 2
Gene namesi
Name:WASF2
Synonyms:WAVE2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:12733. WASF2.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • cell-cell junction Source: Ensembl
  • cytosol Source: Reactome
  • early endosome Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • intracellular Source: MGI
  • lamellipodium Source: MGI
  • ruffle Source: Ensembl
  • SCAR complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401L → D: Decreased interaction with WAVE complex; when associated with D-51. 1 Publication
Mutagenesisi50 – 501I → D: Decreased interaction with WAVE complex; when associated with D-54. 1 Publication
Mutagenesisi51 – 511F → D: Decreased interaction with WAVE complex; when associated with D-40. 1 Publication
Mutagenesisi54 – 541L → D: Decreased interaction with WAVE complex; when associated with D-50. 1 Publication
Mutagenesisi124 – 1241Y → D: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia. 1 Publication
Mutagenesisi150 – 1501Y → D: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia. 1 Publication
Mutagenesisi160 – 1612WK → ED: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia. 1 Publication

Organism-specific databases

PharmGKBiPA37344.

Polymorphism and mutation databases

BioMutaiWASF2.
DMDMi59800456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Wiskott-Aldrich syndrome protein family member 2PRO_0000188994Add
BLAST

Proteomic databases

MaxQBiQ9Y6W5.
PaxDbiQ9Y6W5.
PeptideAtlasiQ9Y6W5.
PRIDEiQ9Y6W5.

PTM databases

PhosphoSiteiQ9Y6W5.

Miscellaneous databases

PMAP-CutDBQ9Y6W5.

Expressioni

Tissue specificityi

Expressed in all tissues with strongest expression in placenta, lung, and peripheral blood leukocytes, but not in skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9Y6W5.
CleanExiHS_WASF2.
GenevisibleiQ9Y6W5. HS.

Organism-specific databases

HPAiCAB022632.
HPA045288.

Interactioni

Subunit structurei

Binds actin and the Arp2/3 complex. Interacts with BAIAP2. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Directly interacts with BRK1. Interacts with human cytomegalovirus protein UL135.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BAIAP2Q9UQB8-45EBI-4290615,EBI-6174091
SORBS3O60504-23EBI-4290615,EBI-1222956
ZDHHC17Q8IUH52EBI-4290615,EBI-524753

Protein-protein interaction databases

BioGridi115465. 21 interactions.
DIPiDIP-41817N.
IntActiQ9Y6W5. 8 interactions.
MINTiMINT-5005787.
STRINGi9606.ENSP00000396211.

Structurei

Secondary structure

1
498
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi436 – 44611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A40X-ray1.80C/F433-464[»]
ProteinModelPortaliQ9Y6W5.
SMRiQ9Y6W5. Positions 21-197, 435-482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6W5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini436 – 45318WH2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi268 – 2714Poly-Pro
Compositional biasi318 – 32811Poly-ProAdd
BLAST
Compositional biasi333 – 3386Poly-Pro
Compositional biasi347 – 3504Poly-Pro
Compositional biasi364 – 3718Poly-Pro
Compositional biasi379 – 3824Poly-Pro
Compositional biasi391 – 40616Poly-ProAdd
BLAST

Domaini

Binds and activates the Arp2/3 complex via the C-terminal domain. Interacts with actin via the WH2 domain.2 Publications

Sequence similaritiesi

Belongs to the SCAR/WAVE family.Curated
Contains 1 WH2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG299696.
GeneTreeiENSGT00730000110593.
HOGENOMiHOG000021456.
HOVERGENiHBG058482.
InParanoidiQ9Y6W5.
KOiK05748.
OMAiMIGIPSP.
OrthoDBiEOG7VHSXK.
PhylomeDBiQ9Y6W5.
TreeFamiTF315031.

Family and domain databases

InterProiIPR028288. SCAR/WAVE_fam.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR12902. PTHR12902. 1 hit.
PfamiPF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00246. WH2. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 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: Q9Y6W5-1) [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
MPLVTRNIEP RHLCRQTLPS VRSELECVTN ITLANVIRQL GSLSKYAEDI
60 70 80 90 100
FGELFTQANT FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF
110 120 130 140 150
RSSTIQDQKL FDRNSLPVPV LETYNTCDTP PPLNNLTPYR DDGKEALKFY
160 170 180 190 200
TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK EKKDNPNRGN VNPRKIKTRK
210 220 230 240 250
EEWEKMKMGQ EFVESKEKLG TSGYPPTLVY QNGSIGCVEN VDASSYPPPP
260 270 280 290 300
QSDSASSPSP SFSEDNLPPP PAEFSYPVDN QRGSGLAGPK RSSVVSPSHP
310 320 330 340 350
PPAPPLGSPP GPKPGFAPPP APPPPPPPMI GIPPPPPPVG FGSPGTPPPP
360 370 380 390 400
SPPSFPPHPD FAAPPPPPPP PAADYPTLPP PPLSQPTGGA PPPPPPPPPP
410 420 430 440 450
GPPPPPFTGA DGQPAIPPPL SDTTKPKSSL PAVSDARSDL LSAIRQGFQL
460 470 480 490
RRVEEQREQE KRDVVGNDVA TILSRRIAVE YSDSEDDSSE FDEDDWSD
Length:498
Mass (Da):54,284
Last modified:February 1, 2005 - v3
Checksum:iC737CE963016DE94
GO
Isoform 2 (identifier: Q9Y6W5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     275-281: SYPVDNQ → RFSAAQG
     282-498: Missing.

