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CHICK:AFAP1

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Species (Taxon ID) Gallus gallus (Chicken). (9031)
Gene Name(s) AFAP1
Protein Name(s) Actin filament-associated protein 1

110 kDa actin filament-associated protein AFAP-110 Neural actin filament protein pp110

External Links
UniProt Q90738
EMBL L20303
L20302
PIR A54592
A55883
RefSeq NP_001128120.1
NP_989536.1
UniGene Gga.185
ProteinModelPortal Q90738
IntAct Q90738
MINT MINT-8013618
STRING 9031.ENSGALP00000025034
PaxDb Q90738
GeneID 374034
KEGG gga:374034
CTD 60312
eggNOG NOG48103
HOGENOM HOG000033832
HOVERGEN HBG106875
InParanoid Q90738
KO K18616
PhylomeDB Q90738
NextBio 20813560
PRO PR:Q90738
Proteomes UP000000539
GO GO:0005737
GO:0005856
GO:0051493
GO:0009966
Gene3D 2.30.29.30
InterPro IPR030113
IPR029907
IPR011993
IPR001849
PANTHER PTHR14338
PTHR14338:SF8
Pfam PF00169
SMART SM00233
PROSITE PS50003

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003779

actin binding

PMID:12134071[1]

ECO:0000314

F

Figure 1 shows that rAFAP-110 bind to actin filaments directly by using gel electrophoresis, EM negative staining, and centrifugation.

complete
CACAO 9392

GO:0003779

actin binding

PMID:12134071[1]

ECO:0000314

F

Figure 2 shows that rAFAP-110 cross links actin through carboxyl terminal region by using a low-speed cosedimentation assay (A), and centrifugation of cross linked actin filaments versus free rAFAP-110 (B).

complete
CACAO 9393

GO:0003779

actin binding

PMID:12134071[1]

ECO:0000314

F

Figure 3 shows rAFAP cross links actin filaments by incubating them with rhodamine-phalloidin-labeled actin filaments.

complete
CACAO 9394

GO:0003779

actin binding

PMID:12134071[1]

ECO:0000314

F

Figure 7 shows that PKC phosphorylation or leucine zipper deletion increases AFAp-110 ability to cross link actin filaments by incubating them with actin filaments (A) and incubating them with rhodamine-phalloidin-labeled actin filaments.

complete
CACAO 9397

involved_in

GO:0018109

peptidyl-arginine phosphorylation

PMID:15485829[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0018108

peptidyl-tyrosine phosphorylation

PMID:15485829[2]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P00523

P

Seeded From UniProt

complete

enables

GO:0042169

SH2 domain binding

PMID:15485829[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0017124

SH3 domain binding

PMID:15485829[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:10741420[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009966

regulation of signal transduction

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029907

P

Seeded From UniProt

complete

involved_in

GO:0051493

regulation of cytoskeleton organization

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029907

P

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206
UniProtKB-SubCell:SL-0090

C

Seeded From UniProt

complete

enables

GO:0017124

SH3 domain binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0729

F

Seeded From UniProt

complete

enables

GO:0003779

actin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0009

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Qian, Y et al. (2002) PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments. Mol. Biol. Cell 13 2311-22 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Han, B et al. (2004) Conversion of mechanical force into biochemical signaling. J. Biol. Chem. 279 54793-801 PubMed GONUTS page
  3. Lee, A et al. (2000) Stabilization and remodeling of the membrane skeleton during lens fiber cell differentiation and maturation. Dev. Dyn. 217 257-70 PubMed GONUTS page