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Protein

Actin filament-associated protein 1

Gene

Afap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Actin filament-associated protein 1
Alternative name(s):
110 kDa actin filament-associated protein
Short name:
AFAP-110
Gene namesi
Name:Afap1
Synonyms:Kiaa3018
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1917542. Afap1.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731Actin filament-associated protein 1PRO_0000317659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity
Modified residuei549 – 5491PhosphoserineBy similarity
Modified residuei665 – 6651PhosphoserineBy similarity
Modified residuei666 – 6661PhosphoserineBy similarity
Modified residuei669 – 6691Phosphoserine1 Publication
Modified residuei680 – 6801PhosphoserineBy similarity
Modified residuei688 – 6881PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues by SRC.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ80YS6.
PaxDbiQ80YS6.
PRIDEiQ80YS6.

PTM databases

PhosphoSiteiQ80YS6.

Expressioni

Gene expression databases

BgeeiQ80YS6.
CleanExiMM_AFAP1.
ExpressionAtlasiQ80YS6. baseline and differential.
GenevisibleiQ80YS6. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ80YS6. 1 interaction.
MINTiMINT-7300872.
STRINGi10090.ENSMUSP00000067779.

Structurei

3D structure databases

ProteinModelPortaliQ80YS6.
SMRiQ80YS6. Positions 343-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 24897PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini348 – 44295PH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni595 – 63844Interaction with F-actinBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili558 – 64992Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi70 – 734SH3-bindingBy similarity
Motifi93 – 964SH2-binding 1By similarity
Motifi452 – 4576SH2-binding 2By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi59 – 10547Pro-richAdd
BLAST

Sequence similaritiesi

Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3-binding

Phylogenomic databases

eggNOGiNOG48103.
GeneTreeiENSGT00390000003998.
HOGENOMiHOG000033832.
HOVERGENiHBG106875.
InParanoidiQ80YS6.
KOiK18616.
OMAiAGRKTQV.
OrthoDBiEOG7KQ217.
PhylomeDBiQ80YS6.
TreeFamiTF332622.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR030113. AFAP.
IPR029907. AFAP-110.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR14338. PTHR14338. 1 hit.
PTHR14338:SF8. PTHR14338:SF8. 1 hit.
PfamiPF00169. PH. 2 hits.
[Graphical view]
SMARTiSM00233. PH. 2 hits.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80YS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEELIVELRL FLELLDHEYL TSTVREKKAV LTNILLRLQS SKGFEVKDHA
60 70 80 90 100
QKAEANNLPA PPQMPLPEIP QPWLPPDSGP PPLPTSSLPE GYYEEAVPLS
110 120 130 140 150
PGKAPEYITS NYDSDAMSSS YESYDEEEED GKGKKTRHQW PSEEASMDLV
160 170 180 190 200
KDAKICAFLL RKKRFGQWTK LLCVIKDTKL LCYKSSKDQQ PQMELPLQGC
210 220 230 240 250
SITYIPRDSK KKKHELKITQ QGTDPLVLAV QSKEQAEQWL KVIKEAYSGC
260 270 280 290 300
SGPVDPECSP PPSTSAPVNK AELEKKLSSE RPSSDGEGGV ENGVTTCNGK
310 320 330 340 350
EQAKRKKPSK SEAKGTVSKV TGKKITKIIG LGKKKPSTDE QTSSAEEDVP
360 370 380 390 400
TCGYLNVLSN SRWRERWCRV KDSKLILHKD RADLKTHLVS IPLRGCEVIP
410 420 430 440 450
GLDSKHPLTF RLLRNGQEVA VLEASSSEDM GRWIGILLAE TGSSTDPGAL
460 470 480 490 500
HYDYIDVEMS ANVIQTAKQT FCFMNRRAVS TSPYLGSLSN GYAHPSGTAL
510 520 530 540 550
HYDDVPCVNG SLKNKKPPAS SNGVPVKGKA PSSQQKKVET AGGVKRTASN
560 570 580 590 600
AEQYKYGKNR VEADAKRLQS KEEELLKRKE ALRNRLAQLR KERKDLRAAI
610 620 630 640 650
EVNAGRKTQA ALEDKLKRLE EECKQREAER VSLELELTEV KESLKKALAG
660 670 680 690 700
GVTLGLAIEP RSGTSSPQSP VFRHRTLENS PISSCDTSDA EGPLPVNSAA
710 720 730
VLKKSQPSSG SSPCRGHVLQ KAKEWELKNG T
Length:731
Mass (Da):80,615
Last modified:June 1, 2003 - v1
Checksum:i58D3D31BED5C2FCD
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431G → R in BAE28086 (PubMed:16141072).Curated
Sequence conflicti52 – 521K → R in BAE28086 (PubMed:16141072).Curated
Sequence conflicti232 – 2321S → G in BAC98293 (PubMed:14621295).Curated
Sequence conflicti249 – 2491G → D in BAC98293 (PubMed:14621295).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19236.1.
RefSeqiNP_081649.1. NM_027373.2.
UniGeneiMm.125167.

Genome annotation databases

EnsembliENSMUST00000064571; ENSMUSP00000067779; ENSMUSG00000029094.
GeneIDi70292.
KEGGimmu:70292.
UCSCiuc008xej.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19236.1.
RefSeqiNP_081649.1. NM_027373.2.
UniGeneiMm.125167.

3D structure databases

ProteinModelPortaliQ80YS6.
SMRiQ80YS6. Positions 343-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80YS6. 1 interaction.
MINTiMINT-7300872.
STRINGi10090.ENSMUSP00000067779.

PTM databases

PhosphoSiteiQ80YS6.

Proteomic databases

MaxQBiQ80YS6.
PaxDbiQ80YS6.
PRIDEiQ80YS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064571; ENSMUSP00000067779; ENSMUSG00000029094.
GeneIDi70292.
KEGGimmu:70292.
UCSCiuc008xej.1. mouse.

Organism-specific databases

CTDi60312.
MGIiMGI:1917542. Afap1.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG48103.
GeneTreeiENSGT00390000003998.
HOGENOMiHOG000033832.
HOVERGENiHBG106875.
InParanoidiQ80YS6.
KOiK18616.
OMAiAGRKTQV.
OrthoDBiEOG7KQ217.
PhylomeDBiQ80YS6.
TreeFamiTF332622.

Miscellaneous databases

ChiTaRSiAfap1. mouse.
NextBioi331322.
PROiQ80YS6.
SOURCEiSearch...

Gene expression databases

BgeeiQ80YS6.
CleanExiMM_AFAP1.
ExpressionAtlasiQ80YS6. baseline and differential.
GenevisibleiQ80YS6. MM.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR030113. AFAP.
IPR029907. AFAP-110.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR14338. PTHR14338. 1 hit.
PTHR14338:SF8. PTHR14338:SF8. 1 hit.
PfamiPF00169. PH. 2 hits.
[Graphical view]
SMARTiSM00233. PH. 2 hits.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAFAP1_MOUSE
AccessioniPrimary (citable) accession number: Q80YS6
Secondary accession number(s): Q3UGX1, Q6ZPE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.