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P16452

- EPB42_HUMAN

UniProt

P16452 - EPB42_HUMAN

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Protein

Erythrocyte membrane protein band 4.2

Gene
EPB42, E42P
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.

GO - Molecular functioni

  1. ATP binding Source: ProtInc
  2. protein binding Source: IntAct
  3. protein-glutamine gamma-glutamyltransferase activity Source: InterPro
  4. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. cell morphogenesis Source: Ensembl
  2. erythrocyte maturation Source: UniProtKB-KW
  3. hemoglobin metabolic process Source: Ensembl
  4. iron ion homeostasis Source: Ensembl
  5. peptide cross-linking Source: InterPro
  6. regulation of cell shape Source: UniProtKB-KW
  7. spleen development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell shape, Erythrocyte maturation

Names & Taxonomyi

Protein namesi
Recommended name:
Erythrocyte membrane protein band 4.2
Short name:
Erythrocyte protein 4.2
Short name:
P4.2
Gene namesi
Name:EPB42
Synonyms:E42P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:3381. EPB42.

Subcellular locationi

Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton
Note: Cytoplasmic surface of erythrocyte membranes.

GO - Cellular componenti

  1. cortical cytoskeleton Source: Ensembl
  2. cytoskeleton Source: ProtInc
  3. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Spherocytosis 5 (SPH5) [MIM:612690]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Absence of band 4.2 associated with spur or target erythrocytes has also been reported.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121A → T in SPH5; Nippon/Fukuoka. 4 Publications
Corresponds to variant rs28933988 [ dbSNP | Ensembl ].
VAR_007482
Natural varianti145 – 1451D → Y in SPH5; Komatsu. 1 Publication
VAR_058099
Natural varianti280 – 2801R → Q in SPH5; Tozeur. 1 Publication
VAR_012268
Natural varianti287 – 2871R → C in SPH5; Shiga. 1 Publication
VAR_058100

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MIMi612690. phenotype.
Orphaneti822. Hereditary spherocytosis.
PharmGKBiPA27814.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 691690Erythrocyte membrane protein band 4.2PRO_0000213720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei248 – 2481Phosphoserine; by PKA Inferred

Post-translational modificationi

Both cAMP-dependent kinase (CAPK) and another kinase present in the red-blood cells seem to be able to phosphorylate EPB42.

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP16452.
PRIDEiP16452.

PTM databases

PhosphoSiteiP16452.

Expressioni

Gene expression databases

ArrayExpressiP16452.
BgeeiP16452.
CleanExiHS_EPB42.
GenevestigatoriP16452.

Organism-specific databases

HPAiHPA040261.

Interactioni

Subunit structurei

Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band 3 anion transport protein.

Binary interactionsi

WithEntry#Exp.IntActNotes
SPINK7P580623EBI-1182496,EBI-1182445

Protein-protein interaction databases

BioGridi108352. 6 interactions.
IntActiP16452. 3 interactions.
STRINGi9606.ENSP00000300215.

Structurei

3D structure databases

ProteinModelPortaliP16452.
SMRiP16452. Positions 5-689.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 399Band 3 binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG87163.
HOGENOMiHOG000231695.
HOVERGENiHBG106048.
InParanoidiP16452.
OMAiSCFAQED.
OrthoDBiEOG7Z0JVS.
PhylomeDBiP16452.
TreeFamiTF324278.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Short (identifier: P16452-1) [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

MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR    50
AFLPALKKVA LTAQTGEQPS KINRTQATFP ISSLGDRKWW SAVVEERDAQ 100
SWTISVTTPA DAVIGHYSLL LQVSGRKQLL LGQFTLLFNP WNREDAVFLK 150
NEAQRMEYLL NQNGLIYLGT ADCIQAESWD FGQFEGDVID LSLRLLSKDK 200
QVEKWSQPVH VARVLGALLH FLKEQRVLPT PQTQATQEGA LLNKRRGSVP 250
ILRQWLTGRG RPVYDGQAWV LAAVACTVLR CLGIPARVVT TFASAQGTGG 300
RLLIDEYYNE EGLQNGEGQR GRIWIFQTST ECWMTRPALP QGYDGWQILH 350
PSAPNGGGVL GSCDLVPVRA VKEGTLGLTP AVSDLFAAIN ASCVVWKCCE 400
DGTLELTDSN TKYVGNNIST KGVGSDRCED ITQNYKYPEG SLQEKEVLER 450
VEKEKMEREK DNGIRPPSLE TASPLYLLLK APSSLPLRGD AQISVTLVNH 500
SEQEKAVQLA IGVQAVHYNG VLAAKLWRKK LHLTLSANLE KIITIGLFFS 550
NFERNPPENT FLRLTAMATH SESNLSCFAQ EDIAICRPHL AIKMPEKAEQ 600
YQPLTASVSL QNSLDAPMED CVISILGRGL IHRERSYRFR SVWPENTMCA 650
KFQFTPTHVG LQRLTVEVDC NMFQNLTNYK SVTVVAPELS A 691

Note: Major isoform.

