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Protein

Neural Wiskott-Aldrich syndrome protein

Gene

WASL

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

Functioni

Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in mitosis and cytokinesis, via its role in the regulation of actin polymerization. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression.4 Publications

GO - Molecular functioni

  • GTPase regulator activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_12541. NOSTRIN mediated eNOS trafficking.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_22351. DCC mediated attractive signaling.
REACT_23832. Nephrin interactions.
REACT_263952. EPHB-mediated forward signaling.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiO00401.

Names & Taxonomyi

Protein namesi
Recommended name:
Neural Wiskott-Aldrich syndrome protein
Short name:
N-WASP
Gene namesi
Name:WASL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:12735. WASL.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Nucleus By similarity

  • Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated.By similarity

GO - Cellular componenti

  • actin cap Source: Ensembl
  • actin cytoskeleton Source: ProtInc
  • cytoplasmic membrane-bounded vesicle Source: BHF-UCL
  • cytosol Source: UniProtKB
  • endocytic vesicle membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • lamellipodium Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37346.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 505504Neural Wiskott-Aldrich syndrome proteinPRO_0000189000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei242 – 2421Phosphoserine; by TNK21 Publication
Modified residuei256 – 2561Phosphotyrosine; by FAK1 and TNK22 Publications
Modified residuei484 – 4841Phosphoserine2 Publications
Modified residuei485 – 4851Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO00401.
PaxDbiO00401.
PRIDEiO00401.

PTM databases

PhosphoSiteiO00401.

Expressioni

Gene expression databases

BgeeiO00401.
CleanExiHS_WASL.
GenevisibleiO00401. HS.

Organism-specific databases

HPAiCAB005399.
HPA005750.

Interactioni

Subunit structurei

Binds actin and the Arp2/3 complex. Interacts with CDC42. Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts with SNX9. Interacts with the WW domains of PRPF40A/FBP11. Interacts with PTK2/FAK1. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with NOSTRIN. Interacts with Shigella flexneri protein IcsA. The interaction with IcsA enhances the affinity of WASL for Arp2/3, thus assembling a tight complex which has maximal activity in actin assembly. Interacts with E.coli effector protein EspF(U). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Binds to TNK2. Interacts with SNX33.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTR3P611573EBI-957615,EBI-351419From a different organism.
ARPC3O151453EBI-957615,EBI-351829
CDC42P609533EBI-957615,EBI-81752
CIB1Q998287EBI-957615,EBI-372594
Fnbp1Q8R5112EBI-957615,EBI-1111424From a different organism.
GRB2P629936EBI-957615,EBI-401755
NCK2O436393EBI-957615,EBI-713635
PTK6Q138823EBI-957615,EBI-1383632
RHOJQ9H4E53EBI-957615,EBI-6285694
RNF8O760644EBI-957615,EBI-373337
SDCBPO005603EBI-957615,EBI-727004
SNX9Q9Y5X12EBI-957615,EBI-77848
SORBS3O60504-23EBI-957615,EBI-1222956
WIPF1O435167EBI-957615,EBI-346356

Protein-protein interaction databases

BioGridi114466. 58 interactions.
DIPiDIP-29042N.
IntActiO00401. 41 interactions.
MINTiMINT-157215.
STRINGi9606.ENSP00000223023.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni219 – 2213Combined sources
Helixi225 – 2273Combined sources
Helixi232 – 2398Combined sources
Helixi243 – 2464Combined sources
Turni249 – 2513Combined sources
Helixi252 – 26211Combined sources
Helixi265 – 2695Combined sources
Helixi435 – 4439Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FF3X-ray2.00C451-465[»]
2LNHNMR-A207-270[»]
2VCPX-ray3.20D/E392-484[»]
4CC2X-ray1.55B/D346-357[»]
4CC7X-ray1.97B/D/F/H/J/L/N346-357[»]
ProteinModelPortaliO00401.
SMRiO00401. Positions 29-150, 207-270, 403-450, 466-491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00401.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 141108WH1PROSITE-ProRule annotationAdd
BLAST
Domaini203 – 21614CRIBPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 42218WH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini433 – 45018WH2 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi277 – 392116Pro-richAdd
BLAST
Compositional biasi485 – 50521Asp-richAdd
BLAST

