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Protein

Erythrocyte membrane protein band 4.2

Gene

EPB42

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

  • ATP binding Source: ProtInc
  • protein-glutamine gamma-glutamyltransferase activity Source: InterPro
  • structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

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 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:3381. EPB42.

Subcellular locationi

GO - Cellular componenti

  • cortical cytoskeleton Source: Ensembl
  • cytoskeleton Source: ProtInc
  • plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Spherocytosis 5 (SPH5)6 Publications

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

Disease descriptionSpherocytosis 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.

See also OMIM:612690
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.

Polymorphism and mutation databases

BioMutaiEPB42.
DMDMi215274164.

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 PKA1 Publication

Post-translational modificationi

Both cAMP-dependent kinase (CAPK) and another kinase present in the red-blood cells seem to be able to phosphorylate EPB42.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP16452.
PRIDEiP16452.

PTM databases

PhosphoSiteiP16452.

Expressioni

Gene expression databases

BgeeiP16452.
CleanExiHS_EPB42.
ExpressionAtlasiP16452. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG87163.
GeneTreeiENSGT00760000119108.
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. AlignAdd to basket

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

        10         20         30         40         50
MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR
60 70 80 90 100
AFLPALKKVA LTAQTGEQPS KINRTQATFP ISSLGDRKWW SAVVEERDAQ
110 120 130 140 150
SWTISVTTPA DAVIGHYSLL LQVSGRKQLL LGQFTLLFNP WNREDAVFLK
160 170 180 190 200
NEAQRMEYLL NQNGLIYLGT ADCIQAESWD FGQFEGDVID LSLRLLSKDK
210 220 230 240 250
QVEKWSQPVH VARVLGALLH FLKEQRVLPT PQTQATQEGA LLNKRRGSVP
260 270 280 290 300
ILRQWLTGRG RPVYDGQAWV LAAVACTVLR CLGIPARVVT TFASAQGTGG
310 320 330 340 350
RLLIDEYYNE EGLQNGEGQR GRIWIFQTST ECWMTRPALP QGYDGWQILH
360 370 380 390 400
PSAPNGGGVL GSCDLVPVRA VKEGTLGLTP AVSDLFAAIN ASCVVWKCCE
410 420 430 440 450
DGTLELTDSN TKYVGNNIST KGVGSDRCED ITQNYKYPEG SLQEKEVLER
460 470 480 490 500
VEKEKMEREK DNGIRPPSLE TASPLYLLLK APSSLPLRGD AQISVTLVNH
510 520 530 540 550
SEQEKAVQLA IGVQAVHYNG VLAAKLWRKK LHLTLSANLE KIITIGLFFS
560 570 580 590 600
NFERNPPENT FLRLTAMATH SESNLSCFAQ EDIAICRPHL AIKMPEKAEQ
610 620 630 640 650
YQPLTASVSL QNSLDAPMED CVISILGRGL IHRERSYRFR SVWPENTMCA
660 670 680 690
KFQFTPTHVG LQRLTVEVDC NMFQNLTNYK SVTVVAPELS A

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3501H → D in AAA74589 (PubMed:2052563).Curated
Sequence conflicti350 – 3501H → D in AAA52385 (PubMed:2052563).Curated
Sequence conflicti350 – 3501H → D in AAA35798 (PubMed:2300550).Curated
Sequence conflicti376 – 3761L → V in AAA74589 (PubMed:2052563).Curated
Sequence conflicti376 – 3761L → V in AAA52385 (PubMed:2052563).Curated
Sequence conflicti376 – 3761L → V in AAA35798 (PubMed:2300550).Curated

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. 2 PublicationsVSP_006416
Alternative sequencei324 – 39572Missing in isoform 3. 1 PublicationVSP_055340Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
ENST00000622454; ENSP00000481226; ENSG00000166947. [P16452-3]
GeneIDi2038.
KEGGihsa:2038.
UCSCiuc001zqz.4. human. [P16452-1]
uc001zrb.4. human. [P16452-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP16452.
SMRiP16452. Positions 5-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP16452.

Polymorphism and mutation databases

BioMutaiEPB42.
DMDMi215274164.

Proteomic databases

PaxDbiP16452.
PRIDEiP16452.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300215; ENSP00000300215; ENSG00000166947. [P16452-2]
ENST00000441366; ENSP00000396616; ENSG00000166947. [P16452-1]
ENST00000622454; ENSP00000481226; ENSG00000166947. [P16452-3]
GeneIDi2038.
KEGGihsa:2038.
UCSCiuc001zqz.4. human. [P16452-1]
uc001zrb.4. human. [P16452-2]

Organism-specific databases

CTDi2038.
GeneCardsiGC15M043398.
HGNCiHGNC:3381. EPB42.
HPAiHPA040261.
MIMi177070. gene.
612690. phenotype.
neXtProtiNX_P16452.
Orphaneti822. Hereditary spherocytosis.
PharmGKBiPA27814.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG87163.
GeneTreeiENSGT00760000119108.
HOGENOMiHOG000231695.
HOVERGENiHBG106048.
InParanoidiP16452.
OMAiSCFAQED.
OrthoDBiEOG7Z0JVS.
PhylomeDBiP16452.
TreeFamiTF324278.

Miscellaneous databases

GeneWikiiProtein_4.2.
GenomeRNAii2038.
NextBioi8277.
PROiP16452.
SOURCEiSearch...

Gene expression databases

BgeeiP16452.
CleanExiHS_EPB42.
ExpressionAtlasiP16452. baseline and differential.
GenevestigatoriP16452.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 162 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

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.