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P08697 (A2AP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-2-antiplasmin

Short name=Alpha-2-AP
Alternative name(s):
Alpha-2-plasmin inhibitor
Short name=Alpha-2-PI
Serpin F2
Gene names
Name:SERPINF2
Synonyms:AAP, PLI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin. Ref.16

Subunit structure

Forms protease inhibiting heterodimer with TMPRSS7.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Involvement in disease

Alpha-2-plasmin inhibitor deficiency (APLID) [MIM:262850]: An autosomal recessive disorder resulting in severe hemorrhagic diathesis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19

Sequence similarities

Belongs to the serpin family.

Ontologies

Keywords
   Biological processAcute phase
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Sulfation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

blood vessel morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

collagen fibril organization

Inferred from sequence or structural similarity PubMed 17958745. Source: BHF-UCL

fibrinolysis

Traceable author statement. Source: Reactome

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of fibrinolysis

Inferred from direct assay PubMed 134998. Source: BHF-UCL

negative regulation of plasminogen activation

Inferred from direct assay PubMed 134998. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 20008146. Source: BHF-UCL

positive regulation of JNK cascade

Inferred from direct assay PubMed 20008146. Source: BHF-UCL

positive regulation of cell differentiation

Inferred from direct assay PubMed 20008146. Source: BHF-UCL

positive regulation of cell-cell adhesion mediated by cadherin

Traceable author statement PubMed 17203182. Source: BHF-UCL

positive regulation of collagen biosynthetic process

Inferred from direct assay PubMed 17958745. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of stress fiber assembly

Inferred from direct assay PubMed 20008146. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17958745. Source: BHF-UCL

positive regulation of transforming growth factor beta production

Inferred from direct assay PubMed 17958745PubMed 20008146. Source: BHF-UCL

regulation of blood vessel size by renin-angiotensin

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to organic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell surface

Inferred from direct assay PubMed 17958745. Source: BHF-UCL

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 6980881. Source: BHF-UCL

fibrinogen complex

Inferred from direct assay PubMed 17317851. Source: BHF-UCL

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionendopeptidase inhibitor activity

Traceable author statement Ref.1. Source: ProtInc

protease binding

Inferred from physical interaction Ref.16. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction PubMed 134998. Source: BHF-UCL

serine-type endopeptidase inhibitor activity

Non-traceable author statement PubMed 12878203. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08697-1)

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.
Isoform 2 (identifier: P08697-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-119: Missing.
     120-122: LAL → VQP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.8 Ref.9
Propeptide28 – 3912
PRO_0000032511
Chain40 – 491452Alpha-2-antiplasmin
PRO_0000032512

Sites

Site403 – 4042Reactive bond for plasmin
Site404 – 4052Reactive bond for chymotrypsin

Amino acid modifications

Modified residue4841Sulfotyrosine Ref.13
Glycosylation1261N-linked (GlcNAc...) Ref.17
Glycosylation2951N-linked (GlcNAc...) Ref.17
Glycosylation3091N-linked (GlcNAc...) Ref.17
Glycosylation3161N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 143 Ref.15
Cross-link41Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-322 in alpha-fibrinogen)

Natural variations

Alternative sequence56 – 11964Missing in isoform 2.
VSP_043833
Alternative sequence120 – 1223LAL → VQP in isoform 2.
VSP_043834
Natural variant21A → V. Ref.6
Corresponds to variant rs2070862 [ dbSNP | Ensembl ].
VAR_047951
Natural variant271A → V. Ref.19
VAR_013252
Natural variant331R → W. Ref.19
Corresponds to variant rs2070863 [ dbSNP | Ensembl ].
VAR_013253
Natural variant981A → G.
Corresponds to variant rs36021516 [ dbSNP | Ensembl ].
VAR_051956
Natural variant1761Missing in APLID; variant Okinawa; probably blocks intracellular transport of alpha-2-plasmin inhibitor. Ref.18
VAR_013254
Natural variant4111V → M in APLID. Ref.19
VAR_013255
Natural variant4341R → K. Ref.19
Corresponds to variant rs1057335 [ dbSNP | Ensembl ].
VAR_013256
Natural variant4511P → S.
Corresponds to variant rs57360598 [ dbSNP | Ensembl ].
VAR_061792

Experimental info

Sequence conflict491L → G AA sequence Ref.10
Sequence conflict1051N → D AA sequence Ref.10
Sequence conflict2891H → D in AAA35543. Ref.7
Sequence conflict4081S → G AA sequence Ref.10
Sequence conflict4551D → N AA sequence Ref.10

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1990. Version 3.
Checksum: 385A1C90E91A63CB

FASTA49154,566
        10         20         30         40         50         60 
MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL KLGNQEPGGQ 

        70         80         90        100        110        120 
TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL 

       130        140        150        160        170        180 
ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE 

       190        200        210        220        230        240 
QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF 

       250        260        270        280        290        300 
WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV 

       310        320        330        340        350        360 
LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF 

       370        380        390        400        410        420 
QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF 

       430        440        450        460        470        480 
EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM 

       490 
EEDYPQFGSP K 

« Hide

Isoform 2 [UniParc].

