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Protein

E3 ubiquitin-protein ligase XIAP

Gene

XIAP

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

Functioni

Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program.12 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi300ZincPROSITE-ProRule annotation1
Metal bindingi303ZincPROSITE-ProRule annotation1
Metal bindingi320ZincPROSITE-ProRule annotation1
Metal bindingi327ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri450 – 485RING-typePROSITE-ProRule annotationAdd BLAST36

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • copper ion homeostasis Source: UniProtKB
  • inhibition of cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of protein linear polyubiquitination Source: UniProtKB
  • positive regulation of protein ubiquitination Source: UniProtKB
  • regulation of BMP signaling pathway Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • regulation of innate immune response Source: UniProtKB
  • regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
  • Wnt signaling pathway Source: UniProtKB-KW

Keywordsi

Molecular functionProtease inhibitor, Thiol protease inhibitor, Transferase
Biological processApoptosis, Ubl conjugation pathway, Wnt signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-111463. SMAC binds to IAPs.
R-HSA-111464. SMAC-mediated dissociation of IAP:caspase complexes.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-5213460. RIPK1-mediated regulated necrosis.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5675482. Regulation of necroptotic cell death.
R-HSA-8948747. Regulation of PTEN localization.
R-HSA-8948751. Regulation of PTEN stability and activity.
SABIO-RKiP98170.
SignaLinkiP98170.
SIGNORiP98170.

Protein family/group databases

MEROPSiI32.007.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase XIAP (EC:2.3.2.27)
Alternative name(s):
Baculoviral IAP repeat-containing protein 4
IAP-like protein
Short name:
ILP
Short name:
hILP
Inhibitor of apoptosis protein 3
Short name:
IAP-3
Short name:
hIAP-3
Short name:
hIAP3
RING-type E3 ubiquitin transferase XIAP
X-linked inhibitor of apoptosis protein
Short name:
X-linked IAP
Gene namesi
Name:XIAP
Synonyms:API3, BIRC4, IAP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000101966.12.
HGNCiHGNC:592. XIAP.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Lymphoproliferative syndrome, X-linked, 2 (XLP2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare immunodeficiency characterized by extreme susceptibility to infection with Epstein-Barr virus (EBV). Symptoms include severe or fatal mononucleosis, acquired hypogammaglobulinemia, pancytopenia and malignant lymphoma.
See also OMIM:300635

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi75Y → G: Loss of interaction with TAB1/MAP3K7IP1; when associated with G-75. 1 Publication1
Mutagenesisi80V → A: Strongly reduced interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Reduced activation of NF-kappa-B. 1 Publication1
Mutagenesisi80V → D: Loss of interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Strongly reduced activation of NF-kappa-B. 1 Publication1
Mutagenesisi86V → E: Loss of dimerization. Reduces activation of NF-kappa-B. 1 Publication1
Mutagenesisi87S → A: No effect on dimerization. 1 Publication1
Mutagenesisi87S → D or E: Abolishes dimerization. Interferes with ubiquitination. 1 Publication1
Mutagenesisi98L → G: Loss of interaction with TAB1/MAP3K7IP1; when associated with G-75. 1 Publication1
Mutagenesisi141L → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi147V → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi148D → A: Abolishes inhibition of caspase-3. Reduced interaction with PRSS25; when associated with S-214. 2 Publications1
Mutagenesisi149I → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi151D → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi167L → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi196D → A: Reduced inhibition of caspase-3. May affect protein folding and stability. 1 Publication1
Mutagenesisi214D → S: Reduced interaction with PRSS25. Reduced interaction with PRSS25; when associated with A-148. 1 Publication1
Mutagenesisi259N → D: Reduced interaction with PRSS25; when associated with S-314. 1 Publication1
Mutagenesisi310W → R: Reduced interaction with PRSS25; when associated with S-314. 1 Publication1
Mutagenesisi314E → S: Decreased interaction with DIABLO/SMAC and with PRSS25. Decreases interaction with PRSS25; when associated with D-259 or A-310. 1 Publication1
Mutagenesisi450C → A or S: Inhibits degradation of active caspase-3. 1 Publication1
Mutagenesisi467H → A: Loss of E3 ubiquitin-protein ligase activity. 1 Publication1

Organism-specific databases

DisGeNETi331.
GeneReviewsiXIAP.
MalaCardsiXIAP.
MIMi300635. phenotype.
OpenTargetsiENSG00000101966.
Orphaneti2442. X-linked lymphoproliferative disease.
PharmGKBiPA25361.