Length:691
Mass (Da):77,009
Last modified:November 25, 2008 - v3
Checksum:i38225C311E478580
GO
Isoform Long (identifier: P16452-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-3: Q → QGEPSQRSTGLAGLYAAPAASPVFIKGSGMD

Show »
Length:721
Mass (Da):79,927
Checksum:iA1C85B41298A93C0
GO
Isoform 3 (identifier: P16452-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-395: Missing.

Note: No experimental confirmation available.

Show »
Length:619
Mass (Da):69,455
Checksum:i640A1E12CC4ED420
GO

Sequence cautioni

The sequence AAA36401.1 differs from that shown. Reason: Frameshift at positions 335 and 340.
The sequence AAA36402.1 differs from that shown. Reason: Frameshift at positions 335 and 340.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121A → T in SPH5; Nippon/Fukuoka. 4 Publications
Corresponds to variant rs28933988 [ dbSNP | Ensembl ].
VAR_007482
Natural varianti145 – 1451D → Y in SPH5; Komatsu. 1 Publication
VAR_058099
Natural varianti280 – 2801R → Q in SPH5; Tozeur. 1 Publication
VAR_012268
Natural varianti287 – 2871R → C in SPH5; Shiga. 1 Publication
VAR_058100

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3 – 31Q → QGEPSQRSTGLAGLYAAPAA SPVFIKGSGMD in isoform Long. VSP_006416
Alternative sequencei324 – 39572Missing in isoform 3. VSP_055340Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3501H → D in AAA74589. 1 Publication
Sequence conflicti350 – 3501H → D in AAA52385. 1 Publication
Sequence conflicti350 – 3501H → D in AAA35798. 1 Publication
Sequence conflicti376 – 3761L → V in AAA74589. 1 Publication
Sequence conflicti376 – 3761L → V in AAA52385. 1 Publication
Sequence conflicti376 – 3761L → V in AAA35798. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60298 mRNA. Translation: AAA74589.1.
L06519
, L06447, L06448, L06449, L06450, L06511, L06512, L06513, L06515, L06516, L06517, L06518 Genomic DNA. Translation: AAA52385.1.
M29399 mRNA. Translation: AAA35798.1.
M30647 mRNA. Translation: AAA36401.1. Frameshift.
M30646 mRNA. Translation: AAA36402.1. Frameshift.
AC068724 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92591.1.
BC096093 mRNA. Translation: AAH96093.1.
BC096094 mRNA. Translation: AAH96094.1.
BC099627 mRNA. Translation: AAH99627.1.
CCDSiCCDS10093.1. [P16452-2]
CCDS45249.1. [P16452-1]
PIRiA39707.
RefSeqiNP_000110.2. NM_000119.2. [P16452-2]
NP_001107606.1. NM_001114134.1. [P16452-1]
UniGeneiHs.368642.

Genome annotation databases

EnsembliENST00000300215; ENSP00000300215; ENSG00000166947. [P16452-2]
ENST00000441366; ENSP00000396616; ENSG00000166947. [P16452-1]
GeneIDi2038.
KEGGihsa:2038.
UCSCiuc001zqz.4. human. [P16452-1]
uc001zrb.4. human. [P16452-2]

Polymorphism databases

DMDMi215274164.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60298 mRNA. Translation: AAA74589.1 .
L06519
, L06447 , L06448 , L06449 , L06450 , L06511 , L06512 , L06513 , L06515 , L06516 , L06517 , L06518 Genomic DNA. Translation: AAA52385.1 .
M29399 mRNA. Translation: AAA35798.1 .
M30647 mRNA. Translation: AAA36401.1 . Frameshift.
M30646 mRNA. Translation: AAA36402.1 . Frameshift.
AC068724 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92591.1 .
BC096093 mRNA. Translation: AAH96093.1 .
BC096094 mRNA. Translation: AAH96094.1 .
BC099627 mRNA. Translation: AAH99627.1 .
CCDSi CCDS10093.1. [P16452-2 ]
CCDS45249.1. [P16452-1 ]
PIRi A39707.
RefSeqi NP_000110.2. NM_000119.2. [P16452-2 ]
NP_001107606.1. NM_001114134.1. [P16452-1 ]
UniGenei Hs.368642.

3D structure databases

ProteinModelPortali P16452.
SMRi P16452. Positions 5-689.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108352. 6 interactions.
IntActi P16452. 3 interactions.
STRINGi 9606.ENSP00000300215.

PTM databases

PhosphoSitei P16452.

Polymorphism databases

DMDMi 215274164.

