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P10153

- RNAS2_HUMAN

UniProt

P10153 - RNAS2_HUMAN

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Protein

Non-secretory ribonuclease

Gene

RNASE2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities.2 Publications

Catalytic activityi

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei42 – 421Proton acceptor
Active sitei156 – 1561Proton donor

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. pancreatic ribonuclease activity Source: UniProtKB-EC
  3. ribonuclease activity Source: ProtInc

GO - Biological processi

  1. chemotaxis Source: UniProtKB
  2. RNA catabolic process Source: ProtInc
  3. RNA phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Chemotaxis

Names & Taxonomyi

Protein namesi
Recommended name:
Non-secretory ribonuclease (EC:3.1.27.5)
Alternative name(s):
Eosinophil-derived neurotoxin
RNase UpI-2
Ribonuclease 2
Short name:
RNase 2
Ribonuclease US
Gene namesi
Name:RNASE2
Synonyms:EDN, RNS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:10045. RNASE2.

Subcellular locationi

Lysosome Curated. Cytoplasmic granule
Note: Matrix of eosinophil's large specific granule.

GO - Cellular componenti

  1. extracellular region Source: ProtInc
  2. extracellular vesicular exosome Source: UniProtKB
  3. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27275 PublicationsAdd
BLAST
Chaini28 – 161134Non-secretory ribonucleasePRO_0000030874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341C-linked (Man)CAR_000004
Glycosylationi44 – 441N-linked (GlcNAc...)
Disulfide bondi50 ↔ 110
Modified residuei60 – 601Nitrated tyrosine1 Publication
Disulfide bondi64 ↔ 123
Disulfide bondi82 ↔ 138
Glycosylationi86 – 861N-linked (GlcNAc...)
Disulfide bondi89 ↔ 98
Glycosylationi92 – 921N-linked (GlcNAc...)
Glycosylationi111 – 1111N-linked (GlcNAc...)
Glycosylationi119 – 1191N-linked (GlcNAc...)

Post-translational modificationi

A particular signal processing and glycosylation pattern may differentiate the UpI2 RNase, found specifically in pregnant women urine, from other nonsecretory RNases.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

PaxDbiP10153.
PeptideAtlasiP10153.
PRIDEiP10153.

PTM databases

PhosphoSiteiP10153.
UniCarbKBiP10153.

Expressioni

Tissue specificityi

Liver, lung, spleen, leukocytes and body fluids.

Gene expression databases

BgeeiP10153.
CleanExiHS_RNASE2.
ExpressionAtlasiP10153. baseline and differential.
GenevestigatoriP10153.

Organism-specific databases

HPAiHPA044983.

Interactioni

Subunit structurei

Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur.3 Publications

Protein-protein interaction databases

BioGridi111965. 1 interaction.
STRINGi9606.ENSP00000303276.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 429
Beta strandi46 – 494
Helixi50 – 6112
Beta strandi66 – 738
Helixi75 – 828
Beta strandi98 – 1003
Beta strandi105 – 11410
Helixi120 – 1223
Beta strandi124 – 14017
Turni143 – 1453
Beta strandi151 – 16111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQVX-ray0.98A28-161[»]
1HI2X-ray1.60A28-161[»]
1HI3X-ray1.80A28-161[»]
1HI4X-ray1.80A28-161[»]
1HI5X-ray1.80A28-161[»]
1K2AX-ray1.00A26-160[»]
2BEXX-ray1.99C/D28-161[»]
2BZZX-ray0.98A28-161[»]
2C01X-ray1.24X28-161[»]
2C02X-ray2.00A28-161[»]
2C05X-ray1.86A28-161[»]
ProteinModelPortaliP10153.
SMRiP10153. Positions 26-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10153.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 695Substrate binding

Domaini

The N-terminal region is necessary for mediating chemotactic activity.

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39501.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiP10153.
KOiK01168.
OMAiRDPPQYP.
OrthoDBiEOG7KDFCP.
PhylomeDBiP10153.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10153 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC
60 70 80 90 100
TNAMQVINNY QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHH
110 120 130 140 150
SGSQVPLIHC NLTTPSPQNI SNCRYAQTPA NMFYIVACDN RDQRRDPPQY
160
PVVPVHLDRI I
Length:161
Mass (Da):18,354
Last modified:January 1, 1990 - v2
Checksum:i9406C4596CA69038
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371W → R AA sequence (PubMed:3926759)Curated
Sequence conflicti39 – 402ET → QE AA sequence (PubMed:3926759)Curated
Sequence conflicti46 – 461T → V AA sequence (PubMed:3926759)Curated
Sequence conflicti47 – 471S → T AA sequence (PubMed:3182786)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001H → Q.
Corresponds to variant rs8012891 [ dbSNP | Ensembl ].
VAR_059820
Natural varianti156 – 1561H → N Probably inactive. 1 Publication
Corresponds to variant rs146887874 [ dbSNP | Ensembl ].
VAR_013150

