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Q9H2H8

- PPIL3_HUMAN

UniProt

Q9H2H8 - PPIL3_HUMAN

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Protein

Peptidyl-prolyl cis-trans isomerase-like 3

Gene

PPIL3

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. May be involved in pre-mRNA splicing.

Catalytic activityi

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

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. mRNA splicing, via spliceosome Source: UniProtKB
  2. protein folding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase-like 3 (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin J
Short name:
CyPJ
Cyclophilin-like protein PPIL3
Rotamase PPIL3
Gene namesi
Name:PPIL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9262. PPIL3.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33589.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 161160Peptidyl-prolyl cis-trans isomerase-like 3PRO_0000064166Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9H2H8.
PaxDbiQ9H2H8.
PRIDEiQ9H2H8.

PTM databases

PhosphoSiteiQ9H2H8.

Expressioni

Tissue specificityi

Ubiquitous. Detected at low levels.1 Publication

Gene expression databases

BgeeiQ9H2H8.
CleanExiHS_PPIL3.
ExpressionAtlasiQ9H2H8. baseline and differential.
GenevestigatoriQ9H2H8.

Organism-specific databases

HPAiHPA040765.

Interactioni

Subunit structurei

Identified in the spliceosome C complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VP3Q991523EBI-751051,EBI-1776808From a different organism.

Protein-protein interaction databases

BioGridi119820. 19 interactions.
IntActiQ9H2H8. 3 interactions.
MINTiMINT-3063495.
STRINGi9606.ENSP00000286175.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi10 – 167Combined sources
Turni18 – 203Combined sources
Helixi22 – 3312Combined sources
Turni34 – 396Combined sources
Beta strandi44 – 463Combined sources
Turni47 – 493Combined sources
Beta strandi50 – 534Combined sources
Beta strandi58 – 614Combined sources
Beta strandi86 – 894Combined sources
Beta strandi92 – 954Combined sources
Beta strandi101 – 1066Combined sources
Helixi109 – 1113Combined sources
Turni112 – 1143Combined sources
Beta strandi117 – 1237Combined sources
Helixi125 – 1328Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi148 – 1558Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XYHX-ray2.60A1-161[»]
2OJUX-ray2.40A/B1-161[»]
2OK3X-ray2.00A1-161[»]
ProteinModelPortaliQ9H2H8.
SMRiQ9H2H8. Positions 1-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H2H8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 154153PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiQ9H2H8.
KOiK12734.
OMAiCEMESRC.
OrthoDBiEOG769ZKZ.
PhylomeDBiQ9H2H8.
TreeFamiTF352224.

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: Q9H2H8-1) [UniParc]FASTAAdd to Basket

Also known as: PPIL3b

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
MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC IFHRNIKGFM
60 70 80 90 100
VQTGDPTGTG RGGNSIWGKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ
110 120 130 140 150
FFITYGKQPH LDMKYTVFGK VIDGLETLDE LEKLPVNEKT YRPLNDVHIK
160
DITIHANPFA Q
Length:161
Mass (Da):18,155
Last modified:March 1, 2001 - v1
Checksum:i5FE190D7858B07D4
GO
Isoform 2 (identifier: Q9H2H8-2) [UniParc]FASTAAdd to Basket

Also known as: PPIL3a

The sequence of this isoform differs from the canonical sequence as follows:
     27-58: NFLALCASNYYNGCIFHRNIKGFMVQTGDPTG → MESRCVPQAGVQWRDLGSLQPPPPGFKQVFCLSLPR

Show »
Length:165
Mass (Da):18,627
Checksum:iA533E5F757C18934
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 622RG → KR in AAO64723. 1 PublicationCurated
Sequence conflicti65 – 651S → V in AAO64723. 1 PublicationCurated
Sequence conflicti78 – 781Y → I in AAO64723. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461D → E.1 Publication
Corresponds to variant rs7562391 [ dbSNP | Ensembl ].
VAR_023417

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei27 – 5832NFLAL…GDPTG → MESRCVPQAGVQWRDLGSLQ PPPPGFKQVFCLSLPR in isoform 2. 2 PublicationsVSP_015468Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF251049 mRNA. Translation: AAK34939.1.
AF271652 mRNA. Translation: AAG44766.1.
AF146799 mRNA. Translation: AAO64723.1.
AK027315 mRNA. Translation: BAB55036.1.
AC005037 Genomic DNA. Translation: AAY14723.1.
BC007693 mRNA. Translation: AAH07693.1.
CCDSiCCDS2332.1. [Q9H2H8-2]
CCDS2333.1. [Q9H2H8-1]
RefSeqiNP_115861.1. NM_032472.3. [Q9H2H8-2]
NP_570981.1. NM_130906.2. [Q9H2H8-1]
XP_005246708.1. XM_005246651.2. [Q9H2H8-2]
XP_005246709.1. XM_005246652.2. [Q9H2H8-1]
UniGeneiHs.121076.

Genome annotation databases

EnsembliENST00000286175; ENSP00000286175; ENSG00000240344. [Q9H2H8-2]
ENST00000392283; ENSP00000376107; ENSG00000240344. [Q9H2H8-1]
ENST00000409449; ENSP00000387012; ENSG00000240344. [Q9H2H8-2]
GeneIDi53938.
KEGGihsa:53938.
UCSCiuc002uwh.3. human. [Q9H2H8-1]
uc002uwi.3. human. [Q9H2H8-2]

Polymorphism databases

DMDMi73921766.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF251049 mRNA. Translation: AAK34939.1 .
AF271652 mRNA. Translation: AAG44766.1 .
AF146799 mRNA. Translation: AAO64723.1 .
AK027315 mRNA. Translation: BAB55036.1 .
AC005037 Genomic DNA. Translation: AAY14723.1 .
BC007693 mRNA. Translation: AAH07693.1 .
CCDSi CCDS2332.1. [Q9H2H8-2 ]
CCDS2333.1. [Q9H2H8-1 ]
RefSeqi NP_115861.1. NM_032472.3. [Q9H2H8-2 ]
NP_570981.1. NM_130906.2. [Q9H2H8-1 ]
XP_005246708.1. XM_005246651.2. [Q9H2H8-2 ]
XP_005246709.1. XM_005246652.2. [Q9H2H8-1 ]
UniGenei Hs.121076.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XYH X-ray 2.60 A 1-161 [» ]
2OJU X-ray 2.40 A/B 1-161 [» ]
2OK3 X-ray 2.00 A 1-161 [» ]
ProteinModelPortali Q9H2H8.
SMRi Q9H2H8. Positions 1-160.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119820. 19 interactions.
IntActi Q9H2H8. 3 interactions.
MINTi MINT-3063495.
STRINGi 9606.ENSP00000286175.

PTM databases

PhosphoSitei Q9H2H8.

Polymorphism databases

DMDMi 73921766.

Proteomic databases

MaxQBi Q9H2H8.
PaxDbi Q9H2H8.
PRIDEi Q9H2H8.

Protocols and materials databases

DNASUi 53938.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286175 ; ENSP00000286175 ; ENSG00000240344 . [Q9H2H8-2 ]
ENST00000392283 ; ENSP00000376107 ; ENSG00000240344 . [Q9H2H8-1 ]
ENST00000409449 ; ENSP00000387012 ; ENSG00000240344 . [Q9H2H8-2 ]
GeneIDi 53938.
KEGGi hsa:53938.
UCSCi uc002uwh.3. human. [Q9H2H8-1 ]
uc002uwi.3. human. [Q9H2H8-2 ]

Organism-specific databases

CTDi 53938.
GeneCardsi GC02M201737.
HGNCi HGNC:9262. PPIL3.
HPAi HPA040765.
MIMi 615811. gene.
neXtProti NX_Q9H2H8.
PharmGKBi PA33589.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0652.
GeneTreei ENSGT00760000119072.
HOGENOMi HOG000065981.
HOVERGENi HBG001065.
InParanoidi Q9H2H8.
KOi K12734.
OMAi CEMESRC.
OrthoDBi EOG769ZKZ.
PhylomeDBi Q9H2H8.
TreeFami TF352224.

Enzyme and pathway databases

BRENDAi 5.2.1.8. 2681.

Miscellaneous databases

ChiTaRSi PPIL3. human.
EvolutionaryTracei Q9H2H8.
GeneWikii PPIL3.
GenomeRNAii 53938.
NextBioi 56240.
PROi Q9H2H8.
SOURCEi Search...

Gene expression databases

Bgeei Q9H2H8.
CleanExi HS_PPIL3.
ExpressionAtlasi Q9H2H8. baseline and differential.
Genevestigatori Q9H2H8.

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. "Molecular cloning and characterization of a novel peptidylprolyl isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain."
    Zhou Z., Ying K., Dai J., Tang R., Wang W., Huang Y., Zhao W., Xie Y., Mao Y.
    Cytogenet. Cell Genet. 92:231-236(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. Ding J.B., Yu L., Zhao S.Y.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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: Embryo.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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), VARIANT GLU-146.
    Tissue: Placenta.
  6. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family."
    Huang L.-L., Zhao X.-M., Huang C.-Q., Yu L., Xia Z.-X.
    Acta Crystallogr. D 61:316-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiPPIL3_HUMAN
AccessioniPrimary (citable) accession number: Q9H2H8
Secondary accession number(s): Q86WF9, Q96IA9, Q9BXZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 115 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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