Chemistry databases

ChEMBLiCHEMBL4198.
GuidetoPHARMACOLOGYi2790.

Polymorphism and mutation databases

BioMutaiXIAP.
DMDMi12643387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001223521 – 497E3 ubiquitin-protein ligase XIAPAdd BLAST497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87Phosphoserine; by PKB2 Publications1
Cross-linki322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei450S-nitrosocysteine1 Publication1

Post-translational modificationi

S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase activity.3 Publications
Autoubiquitinated and degraded by the proteasome in apoptotic cells.2 Publications
Phosphorylation by PKB/AKT protects XIAP against ubiquitination and protects the protein against proteasomal degradation.3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiP98170.
MaxQBiP98170.
PaxDbiP98170.
PeptideAtlasiP98170.
PRIDEiP98170.

PTM databases

iPTMnetiP98170.
PhosphoSitePlusiP98170.

Miscellaneous databases

PMAP-CutDBiP98170.

Expressioni

Tissue specificityi

Ubiquitous, except peripheral blood leukocytes.

Gene expression databases

BgeeiENSG00000101966.
CleanExiHS_XIAP.
ExpressionAtlasiP98170. baseline and differential.
GenevisibleiP98170. HS.

Organism-specific databases

HPAiCAB009203.
HPA042428.

Interactioni

Subunit structurei

Monomer, and homodimer. Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with TAB1/MAP3K7IP1 and AIFM1. Interaction with SMAC hinders binding of TAB1/MAP3K7IP1 and AIFM1. Interacts with TCF25 and COMMD1. Interacts with SEPT4 isoform 6, but not with other SEPT4 isoforms. Interacts with RIP1, RIP2, RIP3, RIP4, CCS and USP19. Interacts (via BIR 2 domain and BIR 3 domain) with HAX1 (via C-terminus) and this interaction blocks ubiquitination of XIAP/BIRC4. Interacts with the monomeric form of BIRC5/survivin. Interacts with TLE3 and TCF7L2/TCF4.16 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi106828. 162 interactors.
CORUMiP98170.
DIPiDIP-27626N.
IntActiP98170. 82 interactors.
MINTiMINT-141734.
STRINGi9606.ENSP00000347858.

Chemistry databases

BindingDBiP98170.