Note: No experimental confirmation available.
Show »
Length:281
Mass (Da):31,979
Checksum:iC5E79110854FAF56
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei275 – 2817SYPVDNQ → RFSAAQG in isoform 2. 1 PublicationVSP_042514
Alternative sequencei282 – 498217Missing in isoform 2. 1 PublicationVSP_042515Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026542 mRNA. Translation: BAA81795.1.
AK303011 mRNA. Translation: BAG64142.1.
AL096774 Genomic DNA. Translation: CAC18518.1.
AL663122 Genomic DNA. No translation available.
BX293535 Genomic DNA. No translation available.
BC040943 mRNA. Translation: AAH40943.1.
CCDSiCCDS304.1. [Q9Y6W5-1]
CCDS55582.1. [Q9Y6W5-2]
RefSeqiNP_001188333.1. NM_001201404.2. [Q9Y6W5-2]
NP_008921.1. NM_006990.4. [Q9Y6W5-1]
UniGeneiHs.469244.
Hs.512079.

Genome annotation databases

EnsembliENST00000536657; ENSP00000439883; ENSG00000158195. [Q9Y6W5-2]
ENST00000618852; ENSP00000483313; ENSG00000158195.
GeneIDi10163.
KEGGihsa:10163.
UCSCiuc001bof.2. human. [Q9Y6W5-1]
uc010ofl.2. human. [Q9Y6W5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026542 mRNA. Translation: BAA81795.1.
AK303011 mRNA. Translation: BAG64142.1.
AL096774 Genomic DNA. Translation: CAC18518.1.
AL663122 Genomic DNA. No translation available.
BX293535 Genomic DNA. No translation available.
BC040943 mRNA. Translation: AAH40943.1.
CCDSiCCDS304.1. [Q9Y6W5-1]
CCDS55582.1. [Q9Y6W5-2]
RefSeqiNP_001188333.1. NM_001201404.2. [Q9Y6W5-2]
NP_008921.1. NM_006990.4. [Q9Y6W5-1]
UniGeneiHs.469244.
Hs.512079.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A40X-ray1.80C/F433-464[»]
ProteinModelPortaliQ9Y6W5.
SMRiQ9Y6W5. Positions 21-197, 435-482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115465. 21 interactions.
DIPiDIP-41817N.
IntActiQ9Y6W5. 8 interactions.
MINTiMINT-5005787.
STRINGi9606.ENSP00000396211.

PTM databases

PhosphoSiteiQ9Y6W5.

Polymorphism and mutation databases

BioMutaiWASF2.
DMDMi59800456.

Proteomic databases

MaxQBiQ9Y6W5.
PaxDbiQ9Y6W5.
PeptideAtlasiQ9Y6W5.
PRIDEiQ9Y6W5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000536657; ENSP00000439883; ENSG00000158195. [Q9Y6W5-2]
ENST00000618852; ENSP00000483313; ENSG00000158195.
GeneIDi10163.
KEGGihsa:10163.
UCSCiuc001bof.2. human. [Q9Y6W5-1]
uc010ofl.2. human. [Q9Y6W5-2]

Organism-specific databases

CTDi10163.
GeneCardsiGC01M027730.
HGNCiHGNC:12733. WASF2.
HPAiCAB022632.
HPA045288.
MIMi605875. gene.
neXtProtiNX_Q9Y6W5.
PharmGKBiPA37344.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299696.
GeneTreeiENSGT00730000110593.
HOGENOMiHOG000021456.
HOVERGENiHBG058482.
InParanoidiQ9Y6W5.
KOiK05748.
OMAiMIGIPSP.
OrthoDBiEOG7VHSXK.
PhylomeDBiQ9Y6W5.
TreeFamiTF315031.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiQ9Y6W5.

Miscellaneous databases

ChiTaRSiWASF2. human.
EvolutionaryTraceiQ9Y6W5.
GeneWikiiWASF2.
GenomeRNAii10163.
NextBioi38478.
PMAP-CutDBQ9Y6W5.
PROiQ9Y6W5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6W5.
CleanExiHS_WASF2.
GenevisibleiQ9Y6W5. HS.

Family and domain databases

InterProiIPR028288. SCAR/WAVE_fam.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR12902. PTHR12902. 1 hit.
PfamiPF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00246. WH2. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex."
    Suetsugu S., Miki H., Takenawa T.
    Biochem. Biophys. Res. Commun. 260:296-302(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN AND THE ARP2/3 COMPLEX, SUBUNIT, DOMAIN, TISSUE SPECIFICITY.
    Tissue: T-cell lymphoma.
  2. "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] (ISOFORM 2).
    Tissue: Testis.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Lymph.
  5. "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling."
    Miki H., Yamaguchi H., Suetsugu S., Takenawa T.
    Nature 408:732-735(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAIAP2.
  6. Cited for: INTERACTION WITH C3ORF10.
  7. Cited for: MUTAGENESIS OF LEU-40; ILE-50; PHE-51 AND LEU-54, SUBUNIT.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135.
  10. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly."
    Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R.
    Proc. Natl. Acad. Sci. U.S.A. 102:16644-16649(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 433-464 IN COMPLEX WITH ACTIN, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-124; TYR-150 AND 160-TRP-LYS-161, SUBUNIT.

Entry informationi

Entry nameiWASF2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6W5
Secondary accession number(s): B4DZN0, O60794, Q9UDY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 2005
Last modified: July 22, 2015
This is version 140 of the entry and version 3 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 1
    Human chromosome 1: 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.