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Protein

Ankyrin repeat domain-containing protein 2

Gene

ANKRD2

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

Functioni

Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress.2 Publications

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • protein kinase B binding Source: UniProtKB
  • RNA polymerase II sequence-specific DNA binding transcription factor binding Source: MGI
  • structural constituent of muscle Source: UniProtKB
  • titin binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

SIGNORiQ9GZV1.

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin repeat domain-containing protein 2
Alternative name(s):
Skeletal muscle ankyrin repeat protein
Short name:
hArpp
Gene namesi
Name:ANKRD2
Synonyms:ARPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:495. ANKRD2.

Subcellular locationi

  • CytoplasmmyofibrilsarcomereI band By similarity
  • Cytoplasmcytosol
  • Nucleus
  • NucleusPML body

  • Note: In the sarcoplasm of differentiated striated muscle cells, where it is cytosolic and enriched in the I band. In nucleus and PML bodies of proliferating and undifferentiated myoblasts. Associates with the euchromatin in the nucleus of myocytes upon muscle stress.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • euchromatin Source: UniProtKB
  • I band Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: HPA
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
  • sarcomere Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991S → A: Loss of interaction and phosphorylation by PKB/AKT2, loss of translocation to the nucleus and loss of function in myocyte differentiation. 1 Publication

Organism-specific databases

PharmGKBiPA24804.

Polymorphism and mutation databases

BioMutaiANKRD2.
DMDMi182676433.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Ankyrin repeat domain-containing protein 2PRO_0000066897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphoserine; by PKB/AKT21 Publication

Post-translational modificationi

Phosphorylation at Ser-99 by PKB/AKT2 in response to oxidative stress induces translocation to the nucleus and negatively regulates myoblast differentiation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9GZV1.
MaxQBiQ9GZV1.
PaxDbiQ9GZV1.
PeptideAtlasiQ9GZV1.
PRIDEiQ9GZV1.

PTM databases

iPTMnetiQ9GZV1.
PhosphoSiteiQ9GZV1.

Expressioni

Tissue specificityi

Mostly expressed in skeletal and cardiac muscles. Found in slow fibers. Also expressed in kidney, but to a lower extent (at protein level).2 Publications

Gene expression databases

BgeeiQ9GZV1.
CleanExiHS_ANKRD2.
ExpressionAtlasiQ9GZV1. baseline and differential.
GenevisibleiQ9GZV1. HS.

Organism-specific databases

HPAiHPA040842.
HPA040884.

Interactioni

Subunit structurei

Interacts with ID3; both proteins cooperate in myoblast differentiation (By similarity). Interacts with TTN/titin. Interacts (via ANK repeats) with TCAP; the interaction is direct. Interacts with TJP1 (via PDZ domains). Interacts with PML; the interaction is direct. Interacts with p53/TP53. Interacts with YBX1. Interacts with AKT2.By similarity4 Publications

GO - Molecular functioni

  • protein kinase B binding Source: UniProtKB
  • RNA polymerase II sequence-specific DNA binding transcription factor binding Source: MGI
  • titin binding Source: GO_Central

Protein-protein interaction databases

BioGridi117669. 8 interactions.
STRINGi9606.ENSP00000306163.

Structurei

3D structure databases

ProteinModelPortaliQ9GZV1.
SMRiQ9GZV1. Positions 150-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati147 – 17630ANK 1Add
BLAST
Repeati180 – 20930ANK 2Add
BLAST
Repeati213 – 24230ANK 3Add
BLAST
Repeati246 – 27530ANK 4Add
BLAST
Repeati279 – 30830ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 120116May mediate interaction with PML, p53/TP53 and YBX1Add
BLAST