Structurei

Secondary structure

1497
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 30Combined sources5
Helixi31 – 33Combined sources3
Beta strandi40 – 42Combined sources3
Helixi44 – 49Combined sources6
Beta strandi52 – 54Combined sources3
Beta strandi61 – 63Combined sources3
Turni64 – 66Combined sources3
Helixi79 – 86Combined sources8
Turni91 – 97Combined sources7
Turni128 – 130Combined sources3
Helixi136 – 142Combined sources7
Helixi150 – 152Combined sources3
Helixi158 – 161Combined sources4
Helixi163 – 168Combined sources6
Turni169 – 172Combined sources4
Helixi175 – 177Combined sources3
Helixi181 – 186Combined sources6
Beta strandi189 – 191Combined sources3
Beta strandi198 – 200Combined sources3
Turni201 – 203Combined sources3
Beta strandi206 – 208Combined sources3
Helixi216 – 223Combined sources8
Helixi228 – 232Combined sources5
Helixi244 – 246Combined sources3
Beta strandi249 – 251Combined sources3
Beta strandi254 – 256Combined sources3
Helixi260 – 262Combined sources3
Helixi265 – 270Combined sources6
Turni271 – 274Combined sources4
Beta strandi277 – 279Combined sources3
Helixi281 – 286Combined sources6
Beta strandi289 – 291Combined sources3
Beta strandi293 – 296Combined sources4
Beta strandi298 – 300Combined sources3
Turni301 – 303Combined sources3
Beta strandi306 – 309Combined sources4
Beta strandi311 – 313Combined sources3
Helixi316 – 323Combined sources8
Helixi328 – 333Combined sources6
Helixi336 – 342Combined sources7
Turni343 – 345Combined sources3
Helixi346 – 353Combined sources8
Helixi354 – 356Combined sources3
Helixi368 – 372Combined sources5
Helixi375 – 381Combined sources7
Helixi386 – 400Combined sources15
Helixi407 – 419Combined sources13
Helixi437 – 447Combined sources11
Turni451 – 453Combined sources3
Beta strandi454 – 457Combined sources4
Beta strandi460 – 463Combined sources4
Helixi472 – 475Combined sources4
Turni482 – 484Combined sources3
Beta strandi489 – 493Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C9QNMR-A124-240[»]
1F9XNMR-A241-356[»]
1G3FNMR-A241-356[»]
1G73X-ray2.00C/D238-358[»]
1I3OX-ray2.70E/F124-240[»]
1I4OX-ray2.40C/D120-260[»]
1I51X-ray2.45E/F124-240[»]
1KMCX-ray2.90C/D124-242[»]
1NW9X-ray2.40A253-350[»]
1TFQNMR-A241-356[»]
1TFTNMR-A241-356[»]
2ECGNMR-A430-497[»]
2JK7X-ray2.82A241-356[»]
2KNANMR-A357-449[»]
2OPYX-ray2.80A249-354[»]
2OPZX-ray3.00A/B/C/D249-357[»]
2POIX-ray1.80A10-99[»]
2POPX-ray3.10B/D10-100[»]
2QRAX-ray2.50A/B/C/D10-99[»]
2VSLX-ray2.10A250-345[»]
3CLXX-ray2.70A/B/C/D241-356[»]
3CM2X-ray2.50A/B/C/D/E/F/G/H/I/J241-356[»]
3CM7X-ray3.10A/B/C/D241-356[»]
3EYLX-ray3.00A/B241-356[»]
3G76X-ray3.00A/B/C/D/E/F/G/H241-356[»]
3HL5X-ray1.80A/B256-346[»]
3UW4X-ray1.79A338-348[»]
3UW5X-ray1.71A/B336-348[»]
4EC4X-ray3.30A/B/C/D/E/F/G/J/K/L241-356[»]
4HY0X-ray2.84A/B/C/D/E/F/G/H238-357[»]
4IC2X-ray2.20A/B429-497[»]
4IC3X-ray1.78A/B429-497[»]
4J3YX-ray1.45A/C152-236[»]
4J44X-ray1.30A/C152-236[»]
4J45X-ray1.48A/C152-236[»]
4J46X-ray1.42A/C152-236[»]
4J47X-ray1.35A/C152-236[»]
4J48X-ray2.10A/C152-236[»]
4KJUX-ray1.60A/C152-236[»]
4KJVX-ray1.70A/C152-236[»]
4KMPX-ray1.95A/B256-348[»]
4MTZX-ray2.10A/B/C/D10-99[»]
4OXCX-ray2.90A/B/C/D10-99[»]
4WVSX-ray2.09A156-231[»]
4WVTX-ray1.96A/B156-231[»]
4WVUX-ray2.02A156-231[»]
5C0KX-ray2.20A249-354[»]
5C0LX-ray2.60A246-354[»]
5C3HX-ray2.65A249-354[»]
5C3KX-ray2.02A249-354[»]
5C7AX-ray2.36A249-354[»]
5C7BX-ray2.68A249-354[»]
5C7CX-ray2.32A249-354[»]
5C7DX-ray2.25A249-354[»]
5C83X-ray2.33A249-354[»]
5C84X-ray2.36A249-354[»]
5M6EX-ray2.32A249-354[»]
5M6FX-ray2.39A249-354[»]
5M6HX-ray2.50A249-354[»]
5M6LX-ray2.61A249-354[»]
5M6MX-ray2.37A249-354[»]
ProteinModelPortaliP98170.
SMRiP98170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98170.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati26 – 93BIR 1Add BLAST68
Repeati163 – 230BIR 2Add BLAST68
Repeati265 – 330BIR 3Add BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni141 – 149Interaction with caspase-79

Domaini

The first BIR domain is involved in interaction with TAB1/MAP3K7IP1 and is important for dimerization. The second BIR domain is sufficient to inhibit CASP3 and CASP7, while the third BIR is involved in CASP9 inhibition. The interactions with DIABLO/SMAC and PRSS25 are mediated by the second and third BIR domains.

