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Q15011

- HERP1_HUMAN

UniProt

Q15011 - HERP1_HUMAN

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Protein

Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein

Gene

HERPUD1

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

Functioni

Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated beta-amyloid protein 40 generation.1 Publication

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular calcium ion homeostasis Source: Ensembl
  3. cellular protein metabolic process Source: Reactome
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  6. positive regulation of protein binding Source: Ensembl
  7. regulation of protein ubiquitination Source: Ensembl
  8. response to unfolded protein Source: UniProtKB
  9. ubiquitin-dependent protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Unfolded protein response

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein
Alternative name(s):
Methyl methanesulfonate (MMF)-inducible fragment protein 1
Gene namesi
Name:HERPUD1
Synonyms:HERP, KIAA0025, MIF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:13744. HERPUD1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 263263CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei264 – 28421HelicalSequence AnalysisAdd
BLAST
Topological domaini285 – 2895LumenalSequence Analysis
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST
Topological domaini311 – 39181CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 proteinPRO_0000114920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15011.
PaxDbiQ15011.
PRIDEiQ15011.

PTM databases

PhosphoSiteiQ15011.

Expressioni

Tissue specificityi

Widely expressed; in the brain, expression seems to be restricted to neurons and vascular smooth muscle cells. Present in activated microglia in senile plaques in the brain of patients with Alzheimer disease.

Inductioni

Up-regulated by endoplasmic reticulum stress and CREB3.2 Publications

Gene expression databases

BgeeiQ15011.
CleanExiHS_HERPUD1.
ExpressionAtlasiQ15011. baseline and differential.
GenevestigatoriQ15011.

Organism-specific databases

HPAiCAB037041.
CAB037104.
HPA040754.
HPA041219.

Interactioni

Subunit structurei

Interacts with PSEN1 and PSEN2. Interacts with SYVN1 and UBXN6.3 Publications

Protein-protein interaction databases

BioGridi115060. 28 interactions.
DIPiDIP-46662N.
IntActiQ15011. 10 interactions.
MINTiMINT-2867283.
STRINGi9606.ENSP00000300302.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 155Combined sources
Beta strandi17 – 204Combined sources
Beta strandi24 – 274Combined sources
Helixi34 – 4411Combined sources
Turni51 – 533Combined sources
Beta strandi55 – 584Combined sources
Beta strandi65 – 673Combined sources
Helixi69 – 724Combined sources
Beta strandi75 – 773Combined sources
Beta strandi79 – 857Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGDNMR-A10-90[»]
ProteinModelPortaliQ15011.
SMRiQ15011. Positions 10-90.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15011.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 7263Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG259558.
GeneTreeiENSGT00390000017671.
HOGENOMiHOG000252989.
HOVERGENiHBG051899.
InParanoidiQ15011.
KOiK14027.
OMAiPLYTRIT.
OrthoDBiEOG7QRQWK.
PhylomeDBiQ15011.
TreeFamiTF324319.

Family and domain databases

InterProiIPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q15011-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MESETEPEPV TLLVKSPNQR HRDLELSGDR GWSVGHLKAH LSRVYPERPR
60 70 80 90 100
PEDQRLIYSG KLLLDHQCLR DLLPKQEKRH VLHLVCNVKS PSKMPEINAK
110 120 130 140 150
VAESTEEPAG SNRGQYPEDS SSDGLRQREV LRNLSSPGWE NISRPEAAQQ
160 170 180 190 200
AFQGLGPGFS GYTPYGWLQL SWFQQIYARQ YYMQYLAATA ASGAFVPPPS
210 220 230 240 250
AQEIPVVSAP APAPIHNQFP AENQPANQNA APQVVVNPGA NQNLRMNAQG
260 270 280 290 300
GPIVEEDDEI NRDWLDWTYS AATFSVFLSI LYFYSSLSRF LMVMGATVVM
310 320 330 340 350
YLHHVGWFPF RPRPVQNFPN DGPPPDVVNQ DPNNNLQEGT DPETEDPNHL
360 370 380 390
PPDRDVLDGE QTSPSFMSTA WLVFKTFFAS LLPEGPPAIA N
Length:391
Mass (Da):43,720
Last modified:November 1, 1996 - v1
Checksum:i3CA827DC7EF0ED22
GO
Isoform 2 (identifier: Q15011-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-76: Missing.