Checksum: 1A5190EC32B5350A
Show »

FASTA42747,907

References

« Hide 'large scale' references
[1]"Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence."
Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T.
J. Biochem. 102:1033-1041(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Organization of the human alpha 2-plasmin inhibitor gene."
Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.
Proc. Natl. Acad. Sci. U.S.A. 85:6836-6840(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
[3]Erratum
Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.
Proc. Natl. Acad. Sci. U.S.A. 86:1612-1613(1989)
[4]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Liver.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 VAL-2.
[7]"Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin)."
Holmes W.E., Nelles L., Lijnen H.R., Collen D.
J. Biol. Chem. 262:1659-1664(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-491 (ISOFORM 1).
[8]"Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma."
Bangert K., Johnsen A.H., Christensen U., Thorsen S.
Biochem. J. 291:623-625(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-58.
Tissue: Plasma.
[9]"Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence."
Christensen S., Sottrup-Jensen L.
FEBS Lett. 312:100-104(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-52.
Tissue: Plasma.
[10]"Amino-acid sequence of human alpha 2-antiplasmin."
Lijnen H.R., Holmes W.E., van Hoef B., Wiman B., Rodriguez H., Collen D.
Eur. J. Biochem. 166:565-574(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 40-491.
[11]"Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma."
Wiman B., Collen D.
Eur. J. Biochem. 78:19-26(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 40-43.
[12]"Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor deduced from that of cDNA."
Sumi Y., Nakamura Y., Aoki N., Sakai M., Muramatsu M.
J. Biochem. 100:1399-1402(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-491.
[13]"Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-antiplasmin."
Hortin G., Fok K.F., Toren P.C., Strauss A.W.
J. Biol. Chem. 262:3082-3085(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 481-491, SULFATION AT TYR-484.
[14]"Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites."
Potempa J., Shieh B.-H., Travis J.
Science 241:699-700(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: REACTIVE SITES.
[15]"Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties."
Christensen S., Valnickova Z., Thogersen I.B., Olsen E.H., Enghild J.J.
Biochem. J. 323:847-852(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND.
[16]"Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity."
Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.
Biochem. J. 390:231-242(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, HETERODIMER WITH TMPRSS7.
[17]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309.
Tissue: Plasma.
[18]"Hereditary alpha 2-plasmin inhibitor deficiency caused by a transport-deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137 by a trinucleotide deletion blocks intracellular transport."
Miura O., Sugahara Y., Aoki N.
J. Biol. Chem. 264:18213-18219(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APLID GLU-176 DEL.
[19]"A novel missense mutation in the human plasmin inhibitor (alpha2-antiplasmin) gene associated with a bleeding tendency."
Lind B., Thorsen S.
Br. J. Haematol. 107:317-322(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APLID MET-411, VARIANTS VAL-27; TRP-33 AND LYS-434.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00174 mRNA. Translation: BAA00124.1.
M20786 expand/collapse EMBL AC list , M20782, M20783, M20784, M20785 Genomic DNA. Translation: AAA51554.1.
AK303763 mRNA. Translation: BAG64729.1.
AC130343 Genomic DNA. No translation available.
BC031592 mRNA. Translation: AAH31592.1.
J02654 mRNA. Translation: AAA35543.1.
D00116 mRNA. Translation: BAA00070.1.
PIRITHUA2. A31402.
RefSeqNP_000925.2. NM_000934.3.
NP_001159392.1. NM_001165920.1.
NP_001159393.1. NM_001165921.1.
XP_005256758.1. XM_005256701.2.
UniGeneHs.159509.

3D structure databases

ProteinModelPortalP08697.
SMRP08697. Positions 31-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111360. 10 interactions.
IntActP08697. 2 interactions.
STRING9606.ENSP00000321853.

Chemistry

DrugBankDB00086. Streptokinase.

Protein family/group databases

MEROPSI04.023.

PTM databases

PhosphoSiteP08697.

Polymorphism databases

DMDM112907.

2D gel databases

SWISS-2DPAGEP08697.

Proteomic databases

PaxDbP08697.
PRIDEP08697.

Protocols and materials databases

DNASU5345.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324015; ENSP00000321853; ENSG00000167711. [P08697-1]
ENST00000382061; ENSP00000371493; ENSG00000167711. [P08697-1]
ENST00000450523; ENSP00000403877; ENSG00000167711. [P08697-2]
GeneID5345.
KEGGhsa:5345.
UCSCuc002ftk.1. human. [P08697-1]
uc010vqr.1. human. [P08697-2]

Organism-specific databases

CTD5345.
GeneCardsGC17P001593.
H-InvDBHIX0013407.
HGNCHGNC:9075. SERPINF2.
HPACAB024863.
HPA001885.
MIM262850. phenotype.
613168. gene.
neXtProtNX_P08697.
Orphanet79. Congenital alpha2 antiplasmin deficiency.
PharmGKBPA35522.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOGENOMHOG000231761.
HOVERGENHBG000043.
InParanoidP08697.
KOK03983.
OMARWFLLEQ.
PhylomeDBP08697.
TreeFamTF317350.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP08697.
BgeeP08697.
CleanExHS_SERPINF2.
GenevestigatorP08697.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSERPINF2. human.
GeneWikiAlpha_2-antiplasmin.
GenomeRNAi5345.
NextBio20714.
PMAP-CutDBP08697.
PROP08697.
SOURCESearch...

Entry information

Entry nameA2AP_HUMAN
AccessionPrimary (citable) accession number: P08697
Secondary accession number(s): B4E1B7 expand/collapse secondary AC list , Q8N5U7, Q9UCG2, Q9UCG3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM