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P78318

- IGBP1_HUMAN

UniProt

P78318 - IGBP1_HUMAN

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Protein

Immunoglobulin-binding protein 1

Gene
IGBP1, IBP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei255 – 2562Cleavage; by calpain

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein phosphatase type 2A regulator activity Source: UniProtKB

GO - Biological processi

  1. B cell activation Source: UniProtKB-KW
  2. negative regulation of apoptotic signaling pathway Source: Ensembl
  3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  4. negative regulation of protein dephosphorylation Source: Ensembl
  5. negative regulation of stress-activated MAPK cascade Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. positive regulation of dephosphorylation Source: Ensembl
  8. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  9. regulation of microtubule-based movement Source: UniProtKB
  10. response to interleukin-1 Source: UniProtKB
  11. response to tumor necrosis factor Source: UniProtKB
  12. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

B-cell activation

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin-binding protein 1
Alternative name(s):
B-cell signal transduction molecule alpha 4
Short name:
Protein alpha-4
CD79a-binding protein 1
Protein phosphatase 2/4/6 regulatory subunit
Renal carcinoma antigen NY-REN-16
Gene namesi
Name:IGBP1
Synonyms:IBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:5461. IGBP1.

Subcellular locationi

Cytoplasm Reviewed prediction

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, 28 (MRXS28) [MIM:300472]: A mental retardation syndrome characterized by agenesis of the corpus callosum, coloboma of the iris and optic nerve, severe retrognathia, and intellectual deficit. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi155 – 1551R → E: Abolishes interaction with PPP2CA. 1 Publication
Mutagenesisi158 – 1581K → D: Abolishes interaction with PPP2CA. 1 Publication
Mutagenesisi162 – 1621Y → D: Abolishes interaction with PPP2CA. 1 Publication
Mutagenesisi214 – 2141E → R: Abolishes interaction with PPP2CA. 1 Publication

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi300472. phenotype.
Orphaneti52055. Agenesis of the corpus callosum - intellectual disability - coloboma - micrognathia.
PharmGKBiPA29694.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 339338Immunoglobulin-binding protein 1PRO_0000218618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei241 – 2411N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated By similarity.
Monoubiquitination by MID1 triggers calpain-mediated cleavage and switches IGBP1 activity from protective to destructive.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP78318.
PaxDbiP78318.
PeptideAtlasiP78318.
PRIDEiP78318.

PTM databases

PhosphoSiteiP78318.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels in heart, skeletal muscle and pancreas.

Gene expression databases

BgeeiP78318.
CleanExiHS_IGBP1.
GenevestigatoriP78318.

Organism-specific databases

HPAiCAB034139.
HPA000634.
HPA001004.

Interactioni

Subunit structurei

Interacts with partially folded PPP2CA, but not with the fully active protein. Interacts with PPP2CB, and with PP4 and PP6. Interacts with MID1 and MID2. Interacts with ubiquitin.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP2CAP6777510EBI-1055954,EBI-712311
PPP2CBP627143EBI-1055954,EBI-1044367
PPP4CP605107EBI-1055954,EBI-1046072
PPP6CO0074310EBI-1055954,EBI-359751
TIPRLO756632EBI-1055954,EBI-1054735

Protein-protein interaction databases

BioGridi109698. 113 interactions.
IntActiP78318. 20 interactions.
MINTiMINT-3022988.
STRINGi9606.ENSP00000348784.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54
Helixi12 – 2716
Helixi36 – 5924
Helixi68 – 703
Turni73 – 753
Helixi76 – 805
Helixi81 – 9010
Helixi95 – 973
Helixi98 – 11821
Beta strandi143 – 1453
Helixi156 – 18025
Helixi186 – 21934

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IYPX-ray2.80A2-234[»]
ProteinModelPortaliP78318.
SMRiP78318. Positions 1-221.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati46 – 6015UIMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 202105Interaction with PPP2CAAdd
BLAST
Regioni225 – 29066Interaction with MID1Add
BLAST

Domaini

The UIM domain is required for protective effect on PP2A By similarity.

Sequence similaritiesi

Belongs to the IGBP1/TAP42 family.

Phylogenomic databases

eggNOGiNOG332001.
HOGENOMiHOG000038526.
HOVERGENiHBG052090.
InParanoidiP78318.
KOiK17606.
OMAiGSRIIQD.
OrthoDBiEOG7992R2.
PhylomeDBiP78318.
TreeFamiTF313433.

Family and domain databases

InterProiIPR007304. TAP42-like.
[Graphical view]
PANTHERiPTHR10933. PTHR10933. 1 hit.
PfamiPF04177. TAP42. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P78318-1 [UniParc]FASTAAdd to Basket

« Hide

MAAEDELQLP RLPELFETGR QLLDEVEVAT EPAGSRIVQE KVFKGLDLLE    50
KAAEMLSQLD LFSRNEDLEE IASTDLKYLL VPAFQGALTM KQVNPSKRLD 100
HLQRAREHFI NYLTQCHCYH VAEFELPKTM NNSAENHTAN SSMAYPSLVA 150
MASQRQAKIQ RYKQKKELEH RLSAMKSAVE SGQADDERVR EYYLLHLQRW 200
IDISLEEIES IDQEIKILRE RDSSREASTS NSSRQERPPV KPFILTRNMA 250
QAKVFGAGYP SLPTMTVSDW YEQHRKYGAL PDQGIAKAAP EEFRKAAQQQ 300
EEQEEKEEED DEQTLHRARE WDDWKDTHPR GYGNRQNMG 339
Length:339
Mass (Da):39,222
Last modified:May 1, 1997 - v1
Checksum:iBB00A116EB45273A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201R → K.
Corresponds to variant rs6625580 [ dbSNP | Ensembl ].
VAR_049570

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08915 mRNA. Translation: CAA70119.1.
BT006736 mRNA. Translation: AAP35382.1.
AL158141, AL139111 Genomic DNA. Translation: CAD13488.2.
BC004137 mRNA. Translation: AAH04137.1.
CCDSiCCDS14396.1.
RefSeqiNP_001542.1. NM_001551.2.
UniGeneiHs.496267.

Genome annotation databases

EnsembliENST00000342206; ENSP00000363661; ENSG00000089289.
ENST00000356413; ENSP00000348784; ENSG00000089289.
GeneIDi3476.
KEGGihsa:3476.
UCSCiuc004dxv.3. human.

Polymorphism databases

DMDMi14285501.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08915 mRNA. Translation: CAA70119.1 .
BT006736 mRNA. Translation: AAP35382.1 .
AL158141 , AL139111 Genomic DNA. Translation: CAD13488.2 .
BC004137 mRNA. Translation: AAH04137.1 .
CCDSi CCDS14396.1.
RefSeqi NP_001542.1. NM_001551.2.
UniGenei Hs.496267.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IYP X-ray 2.80 A 2-234 [» ]
ProteinModelPortali P78318.
SMRi P78318. Positions 1-221.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109698. 113 interactions.
IntActi P78318. 20 interactions.
MINTi MINT-3022988.
STRINGi 9606.ENSP00000348784.

PTM databases

PhosphoSitei P78318.

Polymorphism databases

DMDMi 14285501.

Proteomic databases

MaxQBi P78318.
PaxDbi P78318.
PeptideAtlasi P78318.
PRIDEi P78318.

Protocols and materials databases

DNASUi 3476.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342206 ; ENSP00000363661 ; ENSG00000089289 .
ENST00000356413 ; ENSP00000348784 ; ENSG00000089289 .
GeneIDi 3476.
KEGGi hsa:3476.
UCSCi uc004dxv.3. human.

Organism-specific databases

CTDi 3476.
GeneCardsi GC0XP069353.
HGNCi HGNC:5461. IGBP1.
HPAi CAB034139.
HPA000634.
HPA001004.
MIMi 300139. gene.
300472. phenotype.
neXtProti NX_P78318.
Orphaneti 52055. Agenesis of the corpus callosum - intellectual disability - coloboma - micrognathia.
PharmGKBi PA29694.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG332001.
HOGENOMi HOG000038526.
HOVERGENi HBG052090.
InParanoidi P78318.
KOi K17606.
OMAi GSRIIQD.
OrthoDBi EOG7992R2.
PhylomeDBi P78318.
TreeFami TF313433.

Miscellaneous databases

ChiTaRSi IGBP1. human.
GeneWikii IGBP1.
GenomeRNAii 3476.
NextBioi 13672.
PROi P78318.
SOURCEi Search...

Gene expression databases

Bgeei P78318.
CleanExi HS_IGBP1.
Genevestigatori P78318.

Family and domain databases

InterProi IPR007304. TAP42-like.
[Graphical view ]
PANTHERi PTHR10933. PTHR10933. 1 hit.
Pfami PF04177. TAP42. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression and chromosomal localization of the human alpha 4/IGBP1 gene, the structure of which is closely related to the yeast TAP42 protein of the rapamycin-sensitive signal transduction pathway."
    Onda M., Inui S., Maeda K., Suzuki M., Takahashi E., Sakaguchi N.
    Genomics 46:373-378(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: B-cell.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Placenta.
  5. "Alpha 4 associates with protein phosphatases 2A, 4, and 6."
    Chen J., Peterson R.T., Schreiber S.L.
    Biochem. Biophys. Res. Commun. 247:827-832(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SERINE/THREONINE PROTEIN PHOSPHATASES.
  6. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  7. "MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, Alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders."
    Short K.M., Hopwood B., Yi Z., Cox T.C.
    BMC Cell Biol. 3:1-1(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MID1 AND MID2.
  8. "A new X-linked syndrome with agenesis of the corpus callosum, mental retardation, coloboma, micrognathia, and a mutation in the alpha 4 gene at Xq13."
    Graham J.M. Jr., Wheeler P., Tackels-Horne D., Lin A.E., Hall B.D., May M., Short K.M., Schwartz C.E., Cox T.C.
    Am. J. Med. Genet. A 123:37-44(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRXS28.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Alpha4 is an essential regulator of PP2A phosphatase activity."
    Kong M., Ditsworth D., Lindsten T., Thompson C.B.
    Mol. Cell 36:51-60(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP2CA.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination."
    McConnell J.L., Watkins G.R., Soss S.E., Franz H.S., McCorvey L.R., Spiller B.W., Chazin W.J., Wadzinski B.E.
    Biochemistry 49:1713-1718(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH PPP2CA AND UBIQUITIN.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phosphorylation."
    Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R., Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.
    J. Biol. Chem. 287:24207-24215(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY MID1, PROTEOLYTIC CLEAVAGE.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234 IN COMPLEX WITH PPP2CA, FUNCTION, MUTAGENESIS OF ARG-155; LYS-158; TYR-162 AND GLU-214, INTERACTION WITH PPP2CA.

Entry informationi

Entry nameiIGBP1_HUMAN
AccessioniPrimary (citable) accession number: P78318
Secondary accession number(s): Q8TAB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 129 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

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