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Q92688

- AN32B_HUMAN

UniProt

Q92688 - AN32B_HUMAN

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Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member B

Gene

ANP32B

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

Functioni

Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity By similarity. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome.By similarity1 Publication

GO - Molecular functioni

  1. histone binding Source: UniProt
  2. RNA polymerase binding Source: UniProt

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProt
  2. inner ear development Source: Ensembl
  3. negative regulation of cell differentiation Source: UniProt
  4. nucleosome assembly Source: UniProt
  5. palate development Source: Ensembl
  6. positive regulation of protein export from nucleus Source: UniProt
  7. vasculature development Source: Ensembl
  8. ventricular system development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic leucine-rich nuclear phosphoprotein 32 family member B
Alternative name(s):
Acidic protein rich in leucines
Putative HLA-DR-associated protein I-2
Short name:
PHAPI2
Silver-stainable protein SSP29
Gene namesi
Name:ANP32B
Synonyms:APRIL, PHAPI2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:16677. ANP32B.

Subcellular locationi

Isoform 1 : Nucleus
Note: Accumulates in the nuclei at the S phase.By similarity
Isoform 2 : Cytoplasm
Note: Lacks a nuclear localization signal.

GO - Cellular componenti

  1. cytoplasm Source: UniProt
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24812.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Acidic leucine-rich nuclear phosphoprotein 32 family member BPRO_0000137595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861N6-acetyllysine1 Publication
Modified residuei244 – 2441Phosphothreonine4 Publications

Post-translational modificationi

Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92688.
PaxDbiQ92688.
PRIDEiQ92688.

PTM databases

PhosphoSiteiQ92688.

Miscellaneous databases

PMAP-CutDBQ92688.

Expressioni

Tissue specificityi

Expressed in heart, lung, pancreas, prostate and in spleen, thymus and placenta.1 Publication

Gene expression databases

BgeeiQ92688.
CleanExiHS_ANP32B.
ExpressionAtlasiQ92688. baseline and differential.
GenevestigatoriQ92688.

Interactioni

Subunit structurei

Monomer. Interacts with histones H3 and H4.1 Publication

Protein-protein interaction databases

BioGridi115795. 34 interactions.
IntActiQ92688. 13 interactions.
STRINGi9606.ENSP00000345848.

Structurei

Secondary structure

1
251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119
Helixi16 – 183
Beta strandi20 – 234
Helixi39 – 435
Beta strandi46 – 527
Beta strandi68 – 736
Helixi82 – 865
Beta strandi92 – 943
Beta strandi96 – 994
Helixi104 – 1096
Beta strandi117 – 1193
Helixi124 – 1263
Helixi131 – 1366
Beta strandi157 – 1593

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ELLNMR-A1-161[»]
2RR6NMR-A1-161[»]
ProteinModelPortaliQ92688.
SMRiQ92688. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92688.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati16 – 4025LRR 11 PublicationAdd
BLAST
Repeati43 – 6422LRR 21 PublicationAdd
BLAST
Repeati65 – 8420LRR 31 PublicationAdd
BLAST
Repeati89 – 11022LRR 41 PublicationAdd
BLAST
Domaini123 – 16139LRRCTAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi146 – 251106Asp/Glu-rich (highly acidic)Add
BLAST

Domaini

Histone binding is mediated by the concave surface of the LRR region.

Sequence similaritiesi

Belongs to the ANP32 family.Curated
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG322008.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiQ92688.
OMAiDEVSGEX.
OrthoDBiEOG7TJ3KH.
PhylomeDBiQ92688.
TreeFamiTF317206.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92688-1) [UniParc]FASTAAdd to Basket

Also known as: Anp32b1, PHAPI2b

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
MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI
60 70 80 90 100
NVGLISVSNL PKLPKLKKLE LSENRIFGGL DMLAEKLPNL THLNLSGNKL
110 120 130 140 150
KDISTLEPLK KLECLKSLDL FNCEVTNLND YRESVFKLLP QLTYLDGYDR
160 170 180 190 200
EDQEAPDSDA EVDGVDEEEE DEEGEDEEDE DDEDGEEEEF DEEDDEDEDV
210 220 230 240 250
EGDEDDDEVS EEEEEFGLDE EDEDEDEDEE EEEGGKGEKR KRETDDEGED

D
Length:251
Mass (Da):28,788
Last modified:February 1, 1997 - v1
Checksum:i93A1AADF8EDE7D53
GO
Isoform 2 (identifier: Q92688-2) [UniParc]FASTAAdd to Basket

Also known as: Anp32b2, PHAPI2b

The sequence of this isoform differs from the canonical sequence as follows:
     196-251: Missing.

Note: No canonical donor splice site.

