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P48200

- IREB2_HUMAN

UniProt

P48200 - IREB2_HUMAN

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Protein
Iron-responsive element-binding protein 2
Gene
IREB2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.1 Publication

Cofactori

Binds 1 4Fe-4S cluster per subunit By similarity. 4Fe-4S-binding affects RNA-binding activity, thereby inhibiting activity of the protein By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi512 – 5121Iron-sulfur (4Fe-4S) By similarity
Metal bindingi578 – 5781Iron-sulfur (4Fe-4S) By similarity
Metal bindingi581 – 5811Iron-sulfur (4Fe-4S) By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB
  3. iron-responsive element binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular iron ion homeostasis Source: Ensembl
  3. cellular response to hypoxia Source: Ensembl
  4. erythrocyte homeostasis Source: Ensembl
  5. intestinal absorption Source: Ensembl
  6. iron ion transport Source: UniProtKB
  7. osteoclast differentiation Source: Ensembl
  8. post-embryonic development Source: Ensembl
  9. protoporphyrinogen IX biosynthetic process Source: Ensembl
  10. regulation of translation Source: Ensembl
  11. response to iron(II) ion Source: Ensembl
  12. response to retinoic acid Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Iron-responsive element-binding protein 2
Short name:
IRE-BP 2
Alternative name(s):
Iron regulatory protein 2
Short name:
IRP2
Gene namesi
Name:IREB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:6115. IREB2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Ensembl
  3. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29914.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 963963Iron-responsive element-binding protein 2
PRO_0000076684Add
BLAST

Post-translational modificationi

Ubiquitinated and degraded by the proteasome in presence of high level of iron and oxygen. Ubiquitinated by a SCF complex containing FBXL5. Upon iron and oxygen depletion FBXL5 is degraded, preventing ubiquitination and allowing its RNA-binding activity.3 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP48200.
PaxDbiP48200.
PRIDEiP48200.

PTM databases

PhosphoSiteiP48200.

Expressioni

Gene expression databases

ArrayExpressiP48200.
BgeeiP48200.
CleanExiHS_IREB2.
GenevestigatoriP48200.

Organism-specific databases

HPAiCAB032885.

Interactioni

Subunit structurei

Interacts with RBCK1 isoform 1 and isoform 2 only in iron-rich conditions. Interacts (when associated with the 4Fe-4S) with FBXL5.3 Publications

Protein-protein interaction databases

BioGridi109866. 12 interactions.
IntActiP48200. 2 interactions.
STRINGi9606.ENSP00000258886.

Structurei

3D structure databases

ProteinModelPortaliP48200.
SMRiP48200. Positions 10-129, 220-963.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1048.
HOGENOMiHOG000025704.
HOVERGENiHBG052147.
InParanoidiP48200.
OMAiPCRGQTT.
OrthoDBiEOG7CG6Z7.
PhylomeDBiP48200.
TreeFamiTF313476.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 4 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR006249. Aconitase/Fe_reg_2.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR029755. IRE-BP2.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF31. PTHR11670:SF31. 1 hit.
PfamiPF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 2 hits.
TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48200-1 [UniParc]FASTAAdd to Basket

