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Q8N556

- AFAP1_HUMAN

UniProt

Q8N556 - AFAP1_HUMAN

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Protein
Actin filament-associated protein 1
Gene
AFAP1, AFAP
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

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
Note: Localizes with stress fibers in quiescent cells, concentrated in cell motility structures such as lamellipodia, filopodia and membrane ruffles upon their induction.1 Publication

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 730730Actin filament-associated protein 1
PRO_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 – 6681Phosphoserine3 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.1 Publication

Protein-protein interaction databases

BioGridi121895. 8 interactions.
IntActiQ8N556. 1 interaction.
STRINGi9606.ENSP00000410689.

Structurei

3D structure databases

ProteinModelPortaliQ8N556.
SMRiQ8N556. Positions 342-437.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 24997PH 1
Add
BLAST
Domaini347 – 44195PH 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni594 – 63744Interaction with F-actin By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili557 – 64892 Reviewed prediction
Add
BLAST

Motif

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

Compositional bias

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

Sequence similaritiesi

Contains 2 PH domains.

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.

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

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.
VSP_044838

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971P → L in AAG17055. 1 Publication
Sequence conflicti223 – 2231G → D in AAG17055. 1 Publication
Sequence conflicti238 – 2381E → G in AAG17055. 1 Publication
Sequence conflicti465 – 4651T → A in BAF83496. 1 Publication
Isoform 2 (identifier: Q8N556-2)
Sequence conflicti561 – 5611A → V in BAG60004. 1 Publication

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

« 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].

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: September 3, 2014
This is version 90 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