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Protein

Protein disulfide-isomerase A4

Gene

PDIA4

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

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. chaperone-mediated protein folding Source: UniProtKB
  3. protein folding Source: GO_Central
  4. protein secretion Source: ProtInc
  5. response to endoplasmic reticulum stress Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A4 (EC:5.3.4.1)
Alternative name(s):
Endoplasmic reticulum resident protein 70
Short name:
ER protein 70
Short name:
ERp70
Endoplasmic reticulum resident protein 72
Short name:
ER protein 72
Short name:
ERp-72
Short name:
ERp72
Gene namesi
Name:PDIA4
Synonyms:ERP70, ERP72
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:30167. PDIA4.

Subcellular locationi

Endoplasmic reticulum lumen. Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: GO_Central
  3. endoplasmic reticulum lumen Source: ProtInc
  4. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671190.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 645625Protein disulfide-isomerase A4PRO_0000034229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 94Redox-activePROSITE-ProRule annotation
Disulfide bondi206 ↔ 209Redox-activePROSITE-ProRule annotation
Modified residuei366 – 3661N6-acetyllysine1 Publication
Disulfide bondi555 ↔ 558Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP13667.
PaxDbiP13667.
PeptideAtlasiP13667.
PRIDEiP13667.

2D gel databases

OGPiP13667.
REPRODUCTION-2DPAGEIPI00009904.

PTM databases

PhosphoSiteiP13667.

Expressioni

Gene expression databases

BgeeiP13667.
CleanExiHS_PDIA4.
ExpressionAtlasiP13667. baseline and differential.
GenevestigatoriP13667.

Organism-specific databases

HPAiCAB017368.
HPA006139.
HPA006140.

Interactioni

Subunit structurei

Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.

Binary interactionsi

WithEntry#Exp.IntActNotes
Q763533EBI-1054653,EBI-6248077From a different organism.
PPIBP232843EBI-1054653,EBI-8771982

Protein-protein interaction databases

BioGridi114966. 57 interactions.
IntActiP13667. 17 interactions.
MINTiMINT-4999858.
STRINGi9606.ENSP00000286091.

Structurei

Secondary structure

1
645
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 613Combined sources
Beta strandi64 – 663Combined sources
Turni69 – 713Combined sources
Helixi72 – 765Combined sources
Beta strandi80 – 878Combined sources
Helixi92 – 10918Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi117 – 1215Combined sources
Turni122 – 1243Combined sources
Helixi126 – 1316Combined sources
Beta strandi136 – 1449Combined sources
Beta strandi147 – 1504Combined sources
Helixi157 – 16812Combined sources
Beta strandi178 – 1814Combined sources
Turni184 – 1863Combined sources
Helixi187 – 1937Combined sources
Beta strandi195 – 2028Combined sources
Helixi208 – 2114Combined sources
Helixi213 – 22412Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi232 – 2365Combined sources
Turni237 – 2393Combined sources
Helixi241 – 2466Combined sources
Beta strandi251 – 2599Combined sources
Beta strandi262 – 2654Combined sources
Helixi272 – 28211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IDVX-ray1.95A53-284[»]
ProteinModelPortaliP13667.
SMRiP13667. Positions 54-645.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13667.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 169149Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 301144Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini505 – 636132Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi642 – 6454Prevents secretion from ER

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 5517Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 3 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP13667.
KOiK09582.
OMAiIIGVFKG.
OrthoDBiEOG7VHSX1.
PhylomeDBiP13667.
TreeFamiTF106382.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMiSSF52833. SSF52833. 5 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13667-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD
60 70 80 90 100
EEEDDLEVKE ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE
110 120 130 140 150
YEKIANILKD KDPPIPVAKI DATSASVLAS RFDVSGYPTI KILKKGQAVD
160 170 180 190 200
YEGSRTQEEI VAKVREVSQP DWTPPPEVTL VLTKENFDEV VNDADIILVE
210 220 230 240 250
FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE TDLAKRFDVS
260 270 280 290 300
GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL
310 320 330 340 350
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV
360 370 380 390 400
SQGQLVVMQP EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR
410 420 430 440 450
KVSNDAKRYT RRPLVVVYYS VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF
460 470 480 490 500
AIADEEDYAG EVKDLGLSES GEDVNAAILD ESGKKFAMEP EEFDSDTLRE
510 520 530 540 550
FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM DPKKDVLIEF
560 570 580 590 600
YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
610 620 630 640
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL
Length:645
Mass (Da):72,932
Last modified:May 1, 1991 - v2
Checksum:i1919C2AE12CD2684
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021E → G in BAF83660 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731T → M.
Corresponds to variant rs2290971 [ dbSNP | Ensembl ].
VAR_052580