Sequence similaritiesi

Belongs to the IAP family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri450 – 485RING-typePROSITE-ProRule annotationAdd BLAST36

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG004848.
InParanoidiP98170.
KOiK04725.
OMAiAMYSEEA.
OrthoDBiEOG091G0CXH.
PhylomeDBiP98170.
TreeFamiTF105356.

Family and domain databases

CDDicd00022. BIR. 3 hits.
InterProiView protein in InterPro
IPR001370. BIR_rpt.
IPR001841. Znf_RING.
PfamiView protein in Pfam
PF00653. BIR. 3 hits.
SMARTiView protein in SMART
SM00238. BIR. 3 hits.
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50089. ZF_RING_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P98170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFNSFEGSK TCVPADINKE EEFVEEFNRL KTFANFPSGS PVSASTLARA
60 70 80 90 100
GFLYTGEGDT VRCFSCHAAV DRWQYGDSAV GRHRKVSPNC RFINGFYLEN
110 120 130 140 150
SATQSTNSGI QNGQYKVENY LGSRDHFALD RPSETHADYL LRTGQVVDIS
160 170 180 190 200
DTIYPRNPAM YSEEARLKSF QNWPDYAHLT PRELASAGLY YTGIGDQVQC
210 220 230 240 250
FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNLNIRSE SDAVSSDRNF
260 270 280 290 300
PNSTNLPRNP SMADYEARIF TFGTWIYSVN KEQLARAGFY ALGEGDKVKC
310 320 330 340 350
FHCGGGLTDW KPSEDPWEQH AKWYPGCKYL LEQKGQEYIN NIHLTHSLEE
360 370 380 390 400
CLVRTTEKTP SLTRRIDDTI FQNPMVQEAI RMGFSFKDIK KIMEEKIQIS
410 420 430 440 450
GSNYKSLEVL VADLVNAQKD SMQDESSQTS LQKEISTEEQ LRRLQEEKLC
460 470 480 490
KICMDRNIAI VFVPCGHLVT CKQCAEAVDK CPMCYTVITF KQKIFMS
Length:497
Mass (Da):56,685
Last modified:January 24, 2001 - v2
Checksum:i9D394C16D45EB635
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti162S → C in AAC50373 (PubMed:8552191).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022282107N → S1 PublicationCorresponds to variant dbSNP:rs28382721Ensembl.1
Natural variantiVAR_022283133S → F1 PublicationCorresponds to variant dbSNP:rs28382722Ensembl.1
Natural variantiVAR_022284242D → E1 PublicationCorresponds to variant dbSNP:rs28382723Ensembl.1
Natural variantiVAR_022285423Q → P2 PublicationsCorresponds to variant dbSNP:rs5956583Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32974 mRNA. Translation: AAC50518.1.
U45880 mRNA. Translation: AAC50373.1.
AY886519 Genomic DNA. Translation: AAW62257.1.
AL121601 Genomic DNA. No translation available.
CH471107 Genomic DNA. Translation: EAX11858.1.
CH471107 Genomic DNA. Translation: EAX11859.1.
CH471107 Genomic DNA. Translation: EAX11860.1.
CH471107 Genomic DNA. Translation: EAX11861.1.
BC032729 mRNA. Translation: AAH32729.1.
CCDSiCCDS14606.1.
PIRiS69544.
RefSeqiNP_001158.2. NM_001167.3.
NP_001191330.1. NM_001204401.1.
XP_006724817.1. XM_006724754.2.
XP_011529631.1. XM_011531329.2.
UniGeneiHs.356076.
Hs.736565.

Genome annotation databases

EnsembliENST00000355640; ENSP00000347858; ENSG00000101966.
ENST00000371199; ENSP00000360242; ENSG00000101966.
ENST00000434753; ENSP00000395230; ENSG00000101966.
GeneIDi331.
KEGGihsa:331.
UCSCiuc004etx.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiXIAP_HUMAN
AccessioniPrimary (citable) accession number: P98170
Secondary accession number(s): D3DTF2, Q9NQ14
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 24, 2001
Last modified: November 22, 2017
This is version 194 of the entry and version 2 of the sequence. See 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