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P35232

- PHB_HUMAN

UniProt

P35232 - PHB_HUMAN

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Protein

Prohibitin

Gene

PHB

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

Functioni

Prohibitin inhibits DNA synthesis. It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging.1 Publication

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. histone deacetylase binding Source: BHF-UCL
  3. transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  1. cellular response to interleukin-6 Source: BHF-UCL
  2. DNA replication Source: UniProtKB-KW
  3. histone deacetylation Source: UniProtKB
  4. negative regulation of androgen receptor signaling pathway Source: BHF-UCL
  5. negative regulation of cell growth Source: BHF-UCL
  6. negative regulation of cell proliferation Source: BHF-UCL
  7. negative regulation of glucocorticoid receptor signaling pathway Source: BHF-UCL
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
  9. negative regulation of transcription by competitive promoter binding Source: BHF-UCL
  10. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  11. osteoblast differentiation Source: UniProt
  12. positive regulation of transcription, DNA-templated Source: UniProtKB
  13. progesterone receptor signaling pathway Source: BHF-UCL
  14. regulation of apoptotic process Source: UniProtKB
  15. regulation of transcription, DNA-templated Source: UniProtKB
  16. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA synthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Prohibitin
Gene namesi
Name:PHB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:8912. PHB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: HGNC
  4. membrane Source: UniProtKB
  5. mitochondrial inner membrane Source: UniProtKB
  6. mitochondrion Source: LIFEdb
  7. nucleoplasm Source: UniProtKB
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA33251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272ProhibitinPRO_0000213878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281N6-acetyllysineBy similarity
Modified residuei186 – 1861N6-acetyllysineBy similarity
Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
Modified residuei249 – 2491PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35232.
PaxDbiP35232.
PeptideAtlasiP35232.
PRIDEiP35232.

2D gel databases

DOSAC-COBS-2DPAGEP35232.
OGPiP35232.
REPRODUCTION-2DPAGEIPI00017334.
P35232.
SWISS-2DPAGEP35232.
UCD-2DPAGEP35232.

PTM databases

PhosphoSiteiP35232.

Expressioni

Tissue specificityi

Widely expressed in different tissues.

Developmental stagei

Levels of expression in fibroblasts decrease heterogeneously during cellular aging.1 Publication

Inductioni

Expression increases approximately 3-fold upon entry into G1 phase compared with other phases of the cell cycle. Also induced following inhibition of mitochondrial protein synthesis by thiamphenicol.1 Publication

Gene expression databases

BgeeiP35232.
CleanExiHS_PHB.
ExpressionAtlasiP35232. baseline and differential.
GenevestigatoriP35232.

Organism-specific databases

HPAiHPA003280.

Interactioni

Subunit structurei

Interacts with PHB2. Interacts with STOML2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LONRF3Q496Y02EBI-354213,EBI-2690768
SKP2Q13309-22EBI-354213,EBI-7791408
XPO1O149802EBI-354213,EBI-355867

Protein-protein interaction databases

BioGridi111264. 78 interactions.
DIPiDIP-24248N.
IntActiP35232. 59 interactions.
MINTiMINT-1158239.
STRINGi9606.ENSP00000300408.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 185
Turni19 – 213
Beta strandi22 – 276
Beta strandi29 – 335
Beta strandi50 – 523
Beta strandi54 – 607
Beta strandi65 – 673
Turni87 – 893
Helixi99 – 11012
Helixi115 – 1184
Helixi123 – 14422
Helixi146 – 15510
Beta strandi157 – 1593
Beta strandi165 – 1673
Helixi172 – 19120
Helixi194 – 21118
Helixi212 – 2143
Turni217 – 2226
Helixi224 – 24017
Turni242 – 2465
Helixi247 – 2526

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LU7model-A1-272[»]
ProteinModelPortaliP35232.
SMRiP35232. Positions 61-194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili177 – 21135Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the prohibitin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0330.
GeneTreeiENSGT00550000074770.
HOGENOMiHOG000205692.
HOVERGENiHBG004457.
InParanoidiP35232.
KOiK17080.
OMAiIIFDVRS.
OrthoDBiEOG7V4B04.
PhylomeDBiP35232.
TreeFamiTF300095.

Family and domain databases

InterProiIPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view]
PANTHERiPTHR23222. PTHR23222. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSiPR00679. PROHIBITIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35232-1) [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
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV
60 70 80 90 100
GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA
110 120 130 140 150
SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV
160 170 180 190 200
SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV
210 220 230 240 250
EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ
260 270
LSRSRNITYL PAGQSVLLQL PQ
Length:272
Mass (Da):29,804
Last modified:February 1, 1994 - v1
Checksum:i915494273E342C76
GO
Isoform 2 (identifier: P35232-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-256: Missing.

Note: No experimental confirmation available.

Show »
Length:155
Mass (Da):17,018
Checksum:iFDFDE03209523798
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881V → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_006479
Natural varianti105 – 1051R → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_006480

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei140 – 256117Missing in isoform 2. 1 PublicationVSP_054922Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S85655 mRNA. Translation: AAB21614.1.
L14272 Genomic DNA. Translation: AAO18340.1.
BT007411 mRNA. Translation: AAP36079.1.
AK302258 mRNA. Translation: BAG63609.1.
AC091180 Genomic DNA. No translation available.
BC013401 mRNA. Translation: AAH13401.1.
BC095460 mRNA. Translation: AAH95460.1.
CCDSiCCDS11548.1. [P35232-1]
CCDS62244.1. [P35232-2]
PIRiI52690.
RefSeqiNP_001268425.1. NM_001281496.1. [P35232-1]
NP_001268426.1. NM_001281497.1. [P35232-2]
NP_001268644.1. NM_001281715.1. [P35232-1]
NP_002625.1. NM_002634.3. [P35232-1]
UniGeneiHs.514303.