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05016 mRNA. Translation: AAA58460.1.
AK290971 mRNA. Translation: BAF83660.1.
AC093743 Genomic DNA. Translation: AAQ96863.1.
CH471146 Genomic DNA. Translation: EAW80065.1.
CH471146 Genomic DNA. Translation: EAW80066.1.
BC000425 mRNA. Translation: AAH00425.1.
BC001928 mRNA. Translation: AAH01928.1.
BC006344 mRNA. Translation: AAH06344.1.
BC011754 mRNA. Translation: AAH11754.1.
CCDSiCCDS5893.1.
PIRiA23723.
RefSeqiNP_004902.1. NM_004911.4.
UniGeneiHs.93659.

Genome annotation databases

EnsembliENST00000286091; ENSP00000286091; ENSG00000155660.
GeneIDi9601.
KEGGihsa:9601.
UCSCiuc003wff.2. human.

Polymorphism databases

DMDMi119530.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05016 mRNA. Translation: AAA58460.1.
AK290971 mRNA. Translation: BAF83660.1.
AC093743 Genomic DNA. Translation: AAQ96863.1.
CH471146 Genomic DNA. Translation: EAW80065.1.
CH471146 Genomic DNA. Translation: EAW80066.1.
BC000425 mRNA. Translation: AAH00425.1.
BC001928 mRNA. Translation: AAH01928.1.
BC006344 mRNA. Translation: AAH06344.1.
BC011754 mRNA. Translation: AAH11754.1.
CCDSiCCDS5893.1.
PIRiA23723.
RefSeqiNP_004902.1. NM_004911.4.
UniGeneiHs.93659.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IDVX-ray1.95A53-284[»]
ProteinModelPortaliP13667.
SMRiP13667. Positions 54-645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114966. 57 interactions.
IntActiP13667. 17 interactions.
MINTiMINT-4999858.
STRINGi9606.ENSP00000286091.

PTM databases

PhosphoSiteiP13667.

Polymorphism databases

DMDMi119530.

2D gel databases

OGPiP13667.
REPRODUCTION-2DPAGEIPI00009904.

Proteomic databases

MaxQBiP13667.
PaxDbiP13667.
PeptideAtlasiP13667.
PRIDEiP13667.

Protocols and materials databases

DNASUi9601.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286091; ENSP00000286091; ENSG00000155660.
GeneIDi9601.
KEGGihsa:9601.
UCSCiuc003wff.2. human.

Organism-specific databases

CTDi9601.
GeneCardsiGC07M148700.
HGNCiHGNC:30167. PDIA4.
HPAiCAB017368.
HPA006139.
HPA006140.
neXtProtiNX_P13667.
PharmGKBiPA142671190.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP13667.
KOiK09582.
OMAiIIGVFKG.
OrthoDBiEOG7VHSX1.
PhylomeDBiP13667.
TreeFamiTF106382.

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Miscellaneous databases

ChiTaRSiPDIA4. human.
EvolutionaryTraceiP13667.
GenomeRNAii9601.
NextBioi36019.
PROiP13667.

Gene expression databases

BgeeiP13667.
CleanExiHS_PDIA4.
ExpressionAtlasiP13667. baseline and differential.
GenevestigatoriP13667.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMiSSF52833. SSF52833. 5 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human deoxycytidine kinase. Sequence of cDNA clones and analysis of expression in cell lines with and without enzyme activity."
    Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
    J. Biol. Chem. 264:14762-14768(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. Erratum
    Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
    J. Biol. Chem. 266:5353-5353(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2002) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Muscle.
  7. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
    Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
    Mol. Biol. Cell 13:4456-4469(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  10. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPDIA4_HUMAN
AccessioniPrimary (citable) accession number: P13667
Secondary accession number(s): A8K4K6, Q549T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 1991
Last modified: March 4, 2015
This is version 171 of the entry and version 2 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

Caution

Was originally thought to be a deoxycytidine kinase.1 Publication

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.