Sequence similaritiesi

Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 WH1 domain.PROSITE-ProRule annotation
Contains 2 WH2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270974.
GeneTreeiENSGT00730000110895.
HOGENOMiHOG000143378.
HOVERGENiHBG000222.
InParanoidiO00401.
KOiK05747.
OMAiDAPNGPN.
OrthoDBiEOG7FJH20.
PhylomeDBiO00401.
TreeFamiTF316736.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR030214. N-WASP.
IPR011993. PH_like_dom.
IPR011026. WASP_C.
IPR000697. WH1/EVH1_dom.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR12779:SF3. PTHR12779:SF3. 1 hit.
PfamiPF00786. PBD. 1 hit.
PF00568. WH1. 1 hit.
PF02205. WH2. 2 hits.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00461. WH1. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]
SUPFAMiSSF47912. SSF47912. 2 hits.
PROSITEiPS50108. CRIB. 1 hit.
PS50229. WH1. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O00401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVQQQPPP PRRVTNVGSL LLTPQENESL FTFLGKKCVT MSSAVVQLYA
60 70 80 90 100
ADRNCMWSKK CSGVACLVKD NPQRSYFLRI FDIKDGKLLW EQELYNNFVY
110 120 130 140 150
NSPRGYFHTF AGDTCQVALN FANEEEAKKF RKAVTDLLGR RQRKSEKRRD
160 170 180 190 200
PPNGPNLPMA TVDIKNPEIT TNRFYGPQVN NISHTKEKKK GKAKKKRLTK
210 220 230 240 250
ADIGTPSNFQ HIGHVGWDPN TGFDLNNLDP ELKNLFDMCG ISEAQLKDRE
260 270 280 290 300
TSKVIYDFIE KTGGVEAVKN ELRRQAPPPP PPSRGGPPPP PPPPHNSGPP
310 320 330 340 350
PPPARGRGAP PPPPSRAPTA APPPPPPSRP SVAVPPPPPN RMYPPPPPAL
360 370 380 390 400
PSSAPSGPPP PPPSVLGVGP VAPPPPPPPP PPPGPPPPPG LPSDGDHQVP
410 420 430 440 450
TTAGNKAALL DQIREGAQLK KVEQNSRPVS CSGRDALLDQ IRQGIQLKSV
460 470 480 490 500
ADGQESTPPT PAPTSGIVGA LMEVMQKRSK AIHSSDEDED EDDEEDFEDD

DEWED
Length:505
Mass (Da):54,827
Last modified:February 1, 2005 - v2
Checksum:iB5895C6055E23049
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761Y → H in BAA20128 (PubMed:9322739).Curated
Sequence conflicti201 – 2011A → G in BAA20128 (PubMed:9322739).Curated
Sequence conflicti223 – 2231F → S in BAA20128 (PubMed:9322739).Curated
Sequence conflicti242 – 2421S → L in BAA20128 (PubMed:9322739).Curated
Sequence conflicti248 – 2481D → E in BAA20128 (PubMed:9322739).Curated
Sequence conflicti252 – 2521S → L in BAA20128 (PubMed:9322739).Curated
Sequence conflicti296 – 2961N → S in BAA20128 (PubMed:9322739).Curated
Sequence conflicti333 – 3331A → E in BAA20128 (PubMed:9322739).Curated
Sequence conflicti351 – 3511P → L in CAL26602 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88460 mRNA. Translation: BAA20128.1.
AM295156 mRNA. Translation: CAL26602.1.
AC006333 Genomic DNA. Translation: AAQ96857.1.
BC052955 mRNA. Translation: AAH52955.1.
CCDSiCCDS34743.1.
RefSeqiNP_003932.3. NM_003941.3.
UniGeneiHs.143728.
Hs.731519.
Hs.83916.

Genome annotation databases

EnsembliENST00000223023; ENSP00000223023; ENSG00000106299.
GeneIDi8976.
KEGGihsa:8976.
UCSCiuc003vkz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88460 mRNA. Translation: BAA20128.1.
AM295156 mRNA. Translation: CAL26602.1.
AC006333 Genomic DNA. Translation: AAQ96857.1.
BC052955 mRNA. Translation: AAH52955.1.
CCDSiCCDS34743.1.
RefSeqiNP_003932.3. NM_003941.3.
UniGeneiHs.143728.
Hs.731519.
Hs.83916.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FF3X-ray2.00C451-465[»]
2LNHNMR-A207-270[»]
2VCPX-ray3.20D/E392-484[»]
4CC2X-ray1.55B/D346-357[»]
4CC7X-ray1.97B/D/F/H/J/L/N346-357[»]
ProteinModelPortaliO00401.
SMRiO00401. Positions 29-150, 207-270, 403-450, 466-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114466. 58 interactions.
DIPiDIP-29042N.
IntActiO00401. 41 interactions.
MINTiMINT-157215.
STRINGi9606.ENSP00000223023.

PTM databases

PhosphoSiteiO00401.

Proteomic databases

MaxQBiO00401.
PaxDbiO00401.
PRIDEiO00401.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223023; ENSP00000223023; ENSG00000106299.
GeneIDi8976.
KEGGihsa:8976.
UCSCiuc003vkz.3. human.

Organism-specific databases

CTDi8976.
GeneCardsiGC07M123321.
HGNCiHGNC:12735. WASL.
HPAiCAB005399.
HPA005750.
MIMi605056. gene.
neXtProtiNX_O00401.
PharmGKBiPA37346.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG270974.
GeneTreeiENSGT00730000110895.
HOGENOMiHOG000143378.
HOVERGENiHBG000222.
InParanoidiO00401.
KOiK05747.
OMAiDAPNGPN.
OrthoDBiEOG7FJH20.
PhylomeDBiO00401.
TreeFamiTF316736.

Enzyme and pathway databases

ReactomeiREACT_12541. NOSTRIN mediated eNOS trafficking.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_22351. DCC mediated attractive signaling.
REACT_23832. Nephrin interactions.
REACT_263952. EPHB-mediated forward signaling.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiO00401.

Miscellaneous databases

ChiTaRSiWASL. human.
EvolutionaryTraceiO00401.
GeneWikiiWASL_(gene).
GenomeRNAii8976.
NextBioi33689.
PROiO00401.
SOURCEiSearch...

Gene expression databases

BgeeiO00401.
CleanExiHS_WASL.
GenevisibleiO00401. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR030214. N-WASP.
IPR011993. PH_like_dom.
IPR011026. WASP_C.
IPR000697. WH1/EVH1_dom.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR12779:SF3. PTHR12779:SF3. 1 hit.
PfamiPF00786. PBD. 1 hit.
PF00568. WH1. 1 hit.
PF02205. WH2. 2 hits.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00461. WH1. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]
SUPFAMiSSF47912. SSF47912. 2 hits.
PROSITEiPS50108. CRIB. 1 hit.
PS50229. WH1. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of N-WASP homologs in human and rat brain."
    Fukuoka M., Miki H., Takenawa T.
    Gene 196:43-48(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Analysis of the anti-tumor T cell repertoire of melanoma patients vaccinated with a mixed tumor cell/DC vaccine."
    Lennerz V., Fatho M., Eberts D., Woelfel C., Schreiber S., Huber C., van der Bruggen P., Schmidt C.W., Woelfel T.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Melanoma.
  3. "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].
  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].
    Tissue: Brain.
  5. "Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri."
    Suzuki T., Miki H., Takenawa T., Sasakawa C.
    EMBO J. 17:2767-2776(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHIGELLA FLEXNERI ICSA.
  6. "Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility."
    Egile C., Loisel T.P., Laurent V., Li R., Pantaloni D., Sansonetti P.J., Carlier M.-F.
    J. Cell Biol. 146:1319-1332(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHIGELLA FLEXNERI ICSA.
  7. "Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual hydroxyamino acid specificity in a tyrosine kinase."
    Yokoyama N., Lougheed J., Miller W.T.
    J. Biol. Chem. 280:42219-42226(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-242 AND TYR-256 BY TNK2, INTERACTION WITH WASL.
  8. "NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS."
    Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W., Schilling K.
    J. Cell Sci. 118:5059-5069(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOSTRIN.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein."
    Zhang J., Zhang X., Guo Y., Xu L., Pei D.
    J. Biol. Chem. 284:21659-21669(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNX33.
  12. "Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation."
    Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., Robbins D., Rosen M.K., Saksela K., Leong J.M.
    Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), IDENTIFICATION IN A COMPLEX WITH BAIAP2L1 AND E.COLI EFFECTOR PROTEIN ESPF(U).
  13. "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 TYR-256; SER-484 AND SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-484 AND SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins."
    Aguda A.H., Xue B., Irobi E., Preat T., Robinson R.C.
    Structure 14:469-476(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 451-465.
  19. "Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex."
    Gaucher J.F., Mauge C., Didry D., Guichard B., Renault L., Carlier M.F.
    J. Biol. Chem. 287:34646-34659(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 392-484 IN COMPLEX WITH ACTIN, FUNCTION, SUBUNIT, INTERACTION WITH THE ARP2/3 COMPLEX, ACTIN-BINDING.
  20. "Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly."
    Aitio O., Hellman M., Skehan B., Kesti T., Leong J.M., Saksela K., Permi P.
    Structure 20:1692-1703(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 207-270 IN COMPLEX WITH BAIAP2L1 AND THE E.COLI SECRETED EFFECTOR PROTEIN ESPF(U), IDENTIFICATION IN A COMPLEX WITH BAIAP2L1 AND E.COLI EFFECTOR PROTEIN ESPF(U), FUNCTION.

Entry informationi

Entry nameiWASL_HUMAN
AccessioniPrimary (citable) accession number: O00401
Secondary accession number(s): A1JUI9, Q7Z746
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 2005
Last modified: June 24, 2015
This is version 155 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

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.