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Protein

Protein disulfide-isomerase

Gene

P4HB

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

Functioni

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).3 Publications

Catalytic activityi

Catalyzes the rearrangement of -S-S- bonds in proteins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei53Nucleophile1
Sitei54Contributes to redox potential value1
Sitei55Contributes to redox potential value1
Active sitei56Nucleophile1
Sitei120Lowers pKa of C-terminal Cys of first active site1
Active sitei397NucleophileBy similarity1
Sitei398Contributes to redox potential valueBy similarity1
Sitei399Contributes to redox potential valueBy similarity1
Active sitei400NucleophileBy similarity1
Sitei461Lowers pKa of C-terminal Cys of second active siteBy similarity1

GO - Molecular functioni

  • integrin binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • procollagen-proline 4-dioxygenase activity Source: ProtInc
  • protein disulfide isomerase activity Source: CACAO
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to hypoxia Source: BHF-UCL
  • lipoprotein biosynthetic process Source: Reactome
  • peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: MGI
  • positive regulation of viral entry into host cell Source: UniProtKB
  • regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • response to endoplasmic reticulum stress Source: BHF-UCL
  • response to reactive oxygen species Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Enzyme and pathway databases

BioCyciZFISH:HS06845-MONOMER.
BRENDAi5.3.4.1. 2681.
ReactomeiR-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-8866423. VLDL biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
p55
Gene namesi
Name:P4HB
Synonyms:ERBA2L, PDI, PDIA1, PO4DB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:8548. P4HB.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum chaperone complex Source: Ensembl
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • external side of plasma membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular region Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • procollagen-proline 4-dioxygenase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Cole-Carpenter syndrome 1 (CLCRP1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Cole-Carpenter syndrome, a disorder characterized by features of osteogenesis imperfecta such as bone deformities and severe bone fragility with frequent fractures, in association with craniosynostosis, ocular proptosis, hydrocephalus, growth failure and distinctive facial features. Craniofacial findings include marked frontal bossing, midface hypoplasia, and micrognathia. Despite the craniosynostosis and hydrocephalus, intellectual development is normal. CLCRP1 inheritance is autosomal dominant.
See also OMIM:112240
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073440393Y → C in CLCRP1; impairs ability to act as a disulfide isomerase enzyme. 1 PublicationCorresponds to variant rs786204843dbSNPEnsembl.1

Keywords - Diseasei

Craniosynostosis, Disease mutation, Osteogenesis imperfecta

Organism-specific databases

DisGeNETi5034.
MIMi112240. phenotype.
OpenTargetsiENSG00000185624.
PharmGKBiPA32876.

Chemistry databases

ChEMBLiCHEMBL5422.
DrugBankiDB03615. Ribostamycin.

Polymorphism and mutation databases

BioMutaiP4HB.
DMDMi2507460.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Combined sources4 PublicationsAdd BLAST17
ChainiPRO_000003419518 – 508Protein disulfide-isomeraseAdd BLAST491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 56Redox-activePROSITE-ProRule annotation1 Publication
Modified residuei200N6-acetyllysineBy similarity1
Modified residuei222N6-succinyllysineBy similarity1
Modified residuei271N6-succinyllysineBy similarity1
Modified residuei357Phosphoserine; by FAM20C1 Publication1
Disulfide bondi397 ↔ 400Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP07237.
MaxQBiP07237.
PaxDbiP07237.
PeptideAtlasiP07237.
PRIDEiP07237.
TopDownProteomicsiP07237.

2D gel databases

DOSAC-COBS-2DPAGEP07237.
OGPiP07237.
REPRODUCTION-2DPAGEIPI00010796.
P07237.
SWISS-2DPAGEP07237.

PTM databases

iPTMnetiP07237.
PhosphoSitePlusiP07237.
SwissPalmiP07237.

Miscellaneous databases

PMAP-CutDBP07237.

Expressioni

Gene expression databases

BgeeiENSG00000185624.
CleanExiHS_P4HB.
ExpressionAtlasiP07237. baseline and differential.
GenevisibleiP07237. HS.

Organism-specific databases

HPAiCAB012463.
HPA018884.

Interactioni

Subunit structurei

Heterodimer; heterodimerizes with the protein microsomal triglyceride transfer MTTP (PubMed:23475612, PubMed:26224785). Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity (By similarity). Binds UBQLN1 (PubMed:12095988). Interacts with ERO1B (PubMed:11707400). Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERO1AQ96HE72EBI-395883,EBI-2564539
HM13Q8TCT93EBI-395883,EBI-347472
PRDX4Q131622EBI-395883,EBI-2211957
TAP1Q035184EBI-395883,EBI-747259

GO - Molecular functioni

  • integrin binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi111073. 128 interactors.
DIPiDIP-32979N.
IntActiP07237. 56 interactors.
MINTiMINT-4999403.
STRINGi9606.ENSP00000327801.

Chemistry databases

BindingDBiP07237.