« Hide

MDAPKAGYAF EYLIETLNDS SHKKFFDVSK LGTKYDVLPY SIRVLLEAAV    50
RNCDGFLMKK EDVMNILDWK TKQSNVEVPF FPARVLLQDF TGIPAMVDFA 100
AMREAVKTLG GDPEKVHPAC PTDLTVDHSL QIDFSKCAIQ NAPNPGGGDL 150
QKAGKLSPVK VQPKKLPCRG QTTCRGSCDS GELGRNSGTF SSQIENTPIL 200
CPFHLQPVPE PETVLKNQEV EFGRNRERLQ FFKWSSRVFK NVAVIPPGTG 250
MAHQINLEYL SRVVFEEKDL LFPDSVVGTD SHITMVNGLG ILGWGVGGIE 300
TEAVMLGLPV SLTLPEVVGC ELTGSSNPFV TSIDVVLGIT KHLRQVGVAG 350
KFVEFFGSGV SQLSIVDRTT IANMCPEYGA ILSFFPVDNV TLKHLEHTGF 400
SKAKLESMET YLKAVKLFRN DQNSSGEPEY SQVIQINLNS IVPSVSGPKR 450
PQDRVAVTDM KSDFQACLNE KVGFKGFQIA AEKQKDIVSI HYEGSEYKLS 500
HGSVVIAAVI SCTNNCNPSV MLAAGLLAKK AVEAGLRVKP YIRTSLSPGS 550
GMVTHYLSSS GVLPYLSKLG FEIVGYGCSI CVGNTAPLSD AVLNAVKQGD 600
LVTCGILSGN KNFEGRLCDC VRANYLASPP LVVAYAIAGT VNIDFQTEPL 650
GTDPTGKNIY LHDIWPSREE VHRVEEEHVI LSMFKALKDK IEMGNKRWNS 700
LEAPDSVLFP WDLKSTYIRC PSFFDKLTKE PIALQAIENA HVLLYLGDSV 750
TTDHISPAGS IARNSAAAKY LTNRGLTPRE FNSYGARRGN DAVMTRGTFA 800
NIKLFNKFIG KPAPKTIHFP SGQTLDVFEA AELYQKEGIP LIILAGKKYG 850
SGNSRDWAAK GPYLLGVKAV LAESYEKIHK DHLIGIGIAP LQFLPGENAD 900
SLGLSGRETF SLTFPEELSP GITLNIQTST GKVFSVIASF EDDVEITLYK 950
HGGLLNFVAR KFS 963
Length:963
Mass (Da):105,045
Last modified:October 5, 2010 - v3
Checksum:iF3585B6BEA8DC9CA
GO

Sequence cautioni

The sequence AAA79926.1 differs from that shown. Reason: Frameshift at positions 605 and 611.
The sequence BAD92640.1 differs from that shown. Reason: Frameshift at position 727.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti159 – 1591V → L.8 Publications
Corresponds to variant rs2958720 [ dbSNP | Ensembl ].
VAR_058409
Natural varianti580 – 5801I → T.7 Publications
Corresponds to variant rs2230940 [ dbSNP | Ensembl ].
VAR_058410

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951E → G in BAF85681. 1 Publication
Sequence conflicti239 – 2391F → L in AAA69901. 1 Publication
Sequence conflicti239 – 2391F → L in AAA79926. 1 Publication
Sequence conflicti452 – 4521Q → R in AAA79926. 1 Publication
Sequence conflicti458 – 4581T → P in BAF85681. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58511 mRNA. Translation: AAA69901.1.
AK292992 mRNA. Translation: BAF85681.1.
AB209403 mRNA. Translation: BAD92640.1. Frameshift.
DQ496102 Genomic DNA. Translation: ABF47091.1.
AC011270 Genomic DNA. No translation available.
AC027228 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99169.1.
BC117481 mRNA. Translation: AAI17482.1.
BC117483 mRNA. Translation: AAI17484.1.
U20180 mRNA. Translation: AAA79926.1. Frameshift.
AL133439 mRNA. Translation: CAB62825.1.
CCDSiCCDS10302.1.
PIRiB57238.
RefSeqiNP_004127.1. NM_004136.2.
UniGeneiHs.436031.

Genome annotation databases

EnsembliENST00000258886; ENSP00000258886; ENSG00000136381.
GeneIDi3658.
KEGGihsa:3658.
UCSCiuc010unb.1. human.

Polymorphism databases

DMDMi308153591.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58511 mRNA. Translation: AAA69901.1 .
AK292992 mRNA. Translation: BAF85681.1 .
AB209403 mRNA. Translation: BAD92640.1 . Frameshift.
DQ496102 Genomic DNA. Translation: ABF47091.1 .
AC011270 Genomic DNA. No translation available.
AC027228 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99169.1 .
BC117481 mRNA. Translation: AAI17482.1 .
BC117483 mRNA. Translation: AAI17484.1 .
U20180 mRNA. Translation: AAA79926.1 . Frameshift.
AL133439 mRNA. Translation: CAB62825.1 .
CCDSi CCDS10302.1.
PIRi B57238.
RefSeqi NP_004127.1. NM_004136.2.
UniGenei Hs.436031.

3D structure databases

ProteinModelPortali P48200.
SMRi P48200. Positions 10-129, 220-963.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109866. 12 interactions.
IntActi P48200. 2 interactions.
STRINGi 9606.ENSP00000258886.

PTM databases

PhosphoSitei P48200.

Polymorphism databases

DMDMi 308153591.

Proteomic databases

MaxQBi P48200.
PaxDbi P48200.
PRIDEi P48200.

Protocols and materials databases

DNASUi 3658.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258886 ; ENSP00000258886 ; ENSG00000136381 .
GeneIDi 3658.
KEGGi hsa:3658.
UCSCi uc010unb.1. human.

Organism-specific databases

CTDi 3658.
GeneCardsi GC15P078730.
HGNCi HGNC:6115. IREB2.
HPAi CAB032885.
MIMi 147582. gene.
neXtProti NX_P48200.
PharmGKBi PA29914.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1048.
HOGENOMi HOG000025704.
HOVERGENi HBG052147.
InParanoidi P48200.
OMAi PCRGQTT.
OrthoDBi EOG7CG6Z7.
PhylomeDBi P48200.
TreeFami TF313476.

Miscellaneous databases

ChiTaRSi IREB2. human.
GenomeRNAii 3658.
NextBioi 14307.
PROi P48200.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48200.
Bgeei P48200.
CleanExi HS_IREB2.
Genevestigatori P48200.

Family and domain databases

Gene3Di 3.20.19.10. 1 hit.
3.30.499.10. 4 hits.
3.40.1060.10. 1 hit.
InterProi IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR006249. Aconitase/Fe_reg_2.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR029755. IRE-BP2.
[Graphical view ]
PANTHERi PTHR11670. PTHR11670. 1 hit.
PTHR11670:SF31. PTHR11670:SF31. 1 hit.
Pfami PF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view ]
PRINTSi PR00415. ACONITASE.
SUPFAMi SSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 2 hits.
TIGRFAMsi TIGR01341. aconitase_1. 1 hit.
PROSITEi PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation."
    Samaniego F., Chin J., Iwai K., Rouault T.A., Klausner R.D.
    J. Biol. Chem. 269:30904-30910(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, RNA-BINDING, VARIANTS LEU-159 AND THR-580.
  2. "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], VARIANTS LEU-159 AND THR-580.
    Tissue: Trachea.
  3. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-159 AND THR-580.
    Tissue: Brain.
  4. NIEHS SNPs program
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-159 AND THR-580.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LEU-159 AND THR-580.
  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], VARIANTS LEU-159 AND THR-580.
    Tissue: Brain.
  8. "Cloning of the cDNA encoding an RNA regulatory protein -- the human iron-responsive element-binding protein."
    Rouault T.A., Tang C.K., Kaptain S., Burgess W.H., Haile D.J., Samaniego F., McBride O.W., Harford J.B., Klausner R.D.
    Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-159 AND THR-580.
  9. "Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels."
    Guo B., Brown F.M., Phillips J.D., Yu Y., Leibold E.A.
    J. Biol. Chem. 270:16529-16535(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-963.
    Tissue: Brain.
  10. The European IMAGE consortium
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 847-963.
  11. "Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2."
    Yamanaka K., Ishikawa H., Megumi Y., Tokunaga F., Kanie M., Rouault T.A., Morishima I., Minato N., Ishimori K., Iwai K.
    Nat. Cell Biol. 5:336-340(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH RBCK1.
  12. Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
  13. "An E3 ligase possessing an iron responsive hemerythrin domain is a regulator of iron homeostasis."
    Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N., Li Q., Grishin N.V., Bruick R.K.
    Science 326:722-726(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiIREB2_HUMAN
AccessioniPrimary (citable) accession number: P48200
Secondary accession number(s): A8KAC7
, Q13095, Q1HE21, Q59FQ7, Q9UF17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 128 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

Keywords - Technical termi

Complete proteome, 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

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