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30510 mRNA. Translation: AAC82505.1.
M28129 mRNA. Translation: AAA50284.1.
M24157 mRNA. Translation: AAA52337.1.
X16546 Genomic DNA. Translation: CAA34546.1.
AF294007 Genomic DNA. Translation: AAG31577.1.
AF294008 Genomic DNA. Translation: AAG31578.1.
AF294009 Genomic DNA. Translation: AAG31579.1.
AF294010 Genomic DNA. Translation: AAG31580.1.
AF294011 Genomic DNA. Translation: AAG31581.1.
AF294012 Genomic DNA. Translation: AAG31582.1.
AF294013 Genomic DNA. Translation: AAG31583.1.
AF294014 Genomic DNA. Translation: AAG31584.1.
AF294015 Genomic DNA. Translation: AAG31585.1.
X55987 Genomic DNA. Translation: CAA39459.1.
X55988 mRNA. Translation: CAA39460.1.
BC093678 mRNA. Translation: AAH93678.1.
BC093680 mRNA. Translation: AAH93680.1.
BC096059 mRNA. Translation: AAH96059.1.
CCDSiCCDS9561.1.
PIRiA35328. A33922.
RefSeqiNP_002925.1. NM_002934.2.
UniGeneiHs.728.

Genome annotation databases

EnsembliENST00000304625; ENSP00000303276; ENSG00000169385.
GeneIDi6036.
KEGGihsa:6036.
UCSCiuc001vyl.1. human.

Polymorphism databases

DMDMi133168.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30510 mRNA. Translation: AAC82505.1 .
M28129 mRNA. Translation: AAA50284.1 .
M24157 mRNA. Translation: AAA52337.1 .
X16546 Genomic DNA. Translation: CAA34546.1 .
AF294007 Genomic DNA. Translation: AAG31577.1 .
AF294008 Genomic DNA. Translation: AAG31578.1 .
AF294009 Genomic DNA. Translation: AAG31579.1 .
AF294010 Genomic DNA. Translation: AAG31580.1 .
AF294011 Genomic DNA. Translation: AAG31581.1 .
AF294012 Genomic DNA. Translation: AAG31582.1 .
AF294013 Genomic DNA. Translation: AAG31583.1 .
AF294014 Genomic DNA. Translation: AAG31584.1 .
AF294015 Genomic DNA. Translation: AAG31585.1 .
X55987 Genomic DNA. Translation: CAA39459.1 .
X55988 mRNA. Translation: CAA39460.1 .
BC093678 mRNA. Translation: AAH93678.1 .
BC093680 mRNA. Translation: AAH93680.1 .
BC096059 mRNA. Translation: AAH96059.1 .
CCDSi CCDS9561.1.
PIRi A35328. A33922.
RefSeqi NP_002925.1. NM_002934.2.
UniGenei Hs.728.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GQV X-ray 0.98 A 28-161 [» ]
1HI2 X-ray 1.60 A 28-161 [» ]
1HI3 X-ray 1.80 A 28-161 [» ]
1HI4 X-ray 1.80 A 28-161 [» ]
1HI5 X-ray 1.80 A 28-161 [» ]
1K2A X-ray 1.00 A 26-160 [» ]
2BEX X-ray 1.99 C/D 28-161 [» ]
2BZZ X-ray 0.98 A 28-161 [» ]
2C01 X-ray 1.24 X 28-161 [» ]
2C02 X-ray 2.00 A 28-161 [» ]
2C05 X-ray 1.86 A 28-161 [» ]
ProteinModelPortali P10153.
SMRi P10153. Positions 26-161.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111965. 1 interaction.
STRINGi 9606.ENSP00000303276.

Chemistry

BindingDBi P10153.
ChEMBLi CHEMBL5120.

PTM databases

PhosphoSitei P10153.
UniCarbKBi P10153.

Polymorphism databases

DMDMi 133168.

Proteomic databases

PaxDbi P10153.
PeptideAtlasi P10153.
PRIDEi P10153.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304625 ; ENSP00000303276 ; ENSG00000169385 .
GeneIDi 6036.
KEGGi hsa:6036.
UCSCi uc001vyl.1. human.

Organism-specific databases

CTDi 6036.
GeneCardsi GC14P021423.
HGNCi HGNC:10045. RNASE2.
HPAi HPA044983.
MIMi 131410. gene.
neXtProti NX_P10153.
PharmGKBi PA34413.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39501.
HOGENOMi HOG000276882.
HOVERGENi HBG008396.
InParanoidi P10153.
KOi K01168.
OMAi RDPPQYP.
OrthoDBi EOG7KDFCP.
PhylomeDBi P10153.
TreeFami TF333393.

