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Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member E

Gene

ANP32E

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

Functioni

Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AFZ from the nucleosome: removes H2A.Z/H2AFZ from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AFZ in the nucleosome. May stabilize the evicted H2A.Z/H2AFZ-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis.1 Publication

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • phosphatase inhibitor activity Source: UniProtKB

GO - Biological processi

  • histone exchange Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic leucine-rich nuclear phosphoprotein 32 family member E
Alternative name(s):
LANP-like protein
Short name:
LANP-L
Gene namesi
Name:ANP32E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16673. ANP32E.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB
  • nucleus Source: UniProtKB
  • Swr1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi218 – 2225LSYLM → ASYAA in ANP32E-m1; abolished ability to interact with the H2A.Z/H2AFZ-H2B dimer. 1 Publication
Mutagenesisi232 – 2354DDDY → ADAA in ANP32E-m2; abolished ability to interact with the H2A.Z/H2AFZ-H2B dimer. 1 Publication

Organism-specific databases

PharmGKBiPA134880751.

Polymorphism and mutation databases

DMDMi30580363.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 268268Acidic leucine-rich nuclear phosphoprotein 32 family member EPRO_0000137599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Post-translational modificationi

Phosphorylated. The phosphorylation is nuclear localization signal (NLS)-dependent (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BTT0.
MaxQBiQ9BTT0.
PaxDbiQ9BTT0.
PeptideAtlasiQ9BTT0.
PRIDEiQ9BTT0.
TopDownProteomicsiQ9BTT0-1. [Q9BTT0-1]

PTM databases

iPTMnetiQ9BTT0.
PhosphoSiteiQ9BTT0.

Expressioni

Tissue specificityi

Expressed in peripheral blood leukocytes, colon, small intestine, prostate, thymus, spleen, skeletal muscle, liver and kidney.1 Publication

Gene expression databases

BgeeiQ9BTT0.
CleanExiHS_ANP32E.
ExpressionAtlasiQ9BTT0. baseline and differential.
GenevisibleiQ9BTT0. HS.

Organism-specific databases

HPAiCAB021114.

Interactioni

Subunit structurei

Interacts with the importin alpha KPNA1 and KPNA2 (By similarity). Component of a SWR1-like complex, composed of EP400, KAT5/TIP60, TRRAP, BRD8, RUVBL1, RUVBL2, ING3 and ANP32E; the complex does not contain SRCAP. Interacts with H2A.Z/H2AFZ.By similarity1 Publication

GO - Molecular functioni

  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123548. 30 interactions.
IntActiQ9BTT0. 7 interactions.
MINTiMINT-3061467.
STRINGi9606.ENSP00000324074.

Structurei

Secondary structure

1
268
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi218 – 2225Combined sources
Beta strandi223 – 2253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CAYX-ray1.48C215-240[»]
4NFTX-ray2.61E/F185-232[»]
ProteinModelPortaliQ9BTT0.
SMRiQ9BTT0. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 3821LRR 1Add
BLAST
Repeati43 – 6422LRR 2Add
BLAST
Repeati65 – 8723LRR 3Add
BLAST
Repeati89 – 11022LRR 4Add
BLAST
Domaini123 – 16139LRRCTAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 26854ZID domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi151 – 266116Asp/Glu-rich (highly acidic)Add
BLAST

Domaini

The H2A.Z-interacting domain (ZID) mediates a direct interaction with H2A.Z/H2AFZ.1 Publication

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

eggNOGiKOG2739. Eukaryota.
ENOG4111HZT. LUCA.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiQ9BTT0.
KOiK18648.
OMAiRCPNLTY.
OrthoDBiEOG7TJ3KH.
PhylomeDBiQ9BTT0.
TreeFamiTF317206.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BTT0-1) [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
MEMKKKINLE LRNRSPEEVT ELVLDNCLCV NGEIEGLNDT FKELEFLSMA
60 70 80 90 100
NVELSSLARL PSLNKLRKLE LSDNIISGGL EVLAEKCPNL TYLNLSGNKI
110 120 130 140 150
KDLSTVEALQ NLKNLKSLDL FNCEITNLED YRESIFELLQ QITYLDGFDQ
160 170 180 190 200
EDNEAPDSEE EDDEDGDEDD EEEEENEAGP PEGYEEEEEE EEEEDEDEDE
210 220 230 240 250
DEDEAGSELG EGEEEVGLSY LMKEEIQDEE DDDDYVEEGE EEEEEEEGGL
260
RGEKRKRDAE DDGEEEDD
Length:268
Mass (Da):30,692
Last modified:June 1, 2001 - v1
Checksum:i99D74AF4B59BF971
GO
Isoform 2 (identifier: Q9BTT0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-109: Missing.