Show »
Length:390
Mass (Da):43,592
Checksum:i7BCA8854403C71AF
GO
Isoform 3 (identifier: Q15011-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-76: Missing.
     145-302: Missing.

Show »
Length:232
Mass (Da):26,220
Checksum:iBE916EB3E3CD79C0
GO
Isoform 4 (identifier: Q15011-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-99: Missing.

Note: No experimental confirmation available.

Show »
Length:366
Mass (Da):40,851
Checksum:iDD39A053E4D46626
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501R → H.
Corresponds to variant rs2217332 [ dbSNP | Ensembl ].
VAR_024277

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei75 – 9925Missing in isoform 4. CuratedVSP_047333Add
BLAST
Alternative sequencei76 – 761Missing in isoform 2 and isoform 3. 2 PublicationsVSP_006708
Alternative sequencei145 – 302158Missing in isoform 3. 1 PublicationVSP_006709Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034989 mRNA. Translation: BAB07891.1.
D14695 mRNA. Translation: BAA03521.1.
AF055001 mRNA. Translation: AAC09355.1.
AF055003 mRNA. Translation: AAC09357.1.
AB034990 Genomic DNA. Translation: BAB19010.1.
CR457116 mRNA. Translation: CAG33397.1.
AC012181 Genomic DNA. No translation available.
BC000086 mRNA. Translation: AAH00086.1.
BC008320 mRNA. Translation: AAH08320.1.
BC009739 mRNA. Translation: AAH09739.1.
BC032673 mRNA. Translation: AAH32673.1.
CCDSiCCDS10771.1. [Q15011-1]
CCDS45492.1. [Q15011-2]
RefSeqiNP_001010989.1. NM_001010989.2. [Q15011-2]
NP_001259032.1. NM_001272103.1.
NP_055500.1. NM_014685.3. [Q15011-1]
UniGeneiHs.146393.

Genome annotation databases

EnsembliENST00000300302; ENSP00000300302; ENSG00000051108. [Q15011-2]
ENST00000344114; ENSP00000340931; ENSG00000051108. [Q15011-3]
ENST00000379792; ENSP00000369118; ENSG00000051108. [Q15011-4]
ENST00000439977; ENSP00000409555; ENSG00000051108. [Q15011-1]
GeneIDi9709.
KEGGihsa:9709.
UCSCiuc002eke.2. human. [Q15011-1]
uc002ekf.2. human. [Q15011-2]
uc031qwh.1. human. [Q15011-3]

Polymorphism databases

DMDMi3123034.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034989 mRNA. Translation: BAB07891.1 .
D14695 mRNA. Translation: BAA03521.1 .
AF055001 mRNA. Translation: AAC09355.1 .
AF055003 mRNA. Translation: AAC09357.1 .
AB034990 Genomic DNA. Translation: BAB19010.1 .
CR457116 mRNA. Translation: CAG33397.1 .
AC012181 Genomic DNA. No translation available.
BC000086 mRNA. Translation: AAH00086.1 .
BC008320 mRNA. Translation: AAH08320.1 .
BC009739 mRNA. Translation: AAH09739.1 .
BC032673 mRNA. Translation: AAH32673.1 .
CCDSi CCDS10771.1. [Q15011-1 ]
CCDS45492.1. [Q15011-2 ]
RefSeqi NP_001010989.1. NM_001010989.2. [Q15011-2 ]
NP_001259032.1. NM_001272103.1.
NP_055500.1. NM_014685.3. [Q15011-1 ]
UniGenei Hs.146393.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WGD NMR - A 10-90 [» ]
ProteinModelPortali Q15011.
SMRi Q15011. Positions 10-90.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115060. 28 interactions.
DIPi DIP-46662N.
IntActi Q15011. 10 interactions.
MINTi MINT-2867283.
STRINGi 9606.ENSP00000300302.