Miscellaneous databases

EvolutionaryTracei P10153.
GeneWikii Eosinophil-derived_neurotoxin.
GenomeRNAii 6036.
NextBioi 23525.
PROi P10153.
SOURCEi Search...

Gene expression databases

Bgeei P10153.
CleanExi HS_RNASE2.
ExpressionAtlasi P10153. baseline and differential.
Genevestigatori P10153.

Family and domain databases

Gene3Di 3.10.130.10. 1 hit.
InterProi IPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view ]
PANTHERi PTHR11437. PTHR11437. 1 hit.
Pfami PF00074. RnaseA. 1 hit.
[Graphical view ]
PRINTSi PR00794. RIBONUCLEASE.
ProDomi PD000535. RNaseA. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00092. RNAse_Pc. 1 hit.
[Graphical view ]
SUPFAMi SSF54076. SSF54076. 1 hit.
PROSITEi PS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases."
    Hamann K.J., Barker R.L., Loegering D.A., Pease L.R., Gleich G.J.
    Gene 83:161-167(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases."
    Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R., Gleich G.J.
    J. Immunol. 143:952-955(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family."
    Rosenberg H.F., Tenen D.G., Ackerman S.J.
    Proc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily."
    Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T., Schad C.R., Pease L.R., Gleich G.J., Barker R.L.
    Genomics 7:535-546(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Sequence variation at two eosinophil-associated ribonuclease loci in humans."
    Zhang J., Rosenberg H.F.
    Genetics 156:1949-1958(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-156.
  6. Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.
    Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Colon and Leukemia.
  7. "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].
  8. Cited for: PROTEIN SEQUENCE OF 28-161.
  9. "Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease."
    Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J., McKean D.J.
    Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-82, FUNCTION.
  10. "Purification and properties of bovine kidney ribonucleases."
    Niwata Y., Ohgi K., Sanda A., Takizawa Y., Irie M.
    J. Biochem. 97:923-934(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-55.
  11. "Purification and characterization of a ribonuclease from human liver."
    Sorrentino S., Tucker G.K., Glitz D.G.
    J. Biol. Chem. 263:16125-16131(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-53.
    Tissue: Liver.
  12. "Characterization of a unique nonsecretory ribonuclease from urine of pregnant women."
    Sakakibara R., Hashida K., Kitahara T., Ishiguro M.
    J. Biochem. 111:325-330(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-43.
    Tissue: Urine.
  13. "Characterisation of UGP and its relationship with beta-core fragment."
    Kardana A., Bagshawe K.D., Coles B., Read D., Taylor M.
    Br. J. Cancer 67:686-692(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-45.
    Tissue: Urine.
  14. "New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us."
    Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J., Vliegenthart J.F.G.
    Biochemistry 33:13524-13530(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-34.
  15. "The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose."
    de Beer T., Vliegenthart J.F.G., Loeffler A., Hofsteenge J.
    Biochemistry 34:11785-11789(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF C-GLYCOSYLATED GROUP.
  16. "Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp."
    Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D., Hofsteenge J.
    Mol. Biol. Cell 9:301-309(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-34.
  17. "Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2)."
    Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.
    Biochemistry 42:1451-1459(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNH1.
  18. "Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells."
    Yang D., Rosenberg H.F., Chen Q., Dyer K.D., Kurosaka K., Oppenheim J.J.
    Blood 102:3396-3403(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CHEMOTAXIS.
  19. Cited for: NITRATION AT TYR-60.
  20. "X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83-A resolution."
    Mosimann S.C., Newton D.L., Youle R.J., James M.N.G.
    J. Mol. Biol. 260:540-552(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
  21. "Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN). High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors."
    Leonidas D.D., Boix E., Prill R., Suzuki M., Turton R., Minson K., Swaminathan G.J., Youle R.J., Acharya K.R.
    J. Biol. Chem. 276:15009-15017(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  22. "Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor."
    Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.
    J. Mol. Biol. 347:637-655(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 28-161 IN COMPLEX WITH RNH1, SUBUNIT.
  23. "Crystal structures of eosinophil-derived neurotoxin (EDN) in complex with the inhibitors 5'-ATP, Ap3A, Ap4A, and Ap5A."
    Baker M.D., Holloway D.E., Swaminathan G.J., Acharya K.R.
    Biochemistry 45:416-426(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 28-161 IN COMPLEX WITH ADP AND ATP.

Entry informationi

Entry nameiRNAS2_HUMAN
AccessioniPrimary (citable) accession number: P10153
Secondary accession number(s): Q52M39, Q9H2B7, Q9UCG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: October 29, 2014
This is version 165 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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