Note: No experimental confirmation available.
Show »
Length:227
Mass (Da):26,321
Checksum:i059CB2D637B6C426
GO
Isoform 3 (identifier: Q9BTT0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: Gene prediction based on EST data.
Show »
Length:220
Mass (Da):25,125
Checksum:iC7564983F775F210
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1862Missing in AAL25814 (PubMed:12438741).Curated
Sequence conflicti185 – 1862Missing in BAC04505 (PubMed:14702039).Curated
Sequence conflicti185 – 1862Missing in BAG64448 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848Missing in isoform 3. CuratedVSP_047262Add
BLAST
Alternative sequencei69 – 10941Missing in isoform 2. 1 PublicationVSP_045618Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY057381 mRNA. Translation: AAL25814.1.
AK095228 mRNA. Translation: BAC04505.1.
AK092672 mRNA. Translation: BAC03942.1.
AK303392 mRNA. Translation: BAG64448.1.
AL832674 mRNA. No translation available.
AL138795 Genomic DNA. Translation: CAI22806.1.
AL138795 Genomic DNA. Translation: CAI22808.1.
CH471121 Genomic DNA. Translation: EAW53575.1.
CH471121 Genomic DNA. Translation: EAW53577.1.
BC003380 mRNA. Translation: AAH03380.1.
CCDSiCCDS44214.1. [Q9BTT0-2]
CCDS44215.1. [Q9BTT0-3]
CCDS946.1. [Q9BTT0-1]
RefSeqiNP_001129950.1. NM_001136478.3. [Q9BTT0-2]
NP_001129951.1. NM_001136479.2. [Q9BTT0-3]
NP_001267488.1. NM_001280559.1.
NP_001267489.1. NM_001280560.1.
NP_112182.1. NM_030920.4. [Q9BTT0-1]
UniGeneiHs.656466.

Genome annotation databases

EnsembliENST00000436748; ENSP00000393718; ENSG00000143401. [Q9BTT0-2]
ENST00000583931; ENSP00000463154; ENSG00000143401. [Q9BTT0-1]
ENST00000616917; ENSP00000481415; ENSG00000143401. [Q9BTT0-3]
GeneIDi81611.
KEGGihsa:81611.
UCSCiuc031uxy.2. human. [Q9BTT0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY057381 mRNA. Translation: AAL25814.1.
AK095228 mRNA. Translation: BAC04505.1.
AK092672 mRNA. Translation: BAC03942.1.
AK303392 mRNA. Translation: BAG64448.1.
AL832674 mRNA. No translation available.
AL138795 Genomic DNA. Translation: CAI22806.1.
AL138795 Genomic DNA. Translation: CAI22808.1.
CH471121 Genomic DNA. Translation: EAW53575.1.
CH471121 Genomic DNA. Translation: EAW53577.1.
BC003380 mRNA. Translation: AAH03380.1.
CCDSiCCDS44214.1. [Q9BTT0-2]
CCDS44215.1. [Q9BTT0-3]
CCDS946.1. [Q9BTT0-1]
RefSeqiNP_001129950.1. NM_001136478.3. [Q9BTT0-2]
NP_001129951.1. NM_001136479.2. [Q9BTT0-3]
NP_001267488.1. NM_001280559.1.
NP_001267489.1. NM_001280560.1.
NP_112182.1. NM_030920.4. [Q9BTT0-1]
UniGeneiHs.656466.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CAYX-ray1.48C215-240[»]
4NFTX-ray2.61E/F185-232[»]
ProteinModelPortaliQ9BTT0.
SMRiQ9BTT0. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123548. 30 interactions.
IntActiQ9BTT0. 7 interactions.
MINTiMINT-3061467.
STRINGi9606.ENSP00000324074.

PTM databases

iPTMnetiQ9BTT0.
PhosphoSiteiQ9BTT0.

Polymorphism and mutation databases

DMDMi30580363.

Proteomic databases

EPDiQ9BTT0.
MaxQBiQ9BTT0.
PaxDbiQ9BTT0.
PeptideAtlasiQ9BTT0.
PRIDEiQ9BTT0.
TopDownProteomicsiQ9BTT0-1. [Q9BTT0-1]

Protocols and materials databases

DNASUi81611.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000436748; ENSP00000393718; ENSG00000143401. [Q9BTT0-2]
ENST00000583931; ENSP00000463154; ENSG00000143401. [Q9BTT0-1]
ENST00000616917; ENSP00000481415; ENSG00000143401. [Q9BTT0-3]
GeneIDi81611.
KEGGihsa:81611.
UCSCiuc031uxy.2. human. [Q9BTT0-1]

Organism-specific databases

CTDi81611.
GeneCardsiANP32E.
HGNCiHGNC:16673. ANP32E.
HPAiCAB021114.
MIMi609611. gene.
neXtProtiNX_Q9BTT0.
PharmGKBiPA134880751.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2739. Eukaryota.
ENOG4111HZT. LUCA.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiQ9BTT0.
KOiK18648.
OMAiRCPNLTY.
OrthoDBiEOG7TJ3KH.
PhylomeDBiQ9BTT0.
TreeFamiTF317206.

Miscellaneous databases

ChiTaRSiANP32E. human.
GeneWikiiANP32E.
GenomeRNAii81611.
PROiQ9BTT0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BTT0.
CleanExiHS_ANP32E.
ExpressionAtlasiQ9BTT0. baseline and differential.
GenevisibleiQ9BTT0. HS.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel human gene (ANP32E alias LANPL) from human fetal brain."
    Jiang M., Ma Y., Ni X., Cao G., Ji C., Cheng H., Tang R., Xie Y., Mao Y.
    Cytogenet. Genome Res. 97:68-71(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "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] (ISOFORMS 1 AND 2).
    Tissue: Pulmonary artery, Thymus and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adipose tissue.
  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: Cervix.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 215-240 IN COMPLEX WITH HISTONES H2AFZ AND H2B, FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX, INTERACTION WITH H2AFZ, MUTAGENESIS OF 218-LEU--MET-222 AND 232-ASP--TYR-235.

Entry informationi

Entry nameiAN32E_HUMAN
AccessioniPrimary (citable) accession number: Q9BTT0
Secondary accession number(s): B4E0I6
, E9PEA6, Q5TB18, Q5TB20, Q8N1S4, Q8WWW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 140 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 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.