PTM databases

PhosphoSitei Q15011.

Polymorphism databases

DMDMi 3123034.

Proteomic databases

MaxQBi Q15011.
PaxDbi Q15011.
PRIDEi Q15011.

Protocols and materials databases

DNASUi 9709.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300302 ; ENSP00000300302 ; ENSG00000051108 . [Q15011-2 ]
ENST00000344114 ; ENSP00000340931 ; ENSG00000051108 . [Q15011-3 ]
ENST00000379792 ; ENSP00000369118 ; ENSG00000051108 . [Q15011-4 ]
ENST00000439977 ; ENSP00000409555 ; ENSG00000051108 . [Q15011-1 ]
GeneIDi 9709.
KEGGi hsa:9709.
UCSCi uc002eke.2. human. [Q15011-1 ]
uc002ekf.2. human. [Q15011-2 ]
uc031qwh.1. human. [Q15011-3 ]

Organism-specific databases

CTDi 9709.
GeneCardsi GC16P056965.
HGNCi HGNC:13744. HERPUD1.
HPAi CAB037041.
CAB037104.
HPA040754.
HPA041219.
MIMi 608070. gene.
neXtProti NX_Q15011.
PharmGKBi PA29252.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259558.
GeneTreei ENSGT00390000017671.
HOGENOMi HOG000252989.
HOVERGENi HBG051899.
InParanoidi Q15011.
KOi K14027.
OMAi PLYTRIT.
OrthoDBi EOG7QRQWK.
PhylomeDBi Q15011.
TreeFami TF324319.

Enzyme and pathway databases

Reactomei REACT_18355. ATF4 activates genes.

Miscellaneous databases

ChiTaRSi HERPUD1. human.
EvolutionaryTracei Q15011.
GeneWikii HERPUD1.
GenomeRNAii 9709.
NextBioi 36487.
PROi Q15011.
SOURCEi Search...

Gene expression databases

Bgeei Q15011.
CleanExi HS_HERPUD1.
ExpressionAtlasi Q15011. baseline and differential.
Genevestigatori Q15011.

Family and domain databases

InterProi IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00240. ubiquitin. 1 hit.
[Graphical view ]
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress."
    Kokame K., Agarwala K.L., Kato H., Miyata T.
    J. Biol. Chem. 275:32846-32853(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
    Tissue: Umbilical vein endothelial cell.
  2. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. Yu W., Gibbs R.A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. "Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response."
    Kokame K., Kato H., Miyata T.
    J. Biol. Chem. 276:9199-9205(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 3).
    Tissue: Brain, Eye, Placenta and Testis.
  8. "Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid beta-protein."
    Sai X., Kawamura Y., Kokame K., Yamaguchi H., Shiraishi H., Suzuki R., Suzuki T., Kawaichi M., Miyata T., Kitamura T., De Strooper B., Yanagisawa K., Komano H.
    J. Biol. Chem. 277:12915-12920(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSEN1 AND PSEN2.
  9. "The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway."
    van Laar T., Schouten T., Hoogervorst E., van Eck M., van der Eb A.J., Terleth C.
    FEBS Lett. 469:123-131(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Skin fibroblast.
  10. "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway."
    Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., Koning F., Kloetzel P.-M., Seeger M.
    J. Mol. Biol. 354:1021-1027(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SYVN1.
  11. "Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element."
    Liang G., Audas T.E., Li Y., Cockram G.P., Dean J.D., Martyn A.C., Kokame K., Lu R.
    Mol. Cell. Biol. 26:7999-8010(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. Cited for: INTERACTION WITH UBXN6.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Solution structure of the UBL-domain of HERP."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 10-90.

Entry informationi

Entry nameiHERP1_HUMAN
AccessioniPrimary (citable) accession number: Q15011
Secondary accession number(s): E9PGD1
, O60644, Q6IAN8, Q96D92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 143 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

Miscellaneous

Although the precise topology is not known, experimental data suggest that both the N- and C-termini face the cytosol.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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