Sequence similaritiesi

Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129743.
HOVERGENiHBG071561.
InParanoidiQ9GZV1.
OMAiRGDARQK.
OrthoDBiEOG7FJH17.
PhylomeDBiQ9GZV1.
TreeFamiTF331650.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9GZV1-1) [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
MAKAPSWAGV GALAYKAPEA LWPAEAVMDG TMEDSEAVQR ATALIEQRLA
60 70 80 90 100
QEEENEKLRG DARQKLPMDL LVLEDEKHHG AQSAALQKVK GQERVRKTSL
110 120 130 140 150
DLRREIIDVG GIQNLIELRK KRKQKKRDAL AASHEPPPEP EEITGPVDEE
160 170 180 190 200
TFLKAAVEGK MKVIEKFLAD GGSADTCDQF RRTALHRASL EGHMEILEKL
210 220 230 240 250
LDNGATVDFQ DRLDCTAMHW ACRGGHLEVV KLLQSHGADT NVRDKLLSTP
260 270 280 290 300
LHVAVRTGQV EIVEHFLSLG LEINARDREG DTALHDAVRL NRYKIIKLLL
310 320 330 340 350
LHGADMMTKN LAGKTPTDLV QLWQADTRHA LEHPEPGAEH NGLEGPNDSG
360
RETPQPVPAQ
Length:360
Mass (Da):39,859
Last modified:April 8, 2008 - v3
Checksum:iE88FC3FA242D0739
GO
Isoform 2 (identifier: Q9GZV1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     246-278: Missing.

Note: No experimental confirmation available.
Show »
Length:327
Mass (Da):36,193
Checksum:i8F62DAC9B5DB86B4
GO

Sequence cautioni

The sequence AK056990 differs from that shown. Reason: Erroneous termination at position 210. Translated as Gln.Curated
The sequence BAB60958.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAC19411.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAC19412.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAE47432.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491L → S in CAB99416 (PubMed:10873377).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621A → T.4 Publications
Corresponds to variant rs7094973 [ dbSNP | Ensembl ].
VAR_042498

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei246 – 27833Missing in isoform 2. 1 PublicationVSP_000269Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ304804 Genomic DNA. Translation: CAC19411.1. Different initiation.
AJ304805 mRNA. Translation: CAC19412.1. Different initiation.
AJ583444 mRNA. Translation: CAE47432.1. Different initiation.
AK056990 mRNA. No translation available.
AL355315 Genomic DNA. No translation available.
AL359388 Genomic DNA. No translation available.
BC020817 mRNA. Translation: AAH20817.2.
BC107759 mRNA. Translation: AAI07760.1.
AB058599 mRNA. Translation: BAB60958.1. Different initiation.
AJ249975 mRNA. Translation: CAB99416.1.
CCDSiCCDS44468.1. [Q9GZV1-2]
CCDS7466.1. [Q9GZV1-1]
PIRiJC7713.
RefSeqiNP_001123453.1. NM_001129981.2. [Q9GZV1-2]
NP_001278147.1. NM_001291218.1.
NP_001278148.1. NM_001291219.1.
NP_065082.2. NM_020349.3. [Q9GZV1-1]
UniGeneiHs.73708.

Genome annotation databases

EnsembliENST00000298808; ENSP00000298808; ENSG00000165887. [Q9GZV1-2]
ENST00000307518; ENSP00000306163; ENSG00000165887. [Q9GZV1-1]
GeneIDi26287.
KEGGihsa:26287.
UCSCiuc001knw.5. human. [Q9GZV1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ304804 Genomic DNA. Translation: CAC19411.1. Different initiation.
AJ304805 mRNA. Translation: CAC19412.1. Different initiation.
AJ583444 mRNA. Translation: CAE47432.1. Different initiation.
AK056990 mRNA. No translation available.
AL355315 Genomic DNA. No translation available.
AL359388 Genomic DNA. No translation available.
BC020817 mRNA. Translation: AAH20817.2.
BC107759 mRNA. Translation: AAI07760.1.
AB058599 mRNA. Translation: BAB60958.1. Different initiation.
AJ249975 mRNA. Translation: CAB99416.1.
CCDSiCCDS44468.1. [Q9GZV1-2]
CCDS7466.1. [Q9GZV1-1]
PIRiJC7713.
RefSeqiNP_001123453.1. NM_001129981.2. [Q9GZV1-2]
NP_001278147.1. NM_001291218.1.
NP_001278148.1. NM_001291219.1.
NP_065082.2. NM_020349.3. [Q9GZV1-1]
UniGeneiHs.73708.