Genome annotation databases

EnsembliENST00000300408; ENSP00000300408; ENSG00000167085. [P35232-1]
ENST00000511832; ENSP00000425035; ENSG00000167085. [P35232-2]
ENST00000614445; ENSP00000479488; ENSG00000167085. [P35232-1]
ENST00000617874; ENSP00000484113; ENSG00000167085. [P35232-1]
GeneIDi5245.
KEGGihsa:5245.
UCSCiuc002iox.1. human. [P35232-1]

Polymorphism databases

DMDMi464371.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S85655 mRNA. Translation: AAB21614.1 .
L14272 Genomic DNA. Translation: AAO18340.1 .
BT007411 mRNA. Translation: AAP36079.1 .
AK302258 mRNA. Translation: BAG63609.1 .
AC091180 Genomic DNA. No translation available.
BC013401 mRNA. Translation: AAH13401.1 .
BC095460 mRNA. Translation: AAH95460.1 .
CCDSi CCDS11548.1. [P35232-1 ]
CCDS62244.1. [P35232-2 ]
PIRi I52690.
RefSeqi NP_001268425.1. NM_001281496.1. [P35232-1 ]
NP_001268426.1. NM_001281497.1. [P35232-2 ]
NP_001268644.1. NM_001281715.1. [P35232-1 ]
NP_002625.1. NM_002634.3. [P35232-1 ]
UniGenei Hs.514303.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LU7 model - A 1-272 [» ]
ProteinModelPortali P35232.
SMRi P35232. Positions 61-194.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111264. 78 interactions.
DIPi DIP-24248N.
IntActi P35232. 59 interactions.
MINTi MINT-1158239.
STRINGi 9606.ENSP00000300408.

PTM databases

PhosphoSitei P35232.

Polymorphism databases

DMDMi 464371.

2D gel databases

DOSAC-COBS-2DPAGE P35232.
OGPi P35232.
REPRODUCTION-2DPAGE IPI00017334.
P35232.
SWISS-2DPAGE P35232.
UCD-2DPAGE P35232.

Proteomic databases

MaxQBi P35232.
PaxDbi P35232.
PeptideAtlasi P35232.
PRIDEi P35232.

Protocols and materials databases

DNASUi 5245.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300408 ; ENSP00000300408 ; ENSG00000167085 . [P35232-1 ]
ENST00000511832 ; ENSP00000425035 ; ENSG00000167085 . [P35232-2 ]
ENST00000614445 ; ENSP00000479488 ; ENSG00000167085 . [P35232-1 ]
ENST00000617874 ; ENSP00000484113 ; ENSG00000167085 . [P35232-1 ]
GeneIDi 5245.
KEGGi hsa:5245.
UCSCi uc002iox.1. human. [P35232-1 ]

Organism-specific databases

CTDi 5245.
GeneCardsi GC17M047481.
HGNCi HGNC:8912. PHB.
HPAi HPA003280.
MIMi 176705. gene.
neXtProti NX_P35232.
PharmGKBi PA33251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0330.
GeneTreei ENSGT00550000074770.
HOGENOMi HOG000205692.
HOVERGENi HBG004457.
InParanoidi P35232.
KOi K17080.
OMAi IIFDVRS.
OrthoDBi EOG7V4B04.
PhylomeDBi P35232.
TreeFami TF300095.

Miscellaneous databases

GeneWikii Prohibitin.
GenomeRNAii 5245.
NextBioi 20266.
PROi P35232.
SOURCEi Search...

Gene expression databases

Bgeei P35232.
CleanExi HS_PHB.
ExpressionAtlasi P35232. baseline and differential.
Genevestigatori P35232.

Family and domain databases

InterProi IPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view ]
PANTHERi PTHR23222. PTHR23222. 1 hit.
Pfami PF01145. Band_7. 1 hit.
[Graphical view ]
PRINTSi PR00679. PROHIBITIN.
SMARTi SM00244. PHB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human prohibitin gene located on chromosome 17q21 is mutated in sporadic breast cancer."
    Sato T., Saito H., Swensen J., Olifant A., Wood C., Danner D., Sakamoto T., Takita K., Kasumi F., Miki Y., Skolnick M., Nakamura Y.
    Cancer Res. 52:1643-1646(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-88 AND HIS-105.
    Tissue: Mammary gland.
  2. "The human prohibitin (PHB) gene family and its somatic mutations in human tumors."
    Sato T., Sakamoto T., Takita K., Saito H., Okui K., Nakamura Y.
    Genomics 17:762-764(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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: Testis.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    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: Lung and Muscle.
  7. Bienvenut W.V.
    Submitted (MAR-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 5-11; 84-93; 106-128; 134-143; 178-186 AND 209-219, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 75-83; 94-117; 134-143; 158-177; 220-253 AND 256-272, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  9. "Mammalian prohibitin proteins respond to mitochondrial stress and decrease during cellular senescence."
    Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H., Hall P.A., Wright E.G.
    Exp. Cell Res. 265:262-273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHB2, DEVELOPMENTAL STAGE, INDUCTION.
  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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function."
    Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.
    Mol. Cell. Biol. 31:3845-3856(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STOML2.

Entry informationi

Entry nameiPHB_HUMAN
AccessioniPrimary (citable) accession number: P35232
Secondary accession number(s): B4DY47, Q4VBQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 145 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 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

External Data

Dasty 3