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Q8N556

- AFAP1_HUMAN

UniProt

Q8N556 - AFAP1_HUMAN

Protein

Actin filament-associated protein 1

Gene

AFAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    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

    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: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:24017. AFAP1.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication
    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. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell

    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.

    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 – 2821Phosphoserine2 Publications
    Modified residuei283 – 2831Phosphoserine2 Publications
    Modified residuei548 – 5481Phosphoserine2 Publications
    Modified residuei664 – 6641Phosphoserine2 Publications
    Modified residuei665 – 6651Phosphoserine2 Publications
    Modified residuei668 – 6681Phosphoserine4 Publications
    Modified residuei679 – 6791Phosphoserine2 Publications
    Modified residuei687 – 6871Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine residues by SRC.4 Publications

    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. 8 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.
    HOGENOMiHOG000033832.
    HOVERGENiHBG106875.
    InParanoidiQ8N556.
    OMAiAGRKTQV.
    OrthoDBiEOG7KQ217.
    PhylomeDBiQ8N556.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    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. Align

    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

    MEELIVELRL FLELLDHEYL TSTVREKKAV ITNILLRIQS SKGFDVKDHA    50
    QKQETANSLP APPQMPLPEI PQPWLPPDSG PPPLPTSSLP EGYYEEAVPL 100
    SPGKAPEYIT SNYDSDAMSS SYESYDEEEE DGKGKKTRHQ WPSEEASMDL 150
    VKDAKICAFL LRKKRFGQWT KLLCVIKDTK LLCYKSSKDQ QPQMELPLQG 200
    CNITYIPKDS KKKKHELKIT QQGTDPLVLA VQSKEQAEQW LKVIKEAYSG 250
    CSGPVDSECP PPPSSPVHKA ELEKKLSSER PSSDGEGVVE NGITTCNGKE 300
    QVKRKKSSKS EAKGTVSKVT GKKITKIISL GKKKPSTDEQ TSSAEEDVPT 350
    CGYLNVLSNS RWRERWCRVK DNKLIFHKDR TDLKTHIVSI PLRGCEVIPG 400
    LDSKHPLTFR LLRNGQEVAV LEASSSEDMG RWIGILLAET GSSTDPEALH 450
    YDYIDVEMSA SVIQTAKQTF CFMNRRVISA NPYLGGTSNG YAHPSGTALH 500
    YDDVPCINGS LKGKKPPVAS NGVTGKGKTL SSQPKKADPA AVVKRTGSNA 550
    AQYKYGKNRV EADAKRLQTK EEELLKRKEA LRNRLAQLRK ERKDLRAAIE 600
    VNAGRKPQAI LEEKLKQLEE ECRQKEAERV SLELELTEVK ESLKKALAGG 650
    VTLGLAIEPK SGTSSPQSPV FRHRTLENSP ISSCDTSDTE GPVPVNSAAV 700
    LKKSQAAPGS SPCRGHVLRK AKEWELKNGT 730
    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:
    EMBL
    GenBank
    DDBJ
    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 databases

    DMDMi166919564.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3397.1. [Q8N556-1 ]
    CCDS47010.1. [Q8N556-2 ]
    RefSeqi NP_001128119.1. NM_001134647.1. [Q8N556-2 ]
    NP_940997.1. NM_198595.2. [Q8N556-1 ]
    UniGenei Hs.529369.

    3D structure databases

    ProteinModelPortali Q8N556.
    SMRi Q8N556. Positions 342-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121895. 8 interactions.
    IntActi Q8N556. 1 interaction.
    STRINGi 9606.ENSP00000410689.

    PTM databases

    PhosphoSitei Q8N556.

    Polymorphism databases

    DMDMi 166919564.

    Proteomic databases

    MaxQBi Q8N556.
    PaxDbi Q8N556.
    PRIDEi Q8N556.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358461 ; ENSP00000351245 ; ENSG00000196526 . [Q8N556-1 ]
    ENST00000360265 ; ENSP00000353402 ; ENSG00000196526 . [Q8N556-1 ]
    ENST00000382543 ; ENSP00000371983 ; ENSG00000196526 . [Q8N556-2 ]
    ENST00000420658 ; ENSP00000410689 ; ENSG00000196526 . [Q8N556-2 ]
    GeneIDi 60312.
    KEGGi hsa:60312.
    UCSCi uc003gkg.1. human. [Q8N556-1 ]
    uc011bwk.1. human.

    Organism-specific databases

    CTDi 60312.
    GeneCardsi GC04M007682.
    H-InvDB HIX0031430.
    HGNCi HGNC:24017. AFAP1.
    HPAi CAB024712.
    HPA015642.
    MIMi 608252. gene.
    neXtProti NX_Q8N556.
    PharmGKBi PA162375733.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG48103.
    HOGENOMi HOG000033832.
    HOVERGENi HBG106875.
    InParanoidi Q8N556.
    OMAi AGRKTQV.
    OrthoDBi EOG7KQ217.
    PhylomeDBi Q8N556.

    Miscellaneous databases

    ChiTaRSi AFAP1. human.
    GeneWikii AFAP1.
    GenomeRNAii 60312.
    NextBioi 65281.
    PROi Q8N556.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8N556.
    CleanExi HS_AFAP1.
    Genevestigatori Q8N556.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00169. PH. 2 hits.
    [Graphical view ]
    SMARTi SM00233. PH. 2 hits.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 91 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