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Protein

Actin filament-associated protein 1

Gene

AFAP1

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

Functioni

Can cross-link actin filaments into both network and bundle structures (By similarity). 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. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.By similarity1 Publication

GO - Biological processi

  1. regulation of cytoskeleton organization Source: InterPro
  2. regulation of signal transduction Source: InterPro
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:AFAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24017. AFAP1.

Subcellular locationi

  1. Cytoplasmcytoskeleton 1 Publication

  2. Note: Localizes with stress fibers in quiescent cells, concentrated in cell motility structures such as lamellipodia, filopodia and membrane ruffles upon their induction.

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: HPA
  3. focal adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711P → A: Decreased tyrosine phosphorylation. 1 Publication
Mutagenesisi77 – 771P → A: No effect on tyrosine phosphorylation. 1 Publication
Mutagenesisi93 – 931Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-94; F-125; F-451 and F-453. 1 Publication
Mutagenesisi94 – 941Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-125; F-451 and F-453. 1 Publication
Mutagenesisi125 – 1251Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-451 and F-453. 1 Publication
Mutagenesisi451 – 4511Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-453. 1 Publication
Mutagenesisi453 – 4531Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-451. 1 Publication

Organism-specific databases

PharmGKBiPA162375733.

Polymorphism and mutation databases

BioMutaiAFAP1.
DMDMi166919564.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 730730Actin filament-associated protein 1PRO_0000317658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei282 – 2821Phosphoserine1 Publication
Modified residuei283 – 2831Phosphoserine1 Publication
Modified residuei548 – 5481Phosphoserine1 Publication
Modified residuei664 – 6641Phosphoserine1 Publication
Modified residuei665 – 6651Phosphoserine1 Publication
Modified residuei668 – 6681Phosphoserine4 Publications
Modified residuei679 – 6791Phosphoserine1 Publication
Modified residuei687 – 6871Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues by SRC.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8N556.
PaxDbiQ8N556.
PRIDEiQ8N556.

PTM databases

PhosphoSiteiQ8N556.

Expressioni

Tissue specificityi

Low expression in normal breast epithelial cell line MCF-10A and in tumorigenic breast cancer cell lines MCF-7, T-47D and ZR-75-1. Highly expressed in the invasive breast cancer cell lines MDA-MB-231 and MDA-MB-435. Overexpressed in prostate carcinoma.2 Publications

Gene expression databases

BgeeiQ8N556.
CleanExiHS_AFAP1.
GenevestigatoriQ8N556.

Organism-specific databases

HPAiCAB024712.
HPA015642.

Interactioni

Subunit structurei

Monomer and homomultimer. Interacts via its C-terminus with F-actin; probably involving AFAP1 multimers (By similarity). 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

BioGridi121895. 10 interactions.
IntActiQ8N556. 1 interaction.
STRINGi9606.ENSP00000410689.

Structurei

3D structure databases

ProteinModelPortaliQ8N556.
SMRiQ8N556. Positions 342-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 24997PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini347 – 44195PH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni594 – 63744Interaction with F-actinBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili557 – 64892Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi71 – 744SH3-bindingBy similarity
Motifi94 – 974SH2-binding 1By similarity
Motifi451 – 4566SH2-binding 2By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 10647Pro-richAdd
BLAST

