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Q80YS6 (AFAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin filament-associated protein 1
Alternative name(s):
110 kDa actin filament-associated protein
Short name=AFAP-110
Gene names
Name:Afap1
Synonyms:Kiaa3018
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can cross-link actin filaments into both network and bundle structures. May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton By similarity.

Subunit structure

Monomer and homomultimer. Interacts via its C-terminus with F-actin; probably involving AFAP1 multimers. Interacts with activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with PRKCA, PRKCB and PRKCI By similarity.

Subcellular location

Cytoplasm › cytoskeleton By similarity. Note: Localizes with stress fibers in quiescent cells, concentrated in cell motility structures such as lamellipodia, filopodia and membrane ruffles By similarity.

Post-translational modification

Phosphorylated on tyrosine residues by SRC By similarity.

Sequence similarities

Contains 2 PH domains.

Sequence caution

The sequence BAC98293.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DomainCoiled coil
Repeat
SH3-binding
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphospholipid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 731731Actin filament-associated protein 1
PRO_0000317659

Regions

Domain152 – 24897PH 1
Domain348 – 44295PH 2
Region595 – 63844Interaction with F-actin By similarity
Coiled coil558 – 64992 Potential
Motif70 – 734SH3-binding By similarity
Motif93 – 964SH2-binding 1 By similarity
Motif452 – 4576SH2-binding 2 By similarity
Compositional bias59 – 10547Pro-rich

Amino acid modifications

Modified residue2831Phosphoserine By similarity
Modified residue2841Phosphoserine By similarity
Modified residue5471Phosphothreonine Ref.5
Modified residue5491Phosphoserine By similarity
Modified residue6651Phosphoserine By similarity
Modified residue6661Phosphoserine By similarity
Modified residue6691Phosphoserine Ref.4
Modified residue6801Phosphoserine By similarity
Modified residue6881Phosphoserine By similarity

Experimental info

Sequence conflict431G → R in BAE28086. Ref.2
Sequence conflict521K → R in BAE28086. Ref.2
Sequence conflict2321S → G in BAC98293. Ref.1
Sequence conflict2491G → D in BAC98293. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80YS6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 58D3D31BED5C2FCD

FASTA73180,615
        10         20         30         40         50         60 
MEELIVELRL FLELLDHEYL TSTVREKKAV LTNILLRLQS SKGFEVKDHA QKAEANNLPA 

        70         80         90        100        110        120 
PPQMPLPEIP QPWLPPDSGP PPLPTSSLPE GYYEEAVPLS PGKAPEYITS NYDSDAMSSS 

       130        140        150        160        170        180 
YESYDEEEED GKGKKTRHQW PSEEASMDLV KDAKICAFLL RKKRFGQWTK LLCVIKDTKL 

       190        200        210        220        230        240 
LCYKSSKDQQ PQMELPLQGC SITYIPRDSK KKKHELKITQ QGTDPLVLAV QSKEQAEQWL 

       250        260        270        280        290        300 
KVIKEAYSGC SGPVDPECSP PPSTSAPVNK AELEKKLSSE RPSSDGEGGV ENGVTTCNGK 

       310        320        330        340        350        360 
EQAKRKKPSK SEAKGTVSKV TGKKITKIIG LGKKKPSTDE QTSSAEEDVP TCGYLNVLSN 

       370        380        390        400        410        420 
SRWRERWCRV KDSKLILHKD RADLKTHLVS IPLRGCEVIP GLDSKHPLTF RLLRNGQEVA 

       430        440        450        460        470        480 
VLEASSSEDM GRWIGILLAE TGSSTDPGAL HYDYIDVEMS ANVIQTAKQT FCFMNRRAVS 

       490        500        510        520        530        540 
TSPYLGSLSN GYAHPSGTAL HYDDVPCVNG SLKNKKPPAS SNGVPVKGKA PSSQQKKVET 

       550        560        570        580        590        600 
AGGVKRTASN AEQYKYGKNR VEADAKRLQS KEEELLKRKE ALRNRLAQLR KERKDLRAAI 

       610        620        630        640        650        660 
EVNAGRKTQA ALEDKLKRLE EECKQREAER VSLELELTEV KESLKKALAG GVTLGLAIEP 

       670        680        690        700        710        720 
RSGTSSPQSP VFRHRTLENS PISSCDTSDA EGPLPVNSAA VLKKSQPSSG SSPCRGHVLQ 

       730 
KAKEWELKNG T

« Hide

References

[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Melanocyte, Placenta and Testis.
[3]"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: Testis.
[4]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, MASS SPECTROMETRY.
Tissue: Brain cortex.
[5]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-547, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK129483 mRNA. Translation: BAC98293.1. Different initiation.
AK147706 mRNA. Translation: BAE28086.1.
AK148000 mRNA. Translation: BAE28280.1.
AK161385 mRNA. Translation: BAE36364.1.
BC050814 mRNA. Translation: AAH50814.1.
IPIIPI00467327.
RefSeqNP_081649.1. NM_027373.2.
UniGeneMm.125167.

3D structure databases

HSSPHSSP built from PDB template 2COF based on UniProtKB Q8N4X5.
ProteinModelPortalQ80YS6.
SMRQ80YS6. Positions 156-248, 343-438.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000067779.

PTM databases

PhosphoSiteQ80YS6.

Proteomic databases

PaxDbQ80YS6.
PRIDEQ80YS6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064571; ENSMUSP00000067779; ENSMUSG00000029094.
GeneID70292.
KEGGmmu:70292.
UCSCuc008xej.1. mouse.

Organism-specific databases

CTD60312.
MGIMGI:1917542. Afap1.
RougeSearch...

Phylogenomic databases

eggNOGNOG48103.
GeneTreeENSGT00390000003998.
HOGENOMHOG000033832.
HOVERGENHBG106875.
InParanoidQ80YS6.
OMASPVHKTE.
OrthoDBEOG4J117M.

Gene expression databases

ArrayExpressQ80YS6.
BgeeQ80YS6.
CleanExMM_AFAP1.
GenevestigatorQ80YS6.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00169. PH. 2 hits.
[Graphical view]
SMARTSM00233. PH. 2 hits.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAFAP1. mouse.
NextBio331322.
SOURCESearch...

Entry information

Entry nameAFAP1_MOUSE
AccessionPrimary (citable) accession number: Q80YS6
Secondary accession number(s): Q3UGX1, Q6ZPE4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents