Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O00401 (WASL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neural Wiskott-Aldrich syndrome protein

Short name=N-WASP
Gene names
Name:WASL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.12 Ref.19 Ref.20

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.19 Ref.20

Subcellular location

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

Post-translational modification

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

Sequence similarities

Contains 1 CRIB domain.

Contains 1 WH1 domain.

Contains 2 WH2 domains.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

actin polymerization or depolymerization

Traceable author statement PubMed 9422512. Source: ProtInc

axon guidance

Traceable author statement. Source: Reactome

cellular component movement

Traceable author statement PubMed 9422512. Source: ProtInc

cellular protein complex localization

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

membrane budding

Inferred from sequence or structural similarity. Source: BHF-UCL

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

nitric oxide metabolic process

Traceable author statement. Source: Reactome

positive regulation of Arp2/3 complex-mediated actin nucleation

Inferred from electronic annotation. Source: InterPro

positive regulation of clathrin-mediated endocytosis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

protein complex assembly

Traceable author statement PubMed 9422512. Source: ProtInc

regulation of nitric-oxide synthase activity

Traceable author statement. Source: Reactome

regulation of protein localization

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to bacterium

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

spindle localization

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle organization

Inferred from sequence or structural similarity. Source: BHF-UCL

vesicle transport along actin filament

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentactin cap

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Traceable author statement PubMed 9422512. Source: ProtInc

cytoplasmic membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lamellipodium

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionsmall GTPase regulator activity

Traceable author statement PubMed 9422512. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 505504Neural Wiskott-Aldrich syndrome protein
PRO_0000189000

Regions

Domain34 – 141108WH1
Domain203 – 21614CRIB
Domain405 – 42218WH2 1
Domain433 – 45018WH2 2
Compositional bias277 – 392116Pro-rich
Compositional bias485 – 50521Asp-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.10 Ref.16 Ref.17
Modified residue2421Phosphoserine; by TNK2 Ref.7
Modified residue2561Phosphotyrosine; by FAK1 and TNK2 Ref.7 Ref.13
Modified residue4841Phosphoserine Ref.13 Ref.15
Modified residue4851Phosphoserine Ref.13 Ref.15

Experimental info

Sequence conflict761Y → H in BAA20128. Ref.1
Sequence conflict2011A → G in BAA20128. Ref.1
Sequence conflict2231F → S in BAA20128. Ref.1
Sequence conflict2421S → L in BAA20128. Ref.1
Sequence conflict2481D → E in BAA20128. Ref.1
Sequence conflict2521S → L in BAA20128. Ref.1
Sequence conflict2961N → S in BAA20128. Ref.1
Sequence conflict3331A → E in BAA20128. Ref.1
Sequence conflict3511P → L in CAL26602. Ref.2

Secondary structure

................ 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00401 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: B5895C6055E23049

FASTA50554,827
        10         20         30         40         50         60 
MSSVQQQPPP PRRVTNVGSL LLTPQENESL FTFLGKKCVT MSSAVVQLYA ADRNCMWSKK 

        70         80         90        100        110        120 
CSGVACLVKD NPQRSYFLRI FDIKDGKLLW EQELYNNFVY NSPRGYFHTF AGDTCQVALN 

       130        140        150        160        170        180 
FANEEEAKKF RKAVTDLLGR RQRKSEKRRD PPNGPNLPMA TVDIKNPEIT TNRFYGPQVN 

       190        200        210        220        230        240 
NISHTKEKKK GKAKKKRLTK ADIGTPSNFQ HIGHVGWDPN TGFDLNNLDP ELKNLFDMCG 

       250        260        270        280        290        300 
ISEAQLKDRE TSKVIYDFIE KTGGVEAVKN ELRRQAPPPP PPSRGGPPPP PPPPHNSGPP 

       310        320        330        340        350        360 
PPPARGRGAP PPPPSRAPTA APPPPPPSRP SVAVPPPPPN RMYPPPPPAL PSSAPSGPPP 

       370        380        390        400        410        420 
PPPSVLGVGP VAPPPPPPPP PPPGPPPPPG LPSDGDHQVP TTAGNKAALL DQIREGAQLK 

       430        440        450        460        470        480 
KVEQNSRPVS CSGRDALLDQ IRQGIQLKSV ADGQESTPPT PAPTSGIVGA LMEVMQKRSK 

       490        500 
AIHSSDEDED EDDEEDFEDD DEWED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88460 mRNA. Translation: BAA20128.1.
AM295156 mRNA. Translation: CAL26602.1.
AC006333 Genomic DNA. Translation: AAQ96857.1.
BC052955 mRNA. Translation: AAH52955.1.
RefSeqNP_003932.3. NM_003941.3.
UniGeneHs.143728.
Hs.731519.
Hs.83916.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO00401.
SMRO00401. Positions 29-150, 195-253, 403-450, 466-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114466. 44 interactions.
DIPDIP-29042N.
IntActO00401. 34 interactions.
MINTMINT-157215.
STRING9606.ENSP00000223023.

PTM databases

PhosphoSiteO00401.

Proteomic databases

PaxDbO00401.
PRIDEO00401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223023; ENSP00000223023; ENSG00000106299.
GeneID8976.
KEGGhsa:8976.
UCSCuc003vkz.3. human.

Organism-specific databases

CTD8976.
GeneCardsGC07M123321.
HGNCHGNC:12735. WASL.
HPACAB005399.
HPA005750.
MIM605056. gene.
neXtProtNX_O00401.
PharmGKBPA37346.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270974.
HOGENOMHOG000143378.
HOVERGENHBG000222.
InParanoidO00401.
KOK05747.
OMASKKCCGV.
OrthoDBEOG7FJH20.
PhylomeDBO00401.
TreeFamTF316736.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_111217. Metabolism.
REACT_6900. Immune System.
SignaLinkO00401.

Gene expression databases

BgeeO00401.
CleanExHS_WASL.
GenevestigatorO00401.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011993. PH_like_dom.
IPR027641. WASP.
IPR011026. WASP_C.
IPR000697. WH1/EVH1.
IPR003124. WH2_dom.
[Graphical view]
PANTHERPTHR12779. PTHR12779. 1 hit.
PfamPF00786. PBD. 1 hit.
PF00568. WH1. 1 hit.
PF02205. WH2. 2 hits.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00461. WH1. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]
SUPFAMSSF47912. SSF47912. 2 hits.
PROSITEPS50108. CRIB. 1 hit.
PS50229. WH1. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWASL. human.
EvolutionaryTraceO00401.
GeneWikiWASL_(gene).
GenomeRNAi8976.
NextBio33689.
PROO00401.
SOURCESearch...

Entry information

Entry nameWASL_HUMAN
AccessionPrimary (citable) accession number: O00401
Secondary accession number(s): A1JUI9, Q7Z746
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 2005
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM