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O43447

- PPIH_HUMAN

UniProt

O43447 - PPIH_HUMAN

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Protein

Peptidyl-prolyl cis-trans isomerase H

Gene

PPIH

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

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone.3 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by cyclosporin A.

GO - Molecular functioni

  1. cyclosporin A binding Source: ProtInc
  2. peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
  3. ribonucleoprotein complex binding Source: BHF-UCL

GO - Biological processi

  1. mRNA splicing, via spliceosome Source: BHF-UCL
  2. positive regulation of viral genome replication Source: UniProtKB
  3. protein complex assembly Source: ProtInc
  4. protein folding Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase H (EC:5.2.1.8)
Short name:
PPIase H
Alternative name(s):
Rotamase H
Small nuclear ribonucleoprotein particle-specific cyclophilin H
Short name:
CypH
U-snRNP-associated cyclophilin SnuCyp-20
Short name:
USA-CYP
Gene namesi
Name:PPIH
Synonyms:CYP20, CYPH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14651. PPIH.

Subcellular locationi

Nucleus speckle 1 Publication. Cytoplasm 1 Publication
Note: Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. nuclear speck Source: BHF-UCL
  3. spliceosomal complex Source: BHF-UCL
  4. U4/U6 snRNP Source: BHF-UCL
  5. U4/U6 x U5 tri-snRNP complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi133 – 1331W → F: Abolishes inhibition by cyclosporin A. 1 Publication

Organism-specific databases

PharmGKBiPA33586.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 177176Peptidyl-prolyl cis-trans isomerase HPRO_0000064162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43447.
PaxDbiO43447.
PRIDEiO43447.

PTM databases

PhosphoSiteiO43447.

Expressioni

Gene expression databases

BgeeiO43447.
CleanExiHS_PPIH.
ExpressionAtlasiO43447. baseline and differential.
GenevestigatoriO43447.

Organism-specific databases

HPAiHPA059019.

Interactioni

Subunit structurei

Interacts directly with PRPF4. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Heterodimer with PRPF18.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRPF4O431722EBI-1055615,EBI-718395

Protein-protein interaction databases

BioGridi115728. 20 interactions.
IntActiO43447. 8 interactions.
MINTiMINT-270606.
STRINGi9606.ENSP00000306614.

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 198
Beta strandi22 – 3110
Turni33 – 353
Helixi37 – 4812
Beta strandi67 – 693
Turni70 – 723
Beta strandi73 – 764
Turni79 – 813
Beta strandi82 – 843
Beta strandi109 – 1124
Beta strandi124 – 1296
Helixi132 – 1343
Turni135 – 1373
Beta strandi140 – 1467
Helixi148 – 1558
Helixi161 – 1633
Beta strandi165 – 1673
Beta strandi169 – 1768

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZWX-ray2.00A1-177[»]
1QOIX-ray2.00A1-177[»]
ProteinModelPortaliO43447.
SMRiO43447. Positions 5-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43447.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 176163PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiO43447.
KOiK09567.
OMAiTPKFPDE.
OrthoDBiEOG79GT7W.
PhylomeDBiO43447.
TreeFamiTF312958.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43447-1) [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
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE
60 70 80 90 100
FRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF
110 120 130 140 150
KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV
160 170
MRKIENVPTG PNNKPKLPVV ISQCGEM
Length:177
Mass (Da):19,208
Last modified:June 1, 1998 - v1
Checksum:i566BCE6361E0F339
GO
Isoform 2 (identifier: O43447-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEF → MIAGDSDR

Note: No experimental confirmation available.

Show »
Length:134
Mass (Da):14,492
Checksum:iE55350B73F8A1C3B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151MAVAN…CTGEF → MIAGDSDR in isoform 2. 1 PublicationVSP_056587Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF016371 mRNA. Translation: AAC51927.1.
AF036331 mRNA. Translation: AAC60793.1.
AK294288 mRNA. Translation: BAH11725.1.
AC098484 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07155.1.
BC003412 mRNA. Translation: AAH03412.1.
CCDSiCCDS469.1. [O43447-1]
RefSeqiNP_006338.1. NM_006347.3.
XP_005270419.1. XM_005270362.1.
XP_005270421.1. XM_005270364.2.
XP_006710356.1. XM_006710293.1.
UniGeneiHs.256639.

Genome annotation databases

EnsembliENST00000304979; ENSP00000306614; ENSG00000171960. [O43447-1]
ENST00000372550; ENSP00000361630; ENSG00000171960. [O43447-2]
GeneIDi10465.
KEGGihsa:10465.
UCSCiuc001chq.3. human. [O43447-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF016371 mRNA. Translation: AAC51927.1 .
AF036331 mRNA. Translation: AAC60793.1 .
AK294288 mRNA. Translation: BAH11725.1 .
AC098484 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07155.1 .
BC003412 mRNA. Translation: AAH03412.1 .
CCDSi CCDS469.1. [O43447-1 ]
RefSeqi NP_006338.1. NM_006347.3.
XP_005270419.1. XM_005270362.1.
XP_005270421.1. XM_005270364.2.
XP_006710356.1. XM_006710293.1.
UniGenei Hs.256639.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MZW X-ray 2.00 A 1-177 [» ]
1QOI X-ray 2.00 A 1-177 [» ]
ProteinModelPortali O43447.
SMRi O43447. Positions 5-177.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115728. 20 interactions.
IntActi O43447. 8 interactions.
MINTi MINT-270606.
STRINGi 9606.ENSP00000306614.

Chemistry

DrugBanki DB00172. L-Proline.

PTM databases

PhosphoSitei O43447.

Proteomic databases

MaxQBi O43447.
PaxDbi O43447.
PRIDEi O43447.

Protocols and materials databases

DNASUi 10465.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304979 ; ENSP00000306614 ; ENSG00000171960 . [O43447-1 ]
ENST00000372550 ; ENSP00000361630 ; ENSG00000171960 . [O43447-2 ]
GeneIDi 10465.
KEGGi hsa:10465.
UCSCi uc001chq.3. human. [O43447-1 ]

Organism-specific databases

CTDi 10465.
GeneCardsi GC01P043097.
HGNCi HGNC:14651. PPIH.
HPAi HPA059019.
MIMi 606095. gene.
neXtProti NX_O43447.
PharmGKBi PA33586.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0652.
GeneTreei ENSGT00760000119072.
HOGENOMi HOG000065981.
HOVERGENi HBG001065.
InParanoidi O43447.
KOi K09567.
OMAi TPKFPDE.
OrthoDBi EOG79GT7W.
PhylomeDBi O43447.
TreeFami TF312958.

Miscellaneous databases

ChiTaRSi PPIH. human.
EvolutionaryTracei O43447.
GeneWikii PPIH.
GenomeRNAii 10465.
NextBioi 35462705.
PROi O43447.
SOURCEi Search...

Gene expression databases

Bgeei O43447.
CleanExi HS_PPIH.
ExpressionAtlasi O43447. baseline and differential.
Genevestigatori O43447.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs."
    Horowitz D.S., Kobayashi R., Krainer A.R.
    RNA 3:1374-1387(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 154-164, INTERACTION WITH PRPF3; PRPF4 AND U4/U6 SNRNPS.
    Tissue: Liver.
  2. "The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins."
    Teigelkamp S., Achsel T., Mundt C., Goethel S.-F., Cronshagen U., Lane W.S., Marahiel M., Luehrmann R.
    RNA 4:127-141(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 62-67; 71-81 AND 153-164, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE U4/U5/U6 TRI-SNRNP COMPLEX.
    Tissue: Liver.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Amygdala.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  7. "A cyclophilin functions in pre-mRNA splicing."
    Horowitz D.S., Lee E.J., Mabon S.A., Misteli T.
    EMBO J. 21:470-480(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TRP-133, INTERACTION WITH PRPF4 AND PRPF18.
  8. "The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
    Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
    RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin."
    Reidt U., Reuter K., Achsel T., Ingelfinger D., Luehrmann R., Ficner R.
    J. Biol. Chem. 275:7439-7442(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177.
  12. "Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide."
    Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R., Ficner R.
    J. Mol. Biol. 331:45-56(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4, FUNCTION.

Entry informationi

Entry nameiPPIH_HUMAN
AccessioniPrimary (citable) accession number: O43447
Secondary accession number(s): A6NNE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 1998
Last modified: October 29, 2014
This is version 130 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3