Sequence similaritiesi

Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG48103.
GeneTreeiENSGT00390000003998.
HOGENOMiHOG000033832.
HOVERGENiHBG106875.
InParanoidiQ8N556.
KOiK18616.
OMAiAGRKTQV.
OrthoDBiEOG7KQ217.
PhylomeDBiQ8N556.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR030113. AFAP.
IPR029907. AFAP-110.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N556-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEELIVELRL FLELLDHEYL TSTVREKKAV ITNILLRIQS SKGFDVKDHA
60 70 80 90 100
QKQETANSLP APPQMPLPEI PQPWLPPDSG PPPLPTSSLP EGYYEEAVPL
110 120 130 140 150
SPGKAPEYIT SNYDSDAMSS SYESYDEEEE DGKGKKTRHQ WPSEEASMDL
160 170 180 190 200
VKDAKICAFL LRKKRFGQWT KLLCVIKDTK LLCYKSSKDQ QPQMELPLQG
210 220 230 240 250
CNITYIPKDS KKKKHELKIT QQGTDPLVLA VQSKEQAEQW LKVIKEAYSG
260 270 280 290 300
CSGPVDSECP PPPSSPVHKA ELEKKLSSER PSSDGEGVVE NGITTCNGKE
310 320 330 340 350
QVKRKKSSKS EAKGTVSKVT GKKITKIISL GKKKPSTDEQ TSSAEEDVPT
360 370 380 390 400
CGYLNVLSNS RWRERWCRVK DNKLIFHKDR TDLKTHIVSI PLRGCEVIPG
410 420 430 440 450
LDSKHPLTFR LLRNGQEVAV LEASSSEDMG RWIGILLAET GSSTDPEALH
460 470 480 490 500
YDYIDVEMSA SVIQTAKQTF CFMNRRVISA NPYLGGTSNG YAHPSGTALH
510 520 530 540 550
YDDVPCINGS LKGKKPPVAS NGVTGKGKTL SSQPKKADPA AVVKRTGSNA
560 570 580 590 600
AQYKYGKNRV EADAKRLQTK EEELLKRKEA LRNRLAQLRK ERKDLRAAIE
610 620 630 640 650
VNAGRKPQAI LEEKLKQLEE ECRQKEAERV SLELELTEVK ESLKKALAGG
660 670 680 690 700
VTLGLAIEPK SGTSSPQSPV FRHRTLENSP ISSCDTSDTE GPVPVNSAAV
710 720 730
LKKSQAAPGS SPCRGHVLRK AKEWELKNGT
Length:730
Mass (Da):80,725
Last modified:February 5, 2008 - v2
Checksum:i4E916BB4F82F5547
GO
Isoform 2 (identifier: Q8N556-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     510-510: S → SWEPEDGFPA...GRASLGLNSQ

Note: No experimental confirmation available.Curated

Show »
Length:814
Mass (Da):89,795
Checksum:iB066A95292C261FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971P → L in AAG17055 (PubMed:15485829).Curated
Sequence conflicti223 – 2231G → D in AAG17055 (PubMed:15485829).Curated
Sequence conflicti238 – 2381E → G in AAG17055 (PubMed:15485829).Curated
Sequence conflicti465 – 4651T → A in BAF83496 (PubMed:14702039).Curated
Isoform 2 (identifier: Q8N556-2)
Sequence conflicti561 – 5611A → V in BAG60004 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti403 – 4031S → C.2 Publications
Corresponds to variant rs28406288 [ dbSNP | Ensembl ].
VAR_038578
Natural varianti518 – 5181V → M.1 Publication
Corresponds to variant rs41264705 [ dbSNP | Ensembl ].
VAR_038579

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei510 – 5101S → SWEPEDGFPASCSRGLGEEV LYDNAGLYDNLPPPHIFARY SPADRKASRLSADKLSSNHY KYPASAQSVTNTSSVGRASL GLNSQ in isoform 2. 1 PublicationVSP_044838

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188700 mRNA. Translation: AAG17055.1.
AK290807 mRNA. Translation: BAF83496.1.
AK297631 mRNA. Translation: BAG60004.1.
AC004169 Genomic DNA. No translation available.
AC097381 Genomic DNA. No translation available.
AC112254 Genomic DNA. No translation available.
AC141931 Genomic DNA. No translation available.
AC144451 Genomic DNA. No translation available.
BC032777 mRNA. Translation: AAH32777.1.
AB209676 mRNA. Translation: BAD92913.1.
CCDSiCCDS3397.1. [Q8N556-1]
CCDS47010.1. [Q8N556-2]
RefSeqiNP_001128119.1. NM_001134647.1. [Q8N556-2]
NP_940997.1. NM_198595.2. [Q8N556-1]
UniGeneiHs.529369.

Genome annotation databases

EnsembliENST00000358461; ENSP00000351245; ENSG00000196526. [Q8N556-1]
ENST00000360265; ENSP00000353402; ENSG00000196526. [Q8N556-1]
ENST00000382543; ENSP00000371983; ENSG00000196526. [Q8N556-2]
ENST00000420658; ENSP00000410689; ENSG00000196526. [Q8N556-2]
GeneIDi60312.
KEGGihsa:60312.
UCSCiuc003gkg.1. human. [Q8N556-1]
uc011bwk.1. human.

