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P02771

- FETA_HUMAN

UniProt

P02771 - FETA_HUMAN

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Protein
Alpha-fetoprotein
Gene
AFP, HPAFP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Copper or nickel1 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. SMAD protein signal transduction Source: Ensembl
  2. ovulation from ovarian follicle Source: Ensembl
  3. progesterone metabolic process Source: Ensembl
  4. transport Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Copper, Metal-binding, Nickel

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-fetoprotein
Alternative name(s):
Alpha-1-fetoprotein
Alpha-fetoglobulin
Gene namesi
Name:AFP
Synonyms:HPAFP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:317. AFP.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

MIMi104150. gene+phenotype.
Orphaneti168612. Congenital deficiency in alpha-fetoprotein.
168615. Hereditary persistence of alpha-fetoprotein.
PharmGKBiPA24614.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18184 Publications
Add
BLAST
Chaini19 – 609591Alpha-fetoprotein
PRO_0000001097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi99 ↔ 114
Disulfide bondi113 ↔ 124
Disulfide bondi148 ↔ 193
Disulfide bondi192 ↔ 201
Disulfide bondi224 ↔ 270
Glycosylationi251 – 2511N-linked (GlcNAc...)
CAR_000070
Disulfide bondi269 ↔ 277
Disulfide bondi289 ↔ 303
Disulfide bondi302 ↔ 313
Disulfide bondi384 ↔ 393
Disulfide bondi416 ↔ 462
Disulfide bondi461 ↔ 472
Disulfide bondi485 ↔ 501
Disulfide bondi500 ↔ 511
Disulfide bondi538 ↔ 583
Disulfide bondi582 ↔ 591

Post-translational modificationi

Independent studies suggest heterogeneity of the N-terminal sequence of the mature protein and of the cleavage site of the signal sequence.
Sulfated.

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

MaxQBiP02771.
PaxDbiP02771.
PeptideAtlasiP02771.
PRIDEiP02771.

PTM databases

PhosphoSiteiP02771.
UniCarbKBiP02771.

Expressioni

Tissue specificityi

Plasma. Synthesized by the fetal liver and yolk sac.

Developmental stagei

Occurs in the plasma of fetuses more than 4 weeks old, reaches the highest levels during the 12th-16th week of gestation, and drops to trace amounts after birth. The serum level in adults is usually less than 40 ng/ml. AFP occurs also at high levels in the plasma and ascitic fluid of adults with hepatoma.

Gene expression databases

ArrayExpressiP02771.
BgeeiP02771.
CleanExiHS_AFP.
GenevestigatoriP02771.

Organism-specific databases

HPAiCAB024283.
CAB025339.
HPA010607.
HPA023600.

Interactioni

Subunit structurei

Dimeric and trimeric forms have been found in addition to the monomeric form.

Protein-protein interaction databases

BioGridi106682. 11 interactions.
IntActiP02771. 9 interactions.
MINTiMINT-1401527.
STRINGi9606.ENSP00000226359.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MRKX-ray1.40P137-145[»]
ProteinModelPortaliP02771.
SMRiP02771. Positions 39-608.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 210192Albumin 1
Add
BLAST
Domaini211 – 402192Albumin 2
Add
BLAST
Domaini403 – 601199Albumin 3
Add
BLAST

Sequence similaritiesi

Belongs to the ALB/AFP/VDB family.
Contains 3 albumin domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG45992.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02771.
KOiK16144.
OrthoDBiEOG7S4X5C.
PhylomeDBiP02771.
TreeFamiTF335561.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 2 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02771-1 [UniParc]FASTAAdd to Basket

« Hide

MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF    50
FAQFVQEATY KEVSKMVKDA LTAIEKPTGD EQSSGCLENQ LPAFLEELCH 100
EKEILEKYGH SDCCSQSEEG RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA 150
YEEDRETFMN KFIYEIARRH PFLYAPTILL WAARYDKIIP SCCKAENAVE 200
CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV TKLSQKFTKV 250
NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT 300
ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF 350
LASFVHEYSR RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE 400
LQKYIQESQA LAKRSCGLFQ KLGEYYLQNA FLVAYTKKAP QLTSSELMAI 450
TRKMAATAAT CCQLSEDKLL ACGEGAADII IGHLCIRHEM TPVNPGVGQC 500
CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA QGVALQTMKQ 550
EFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEV CFAEEGQKLI 600
SKTRAALGV 609
Length:609
Mass (Da):68,678
Last modified:July 21, 1986 - v1
Checksum:i4D4E45820E1C2D4F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 1871K → Q.
Corresponds to variant rs35765619 [ dbSNP | Ensembl ].
VAR_033928
Natural varianti570 – 5701A → G.1 Publication
Corresponds to variant rs7790 [ dbSNP | Ensembl ].
VAR_012049

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01514 mRNA. Translation: CAA24758.1.
M16110 Genomic DNA. Translation: AAB58754.1.
AK314817 mRNA. Translation: BAG37340.1.
BC027881 mRNA. Translation: AAH27881.1.
M10949 Genomic DNA. Translation: AAA51674.1.
M10950 Genomic DNA. Translation: AAA51675.1.
Z19532 Genomic DNA. Translation: CAA79592.1.
CCDSiCCDS3556.1.
PIRiA26624. FPHU.
RefSeqiNP_001125.1. NM_001134.2.
UniGeneiHs.518808.

Genome annotation databases

EnsembliENST00000395792; ENSP00000379138; ENSG00000081051.
GeneIDi174.
KEGGihsa:174.
UCSCiuc003hgz.1. human.