3D structure databases

ProteinModelPortaliQ9GZV1.
SMRiQ9GZV1. Positions 150-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117669. 8 interactions.
STRINGi9606.ENSP00000306163.

PTM databases

iPTMnetiQ9GZV1.
PhosphoSiteiQ9GZV1.

Polymorphism and mutation databases

BioMutaiANKRD2.
DMDMi182676433.

Proteomic databases

EPDiQ9GZV1.
MaxQBiQ9GZV1.
PaxDbiQ9GZV1.
PeptideAtlasiQ9GZV1.
PRIDEiQ9GZV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298808; ENSP00000298808; ENSG00000165887. [Q9GZV1-2]
ENST00000307518; ENSP00000306163; ENSG00000165887. [Q9GZV1-1]
GeneIDi26287.
KEGGihsa:26287.
UCSCiuc001knw.5. human. [Q9GZV1-1]

Organism-specific databases

CTDi26287.
GeneCardsiANKRD2.
HGNCiHGNC:495. ANKRD2.
HPAiHPA040842.
HPA040884.
MIMi610734. gene.
neXtProtiNX_Q9GZV1.
PharmGKBiPA24804.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129743.
HOVERGENiHBG071561.
InParanoidiQ9GZV1.
OMAiRGDARQK.
OrthoDBiEOG7FJH17.
PhylomeDBiQ9GZV1.
TreeFamiTF331650.

Enzyme and pathway databases

SIGNORiQ9GZV1.

Miscellaneous databases

GeneWikiiANKRD2.
GenomeRNAii26287.
PROiQ9GZV1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZV1.
CleanExiHS_ANKRD2.
ExpressionAtlasiQ9GZV1. baseline and differential.
GenevisibleiQ9GZV1. HS.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 25-360 (ISOFORM 1), VARIANT THR-62, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  2. "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules."
    Miller M.K., Bang M.-L., Witt C.C., Labeit D., Trombitas C., Watanabe K., Granzier H., McElhinny A.S., Gregorio C.C., Labeit S.
    J. Mol. Biol. 333:951-964(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TTN, VARIANT THR-62.
    Tissue: Heart.
  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 1), VARIANT THR-62.
    Tissue: Skeletal muscle.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-360 (ISOFORM 2).
    Tissue: Skeletal muscle.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-360 (ISOFORM 1), TISSUE SPECIFICITY, VARIANT THR-62.
  7. "Identification of Ankrd2, a novel skeletal muscle gene coding for a stretch-responsive ankyrin-repeat protein."
    Kemp T.J., Sadusky T.J., Saltisi F., Carey N., Moss J., Yang S.Y., Sassoon D.A., Goldspink G., Coulton G.R.
    Genomics 66:229-241(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-150.
    Tissue: Skeletal muscle.
  8. "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle."
    Kojic S., Medeot E., Guccione E., Krmac H., Zara I., Martinelli V., Valle G., Faulkner G.
    J. Mol. Biol. 339:313-325(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML; TCAP; TP53/P53 AND YBX1, SUBCELLULAR LOCATION.
  9. "Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic differentiation upon cellular exposure to H(2)O(2)."
    Cenni V., Bavelloni A., Beretti F., Tagliavini F., Manzoli L., Lattanzi G., Maraldi N.M., Cocco L., Marmiroli S.
    Mol. Biol. Cell 22:2946-2956(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-99 BY PKB/AKT2, MUTAGENESIS OF SER-99, INTERACTION WITH AKT2, SUBCELLULAR LOCATION.
  10. "Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling network of striated muscle."
    Belgrano A., Rakicevic L., Mittempergher L., Campanaro S., Martinelli V.C., Mouly V., Valle G., Kojic S., Faulkner G.
    PLoS ONE 6:E25519-E25519(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TJP1.

Entry informationi

Entry nameiANKR2_HUMAN
AccessioniPrimary (citable) accession number: Q9GZV1
Secondary accession number(s): Q3B778
, Q5T456, Q70EZ9, Q8WUD7, Q96MG0, Q9NQC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: April 8, 2008
Last modified: July 6, 2016
This is version 134 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. 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.