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Protein

Alpha-fetoprotein

Gene

AFP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  1. ovulation from ovarian follicle Source: Ensembl
  2. progesterone metabolic process Source: Ensembl
  3. SMAD protein signal transduction 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 Componenti: 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

Involvement in diseasei

Alpha-fetoprotein deficiency (AFPD)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA benign condition characterized by undetectable AFP levels in the amniotic fluid. Affected individuals are asymptomatic and present normal development.

See also OMIM:615969
Alpha-fetoprotein, hereditary persistence (HPAFP)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA benign autosomal dominant condition characterized by continued expression of alpha-fetoprotein in adult life.

See also OMIM:615970

Organism-specific databases

MIMi615969. phenotype.
615970. phenotype.
Orphaneti168612. Congenital deficiency in alpha-fetoprotein.
168615. Hereditary persistence of alpha-fetoprotein.
PharmGKBiPA24614.

Polymorphism and mutation databases

BioMutaiAFP.
DMDMi120042.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 609591Alpha-fetoproteinPRO_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.1 Publication

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

BgeeiP02771.
CleanExiHS_AFP.
ExpressionAtlasiP02771. baseline and differential.
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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MRKX-ray1.40P137-145[»]
ProteinModelPortaliP02771.
SMRiP02771. Positions 39-608.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
Contains 3 albumin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG45992.
GeneTreeiENSGT00390000000113.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02771.
KOiK16144.
OrthoDBiEOG7S4X5C.
PhylomeDBiP02771.
TreeFamiTF335561.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
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

        10         20         30         40         50
MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF
60 70 80 90 100
FAQFVQEATY KEVSKMVKDA LTAIEKPTGD EQSSGCLENQ LPAFLEELCH
110 120 130 140 150
EKEILEKYGH SDCCSQSEEG RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA
160 170 180 190 200
YEEDRETFMN KFIYEIARRH PFLYAPTILL WAARYDKIIP SCCKAENAVE
210 220 230 240 250
CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV TKLSQKFTKV
260 270 280 290 300
NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT
310 320 330 340 350
ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF
360 370 380 390 400
LASFVHEYSR RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE
410 420 430 440 450
LQKYIQESQA LAKRSCGLFQ KLGEYYLQNA FLVAYTKKAP QLTSSELMAI
460 470 480 490 500
TRKMAATAAT CCQLSEDKLL ACGEGAADII IGHLCIRHEM TPVNPGVGQC
510 520 530 540 550
CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA QGVALQTMKQ
560 570 580 590 600
EFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEV CFAEEGQKLI

SKTRAALGV
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiAFP.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MRKX-ray1.40P137-145[»]
ProteinModelPortaliP02771.
SMRiP02771. Positions 39-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP02771.
UniCarbKBiP02771.

Polymorphism and mutation databases

BioMutaiAFP.
DMDMi120042.

Proteomic databases

MaxQBiP02771.
PaxDbiP02771.
PeptideAtlasiP02771.
PRIDEiP02771.

Protocols and materials databases

DNASUi174.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi174.
GeneCardsiGC04P074308.
HGNCiHGNC:317. AFP.
HPAiCAB024283.
CAB025339.
HPA010607.
HPA023600.
MIMi104150. gene.
615969. phenotype.
615970. phenotype.
neXtProtiNX_P02771.
Orphaneti168612. Congenital deficiency in alpha-fetoprotein.
168615. Hereditary persistence of alpha-fetoprotein.
PharmGKBiPA24614.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45992.
GeneTreeiENSGT00390000000113.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02771.
KOiK16144.
OrthoDBiEOG7S4X5C.
PhylomeDBiP02771.
TreeFamiTF335561.

Miscellaneous databases

ChiTaRSiAFP. human.
GeneWikiiAlpha-fetoprotein.
GenomeRNAii174.
NextBioi698.
PROiP02771.
SOURCEiSearch...

Gene expression databases

BgeeiP02771.
CleanExiHS_AFP.
ExpressionAtlasiP02771. baseline and differential.
GenevestigatoriP02771.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
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]
ProtoNetiSearch...

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, INVOLVEMENT IN HPAFP.
  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. "Congenital deficiency of alpha feto-protein."
    Sharony R., Zadik I., Parvari R.
    Eur. J. Hum. Genet. 12:871-874(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN AFPD.
  17. "A new mutation in the AFP gene responsible for a total absence of alpha feto-protein on second trimester maternal serum screening for Down syndrome."
    Petit F.M., Hebert M., Picone O., Brisset S., Maurin M.L., Parisot F., Capel L., Benattar C., Senat M.V., Tachdjian G., Labrune P.
    Eur. J. Hum. Genet. 17:387-390(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN AFPD.
  18. 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: April 29, 2015
This is version 158 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

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.