Polymorphism databases

DMDMi120042.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Alpha-fetoprotein entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01514 mRNA. Translation: CAA24758.1 .
M16110 Genomic DNA. Translation: AAB58754.1 .
AK314817 mRNA. Translation: BAG37340.1 .
BC027881 mRNA. Translation: AAH27881.1 .
M10949 Genomic DNA. Translation: AAA51674.1 .
M10950 Genomic DNA. Translation: AAA51675.1 .
Z19532 Genomic DNA. Translation: CAA79592.1 .
CCDSi CCDS3556.1.
PIRi A26624. FPHU.
RefSeqi NP_001125.1. NM_001134.2.
UniGenei Hs.518808.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MRK X-ray 1.40 P 137-145 [» ]
ProteinModelPortali P02771.
SMRi P02771. Positions 39-608.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106682. 11 interactions.
IntActi P02771. 9 interactions.
MINTi MINT-1401527.
STRINGi 9606.ENSP00000226359.

PTM databases

PhosphoSitei P02771.
UniCarbKBi P02771.

Polymorphism databases

DMDMi 120042.

Proteomic databases

MaxQBi P02771.
PaxDbi P02771.
PeptideAtlasi P02771.
PRIDEi P02771.

Protocols and materials databases

DNASUi 174.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000395792 ; ENSP00000379138 ; ENSG00000081051 .
GeneIDi 174.
KEGGi hsa:174.
UCSCi uc003hgz.1. human.

Organism-specific databases

CTDi 174.
GeneCardsi GC04P074302.
HGNCi HGNC:317. AFP.
HPAi CAB024283.
CAB025339.
HPA010607.
HPA023600.
MIMi 104150. gene+phenotype.
neXtProti NX_P02771.
Orphaneti 168612. Congenital deficiency in alpha-fetoprotein.
168615. Hereditary persistence of alpha-fetoprotein.
PharmGKBi PA24614.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45992.
HOGENOMi HOG000293137.
HOVERGENi HBG004207.
InParanoidi P02771.
KOi K16144.
OrthoDBi EOG7S4X5C.
PhylomeDBi P02771.
TreeFami TF335561.

Miscellaneous databases

ChiTaRSi AFP. human.
GeneWikii Alpha-fetoprotein.
GenomeRNAii 174.
NextBioi 698.
PROi P02771.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02771.
Bgeei P02771.
CleanExi HS_AFP.
Genevestigatori P02771.

Family and domain databases

InterProi IPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view ]
Pfami PF00273. Serum_albumin. 3 hits.
[Graphical view ]
PIRSFi PIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSi PR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTi SM00103. ALBUMIN. 3 hits.
[Graphical view ]
SUPFAMi SSF48552. SSF48552. 3 hits.
PROSITEi PS00212. ALBUMIN_1. 2 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structures of human alpha-fetoprotein and its mRNA."
    Morinaga T., Sakai M., Wegmann T.G., Tamaoki T.
    Proc. Natl. Acad. Sci. U.S.A. 80:4604-4608(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure, polymorphism, and novel repeated DNA elements revealed by a complete sequence of the human alpha-fetoprotein gene."
    Gibbs P.E.M., Zielinski R., Boyd C., Dugaiczyk A.
    Biochemistry 26:1332-1343(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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], VARIANT GLY-570.
    Tissue: Heart.
  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].
    Tissue: Lung.
  5. "The human alpha-fetoprotein gene. Sequence organization and the 5' flanking region."
    Sakai M., Morinaga T., Urano Y., Watanabe K., Wegmann T.G., Tamaoki T.
    J. Biol. Chem. 260:5055-5060(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 AND 596-609, GENE STRUCTURE.
  6. "A G-->A substitution in an HNF I binding site in the human alpha-fetoprotein gene is associated with hereditary persistence of alpha-fetoprotein (HPAFP)."
    McVey J.H., Michaelides K., Hansen L.P., Ferguson-Smith M., Tilghman S., Krumlauf R., Tuddenham E.G.D.
    Hum. Mol. Genet. 2:379-384(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  7. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 311-332; 348-372 AND 422-437, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "Structure and evolution of human alpha-fetoprotein deduced from partial sequence of cloned cDNA."
    Beattie W.G., Dugaiczyk A.
    Gene 20:415-422(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 429-556.
  9. "Human alpha-fetoprotein primary structure: a mass spectrometric study."
    Pucci P., Siciliano R., Malorni A., Marino G., Tecce M.F., Ceccarini C., Terrana B.
    Biochemistry 30:5061-5066(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-609.
  10. "Studies on human alpha-fetoprotein. Isolation and characterization of monomeric and polymeric forms and amino-terminal sequence analysis."
    Yachnin S., Hsu R., Heinrikson R.L., Miller J.B.
    Biochim. Biophys. Acta 493:418-428(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-35.
  11. "Comparative chemical structures of human alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma."
    Aoyagi Y., Ikenaka T., Ichida F.
    Cancer Res. 37:3663-3667(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-38.
  12. "Alpha fetoprotein: structure and expression in man and inbred mouse strains under normal conditions and liver injury."
    Ruoslahti E., Pihko H., Vaheri A., Seppala M., Virolainen M., Konttinen A.
    Johns Hopkins Med. J. Suppl. 3:249-255(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-39.
  13. "Copper(II)-binding ability of human alpha-fetoprotein."
    Aoyagi Y., Ikenaka T., Ichida F.
    Cancer Res. 38:3483-3486(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: METAL-BINDING.
  14. "Alpha-fetoprotein as a carrier protein in plasma and its bilirubin-binding ability."
    Aoyagi Y., Ikenaka T., Ichida F.
    Cancer Res. 39:3571-3574(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: BILIRUBIN-BINDING.
  15. "Tyrosine sulfation of proteins from the human hepatoma cell line HepG2."
    Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.
    Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFETA_HUMAN
AccessioniPrimary (citable) accession number: P02771
Secondary accession number(s): B2RBU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 152 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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