Show »
Length:195
Mass (Da):22,277
Checksum:iC504A0E604F16F73
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22Missing in CAA69265. (PubMed:9473664)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei196 – 25156Missing in isoform 2. 1 PublicationVSP_019304Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y07569 mRNA. Translation: CAA68855.1.
U70439 mRNA. Translation: AAB37579.1.
Y07969 mRNA. Translation: CAA69265.1.
Y07570 mRNA. Translation: CAA68856.1.
AK313733 mRNA. Translation: BAG36474.1.
AL354726 Genomic DNA. Translation: CAI15260.1.
CH471105 Genomic DNA. Translation: EAW58865.1.
BC013003 mRNA. Translation: AAH13003.1.
BC019658 mRNA. Translation: AAH19658.1.
CCDSiCCDS6732.1. [Q92688-1]
RefSeqiNP_006392.1. NM_006401.2. [Q92688-1]
UniGeneiHs.730654.

Genome annotation databases

EnsembliENST00000339399; ENSP00000345848; ENSG00000136938. [Q92688-1]
GeneIDi10541.
KEGGihsa:10541.
UCSCiuc004aya.3. human. [Q92688-1]

Polymorphism databases

DMDMi26390818.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y07569 mRNA. Translation: CAA68855.1 .
U70439 mRNA. Translation: AAB37579.1 .
Y07969 mRNA. Translation: CAA69265.1 .
Y07570 mRNA. Translation: CAA68856.1 .
AK313733 mRNA. Translation: BAG36474.1 .
AL354726 Genomic DNA. Translation: CAI15260.1 .
CH471105 Genomic DNA. Translation: EAW58865.1 .
BC013003 mRNA. Translation: AAH13003.1 .
BC019658 mRNA. Translation: AAH19658.1 .
CCDSi CCDS6732.1. [Q92688-1 ]
RefSeqi NP_006392.1. NM_006401.2. [Q92688-1 ]
UniGenei Hs.730654.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ELL NMR - A 1-161 [» ]
2RR6 NMR - A 1-161 [» ]
ProteinModelPortali Q92688.
SMRi Q92688. Positions 1-161.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115795. 34 interactions.
IntActi Q92688. 13 interactions.
STRINGi 9606.ENSP00000345848.

PTM databases

PhosphoSitei Q92688.

Polymorphism databases

DMDMi 26390818.

Proteomic databases

MaxQBi Q92688.
PaxDbi Q92688.
PRIDEi Q92688.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339399 ; ENSP00000345848 ; ENSG00000136938 . [Q92688-1 ]
GeneIDi 10541.
KEGGi hsa:10541.
UCSCi uc004aya.3. human. [Q92688-1 ]

Organism-specific databases

CTDi 10541.
GeneCardsi GC09P100745.
HGNCi HGNC:16677. ANP32B.
neXtProti NX_Q92688.
PharmGKBi PA24812.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322008.
GeneTreei ENSGT00560000077130.
HOGENOMi HOG000007361.
HOVERGENi HBG053102.
InParanoidi Q92688.
OMAi DEVSGEX.
OrthoDBi EOG7TJ3KH.
PhylomeDBi Q92688.
TreeFami TF317206.

Miscellaneous databases

ChiTaRSi ANP32B. human.
EvolutionaryTracei Q92688.
GeneWikii ANP32B.
GenomeRNAii 10541.
NextBioi 39993.
PMAP-CutDB Q92688.
PROi Q92688.

Gene expression databases

Bgeei Q92688.
CleanExi HS_ANP32B.
ExpressionAtlasi Q92688. baseline and differential.
Genevestigatori Q92688.

Family and domain databases

InterProi IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view ]
SMARTi SM00446. LRRcap. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Vaesen M., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning and partial characterization of a new silver-stainable protein."
    Zhu L., Henning D., Valdez B.C.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Expression analysis and chromosomal mapping of a novel human gene, APRIL, encoding an acidic protein rich in leucines."
    Mencinger M., Panagopoulos I., Contreras J.A., Mitelman F., Aman P.
    Biochim. Biophys. Acta 1395:176-180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Pancreas.
  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 1).
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] (ISOFORM 1).
    Tissue: Muscle and Testis.
  8. "The Anp32 family of proteins containing leucine-rich repeats."
    Matilla A., Radrizzani M.
    Cerebellum 4:7-18(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain."
    Tochio N., Umehara T., Munemasa Y., Suzuki T., Sato S., Tsuda K., Koshiba S., Kigawa T., Nagai R., Yokoyama S.
    J. Mol. Biol. 401:97-114(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-161, FUNCTION, SUBUNIT, INTERACTION WITH HISTONES H3 AND H4, LEUCINE-RICH REPEATS.

Entry informationi

Entry nameiAN32B_HUMAN
AccessioniPrimary (citable) accession number: Q92688
Secondary accession number(s): B2R9C7
, O00655, P78458, P78459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 132 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3