Proteomic databases

PaxDbi P16452.
PRIDEi P16452.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300215 ; ENSP00000300215 ; ENSG00000166947 . [P16452-2 ]
ENST00000441366 ; ENSP00000396616 ; ENSG00000166947 . [P16452-1 ]
GeneIDi 2038.
KEGGi hsa:2038.
UCSCi uc001zqz.4. human. [P16452-1 ]
uc001zrb.4. human. [P16452-2 ]

Organism-specific databases

CTDi 2038.
GeneCardsi GC15M043398.
HGNCi HGNC:3381. EPB42.
HPAi HPA040261.
MIMi 177070. gene.
612690. phenotype.
neXtProti NX_P16452.
Orphaneti 822. Hereditary spherocytosis.
PharmGKBi PA27814.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG87163.
HOGENOMi HOG000231695.
HOVERGENi HBG106048.
InParanoidi P16452.
OMAi SCFAQED.
OrthoDBi EOG7Z0JVS.
PhylomeDBi P16452.
TreeFami TF324278.

Miscellaneous databases

GeneWikii Protein_4.2.
GenomeRNAii 2038.
NextBioi 8277.
PROi P16452.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16452.
Bgeei P16452.
CleanExi HS_EPB42.
Genevestigatori P16452.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProi IPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view ]
PANTHERi PTHR11590. PTHR11590. 1 hit.
Pfami PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
SMARTi SM00460. TGc. 1 hit.
[Graphical view ]
SUPFAMi SSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII."
    Korsgren C., Cohen C.M.
    Proc. Natl. Acad. Sci. U.S.A. 88:4840-4844(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Tissue: Reticulocyte.
  2. "Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2."
    Korsgren C., Lawler J., Lambert S., Speicher D., Cohen C.M.
    Proc. Natl. Acad. Sci. U.S.A. 87:613-617(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE (ISOFORM SHORT).
    Tissue: Reticulocyte.
  3. "Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane."
    Sung L.A., Chien S., Chang L.-S., Lambert K., Bliss S.A., Bouhassira E.E., Nagel R.L., Schwartz R.S., Rybicki A.C.
    Proc. Natl. Acad. Sci. U.S.A. 87:955-959(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    Tissue: Reticulocyte.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] (ISOFORMS SHORT AND 3).
  7. "Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated."
    Risinger M.A., Dotimas E.M., Cohen C.M.
    J. Biol. Chem. 267:5680-5685(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  8. "Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2)."
    Dotimas E., Speicher D.W., Guptaroy B., Cohen C.M.
    Biochim. Biophys. Acta 1148:19-29(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-248.
  9. "An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2 Nippon)."
    Bouhassira E.E., Schwartz R.S., Yawata Y., Ata K., Kanzaki A., Qiu J.J.-H., Nagel R.L., Rybicki A.C.
    Blood 79:1846-1854(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPH5 THR-112.
  10. "A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka)."
    Takaoka Y., Ideguchi H., Matsuda M., Sakamoto N., Takeuchi T., Fukumaki Y.
    Br. J. Haematol. 88:527-533(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPH5 THR-112.
  11. "A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia."
    Hayette S., Morle L., Bozon M., Ghanem A., Risinger M., Korsgren C., Tanner M.J.A., Fattoum S., Cohen C.M., Delaunay J.
    Br. J. Haematol. 89:762-770(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPH5 GLN-280.
  12. "Band 4.2 Shiga: 317 CGC-->TGC in compound heterozygotes with 142 GCT-->ACT results in band 4.2 deficiency and microspherocytosis."
    Kanzaki A., Yasunaga M., Okamoto N., Inoue T., Yawata A., Wada H., Andoh A., Hodohara K., Fujiyama Y., Bamba T., Harano T., Harano K., Yawata Y.
    Br. J. Haematol. 91:333-340(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SPH5 THR-112 AND CYS-287.
  13. "Band 4.2 Komatsu: 523 GAT-->TAT (175 Asp-->Tyr) in exon 4 of the band 4.2 gene associated with total deficiency of band 4.2, hemolytic anemia with ovalostomatocytosis and marked disruption of the cytoskeletal network."
    Kanzaki A., Yawata Y., Yawata A., Inoue T., Okamoto N., Wada H., Harano T., Harano K., Wilmotte R., Hayette S., Nakamura Y., Niki T., Kawamura Y., Nakamura S., Matsuda T.
    Int. J. Hematol. 61:165-178(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPH5 TYR-145.
  14. "4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis."
    Perrotta S., Iolascon A., Polito R., d'Urzo G., Conte M.L., Miraglia del Giudice E.
    Haematologica 84:660-662(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPH5 THR-112.

Entry informationi

Entry nameiEPB42_HUMAN
AccessioniPrimary (citable) accession number: P16452
Secondary accession number(s): Q4KKX0, Q4VB97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 158 of the entry and version 3 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

The substitution of an Ala for a Cys in the active site may be responsible for the lack of transglutaminase activity of band 4.2.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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