Polymorphism and mutation databases

BioMutaiAFAP1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188700 mRNA. Translation: AAG17055.1.
AK290807 mRNA. Translation: BAF83496.1.
AK297631 mRNA. Translation: BAG60004.1.
AC004169 Genomic DNA. No translation available.
AC097381 Genomic DNA. No translation available.
AC112254 Genomic DNA. No translation available.
AC141931 Genomic DNA. No translation available.
AC144451 Genomic DNA. No translation available.
BC032777 mRNA. Translation: AAH32777.1.
AB209676 mRNA. Translation: BAD92913.1.
CCDSiCCDS3397.1. [Q8N556-1]
CCDS47010.1. [Q8N556-2]
RefSeqiNP_001128119.1. NM_001134647.1. [Q8N556-2]
NP_940997.1. NM_198595.2. [Q8N556-1]
UniGeneiHs.529369.

3D structure databases

ProteinModelPortaliQ8N556.
SMRiQ8N556. Positions 342-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121895. 10 interactions.
IntActiQ8N556. 1 interaction.
STRINGi9606.ENSP00000410689.

PTM databases

PhosphoSiteiQ8N556.

Polymorphism and mutation databases

BioMutaiAFAP1.
DMDMi166919564.

Proteomic databases

MaxQBiQ8N556.
PaxDbiQ8N556.
PRIDEiQ8N556.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358461; ENSP00000351245; ENSG00000196526. [Q8N556-1]
ENST00000360265; ENSP00000353402; ENSG00000196526. [Q8N556-1]
ENST00000382543; ENSP00000371983; ENSG00000196526. [Q8N556-2]
ENST00000420658; ENSP00000410689; ENSG00000196526. [Q8N556-2]
GeneIDi60312.
KEGGihsa:60312.
UCSCiuc003gkg.1. human. [Q8N556-1]
uc011bwk.1. human.

Organism-specific databases

CTDi60312.
GeneCardsiGC04M007682.
H-InvDBHIX0031430.
HGNCiHGNC:24017. AFAP1.
HPAiCAB024712.
HPA015642.
MIMi608252. gene.
neXtProtiNX_Q8N556.
PharmGKBiPA162375733.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG48103.
GeneTreeiENSGT00390000003998.
HOGENOMiHOG000033832.
HOVERGENiHBG106875.
InParanoidiQ8N556.
KOiK18616.
OMAiAGRKTQV.
OrthoDBiEOG7KQ217.
PhylomeDBiQ8N556.

Miscellaneous databases

ChiTaRSiAFAP1. human.
GeneWikiiAFAP1.
GenomeRNAii60312.
NextBioi65281.
PROiQ8N556.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N556.
CleanExiHS_AFAP1.
GenevestigatoriQ8N556.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR030113. AFAP.
IPR029907. AFAP-110.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[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

« Hide 'large scale' publications
  1. "Conversion of mechanical force into biochemical signaling."
    Han B., Bai X.H., Lodyga M., Xu J., Yang B.B., Keshavjee S., Post M., Liu M.
    J. Biol. Chem. 279:54793-54801(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRC, PHOSPHORYLATION BY SRC, MUTAGENESIS OF PRO-71; PRO-77; TYR-93; TYR-94; TYR-125; TYR-451 AND TYR-453.
    Tissue: Lung.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT CYS-403.
    Tissue: Brain and Kidney.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORM 1), VARIANT CYS-403.
    Tissue: Brain.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-730 (ISOFORM 1), VARIANT MET-518.
    Tissue: Brain.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells."
    Dorfleutner A., Stehlik C., Zhang J., Gallick G.E., Flynn D.C.
    J. Cell. Physiol. 213:740-749(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, KNOCKDOWN IN MDA-MB-231 CELLS.
  8. "AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts."
    Zhang J., Park S.I., Artime M.C., Summy J.M., Shah A.N., Bomser J.A., Dorfleutner A., Flynn D.C., Gallick G.E.
    J. Clin. Invest. 117:2962-2973(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, POSSIBLE FUNCTION IN PROSTATE CANCER PROGRESSION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-283; SER-664; SER-665; SER-668; SER-679 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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 SER-548 AND SER-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAFAP1_HUMAN
AccessioniPrimary (citable) accession number: Q8N556
Secondary accession number(s): A8K442
, B4DMU2, E9PDT7, Q59EY5, Q9HBY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: April 29, 2015
This is version 96 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

Miscellaneous

Knockdown in MDA-MB-231 cells resulted in loss of actin stress fibers, decreased adhesion and spreading on fibronectin.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.