Structurei

Secondary structure

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 23Combined sources3
Beta strandi26 – 28Combined sources3
Turni31 – 33Combined sources3
Helixi34 – 40Combined sources7
Beta strandi42 – 49Combined sources8
Helixi54 – 72Combined sources19
Beta strandi78 – 83Combined sources6
Turni84 – 86Combined sources3
Helixi88 – 93Combined sources6
Beta strandi101 – 106Combined sources6
Beta strandi110 – 112Combined sources3
Beta strandi114 – 116Combined sources3
Helixi122 – 132Combined sources11
Beta strandi137 – 139Combined sources3
Helixi143 – 151Combined sources9
Beta strandi153 – 160Combined sources8
Turni162 – 165Combined sources4
Helixi167 – 178Combined sources12
Beta strandi180 – 182Combined sources3
Beta strandi184 – 187Combined sources4
Helixi190 – 195Combined sources6
Beta strandi199 – 209Combined sources11
Beta strandi212 – 215Combined sources4
Helixi222 – 232Combined sources11
Beta strandi237 – 239Combined sources3
Turni242 – 244Combined sources3
Helixi245 – 249Combined sources5
Beta strandi250 – 252Combined sources3
Beta strandi255 – 260Combined sources6
Beta strandi265 – 267Combined sources3
Helixi268 – 280Combined sources13
Turni281 – 285Combined sources5
Beta strandi287 – 291Combined sources5
Helixi296 – 298Combined sources3
Helixi299 – 304Combined sources6
Helixi309 – 311Combined sources3
Beta strandi313 – 319Combined sources7
Beta strandi321 – 323Combined sources3
Beta strandi325 – 327Combined sources3
Beta strandi330 – 332Combined sources3
Helixi336 – 347Combined sources12
Beta strandi353 – 355Combined sources3
Helixi362 – 364Combined sources3
Beta strandi367 – 372Combined sources6
Turni374 – 376Combined sources3
Helixi377 – 381Combined sources5
Beta strandi387 – 393Combined sources7
Helixi398 – 413Combined sources16
Turni414 – 416Combined sources3
Beta strandi418 – 426Combined sources9
Turni427 – 429Combined sources3
Beta strandi439 – 446Combined sources8
Beta strandi448 – 451Combined sources4
Helixi463 – 470Combined sources8
Turni471 – 473Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BJXNMR-A136-245[»]
1MEKNMR-A18-137[»]
1X5CNMR-A368-475[»]
2BJXNMR-A136-245[»]
2K18NMR-A135-357[»]
3BJ5X-ray2.20A230-368[»]
3UEMX-ray2.29A137-479[»]
4EKZX-ray2.51A18-479[»]
4EL1X-ray2.88A/B18-479[»]
4JU5X-ray2.28A/B135-367[»]
ProteinModelPortaliP07237.
SMRiP07237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07237.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 134Thioredoxin 1PROSITE-ProRule annotationAdd BLAST117
Domaini349 – 475Thioredoxin 2PROSITE-ProRule annotationAdd BLAST127

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi505 – 508Prevents secretion from ER4

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0190. Eukaryota.
COG0526. LUCA.
GeneTreeiENSGT00860000133691.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP07237.
KOiK09580.
OMAiIEKYVDP.
OrthoDBiEOG091G08WM.
PhylomeDBiP07237.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07237-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA
60 70 80 90 100
PWCGHCKALA PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP
110 120 130 140 150
TIKFFRNGDT ASPKEYTAGR EADDIVNWLK KRTGPAATTL PDGAAAESLV
160 170 180 190 200
ESSEVAVIGF FKDVESDSAK QFLQAAEAID DIPFGITSNS DVFSKYQLDK
210 220 230 240 250
DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF TEQTAPKIFG
260 270 280 290 300
GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR
310 320 330 340 350
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK
360 370 380 390 400
IKPHLMSQEL PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC
410 420 430 440 450
KQLAPIWDKL GETYKDHENI VIAKMDSTAN EVEAVKVHSF PTLKFFPASA
460 470 480 490 500
DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD DDDLEDLEEA EEPDMEEDDD

QKAVKDEL
Length:508
Mass (Da):57,116
Last modified:November 1, 1997 - v3
Checksum:i906CE6D9900B8FCE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10 – 11AV → PW in CAA28775 (PubMed:3034602).Curated2
Sequence conflicti21E → D AA sequence (PubMed:9399589).Curated1
Sequence conflicti24D → V AA sequence (PubMed:9399589).Curated1
Sequence conflicti44 – 45LL → PP in CAA28775 (PubMed:3034602).Curated2
Sequence conflicti49Y → H in CAA28775 (PubMed:3034602).Curated1
Sequence conflicti141P → R in AAA61169 (PubMed:3611107).Curated1
Sequence conflicti360 – 362LPE → RAG in AAA61169 (PubMed:3611107).Curated3
Sequence conflicti372L → P in AAA61169 (PubMed:3611107).Curated1
Sequence conflicti439S → G in CAA28775 (PubMed:3034602).Curated1
Sequence conflicti444K → G in CAA28775 (PubMed:3034602).Curated1
Sequence conflicti460E → Q in CAA30112 (PubMed:3342239).Curated1
Sequence conflicti481D → V in CAA28775 (PubMed:3034602).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073440393Y → C in CLCRP1; impairs ability to act as a disulfide isomerase enzyme. 1 PublicationCorresponds to variant rs786204843dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05130 mRNA. Translation: CAA28775.1.
J02783 mRNA. Translation: AAA61169.1.
M22806
, M22803, M22804, M22805 Genomic DNA. Translation: AAC13652.1.
AK315631 mRNA. Translation: BAG37999.1.
CH471099 Genomic DNA. Translation: EAW89690.1.
BC010859 mRNA. Translation: AAH10859.1.
BC029617 mRNA. Translation: AAH29617.1.
BC071892 mRNA. Translation: AAH71892.1.
S37207 Genomic DNA. Translation: AAB22262.2.
X07077 mRNA. Translation: CAA30112.1.
CCDSiCCDS11787.1.
PIRiA31913. ISHUSS.
RefSeqiNP_000909.2. NM_000918.3.
UniGeneiHs.464336.

Genome annotation databases

EnsembliENST00000331483; ENSP00000327801; ENSG00000185624.
GeneIDi5034.
KEGGihsa:5034.
UCSCiuc002kbn.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05130 mRNA. Translation: CAA28775.1.
J02783 mRNA. Translation: AAA61169.1.
M22806
, M22803, M22804, M22805 Genomic DNA. Translation: AAC13652.1.
AK315631 mRNA. Translation: BAG37999.1.
CH471099 Genomic DNA. Translation: EAW89690.1.
BC010859 mRNA. Translation: AAH10859.1.
BC029617 mRNA. Translation: AAH29617.1.
BC071892 mRNA. Translation: AAH71892.1.
S37207 Genomic DNA. Translation: AAB22262.2.
X07077 mRNA. Translation: CAA30112.1.
CCDSiCCDS11787.1.
PIRiA31913. ISHUSS.
RefSeqiNP_000909.2. NM_000918.3.
UniGeneiHs.464336.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BJXNMR-A136-245[»]
1MEKNMR-A18-137[»]
1X5CNMR-A368-475[»]
2BJXNMR-A136-245[»]
2K18NMR-A135-357[»]
3BJ5X-ray2.20A230-368[»]
3UEMX-ray2.29A137-479[»]
4EKZX-ray2.51A18-479[»]
4EL1X-ray2.88A/B18-479[»]
4JU5X-ray2.28A/B135-367[»]
ProteinModelPortaliP07237.
SMRiP07237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111073. 128 interactors.
DIPiDIP-32979N.
IntActiP07237. 56 interactors.
MINTiMINT-4999403.
STRINGi9606.ENSP00000327801.

Chemistry databases

BindingDBiP07237.
ChEMBLiCHEMBL5422.
DrugBankiDB03615. Ribostamycin.

PTM databases

iPTMnetiP07237.
PhosphoSitePlusiP07237.
SwissPalmiP07237.

Polymorphism and mutation databases

BioMutaiP4HB.
DMDMi2507460.

2D gel databases

DOSAC-COBS-2DPAGEP07237.
OGPiP07237.
REPRODUCTION-2DPAGEIPI00010796.
P07237.
SWISS-2DPAGEP07237.

Proteomic databases

EPDiP07237.
MaxQBiP07237.
PaxDbiP07237.
PeptideAtlasiP07237.
PRIDEiP07237.
TopDownProteomicsiP07237.

Protocols and materials databases

DNASUi5034.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331483; ENSP00000327801; ENSG00000185624.
GeneIDi5034.
KEGGihsa:5034.
UCSCiuc002kbn.2. human.

Organism-specific databases

CTDi5034.
DisGeNETi5034.
GeneCardsiP4HB.
HGNCiHGNC:8548. P4HB.
HPAiCAB012463.
HPA018884.
MIMi112240. phenotype.
176790. gene.
neXtProtiNX_P07237.
OpenTargetsiENSG00000185624.
PharmGKBiPA32876.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0190. Eukaryota.
COG0526. LUCA.
GeneTreeiENSGT00860000133691.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP07237.
KOiK09580.
OMAiIEKYVDP.
OrthoDBiEOG091G08WM.
PhylomeDBiP07237.
TreeFamiTF106381.

Enzyme and pathway databases

BioCyciZFISH:HS06845-MONOMER.
BRENDAi5.3.4.1. 2681.
ReactomeiR-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-8866423. VLDL biosynthesis.

Miscellaneous databases

ChiTaRSiP4HB. human.
EvolutionaryTraceiP07237.
GeneWikiiP4HB.
GenomeRNAii5034.
PMAP-CutDBP07237.
PROiP07237.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185624.
CleanExiHS_P4HB.
ExpressionAtlasiP07237. baseline and differential.
GenevisibleiP07237. HS.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDIA1_HUMAN
AccessioniPrimary (citable) accession number: P07237
Secondary accession number(s): B2RDQ2
, P30037, P32079, Q15205, Q6LDE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 220 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

Reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

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 one 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.