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Q92625 (ANS1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ankyrin repeat and SAM domain-containing protein 1A
Alternative name(s):
Odin
Gene names
Name:ANKS1A
Synonyms:ANKS1, KIAA0229, ODIN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1134 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction By similarity. Ref.6

Subunit structure

Interacts with EPHA8; EPHA8 kinase activity-independent but stimulated by EPHA8 ubiquitination By similarity. Interacts (via SAM domain) with EPHA2 (via SAM domain). Ref.15

Subcellular location

Cytoplasm. Cell projection By similarity. Note: Cytoplasmic before and after growth factor treatment.

Tissue specificity

Widely expressed (at protein level).

Post-translational modification

Phosphorylated on tyrosine residues in response to EGF and PDGF By similarity.

Sequence similarities

Contains 6 ANK repeats.

Contains 1 PID domain.

Contains 2 SAM (sterile alpha motif) domains.

Sequence caution

The sequence BAA13218.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 11341133Ankyrin repeat and SAM domain-containing protein 1A
PRO_0000066921

Regions

Repeat79 – 10830ANK 1
Repeat112 – 14130ANK 2
Repeat148 – 17730ANK 3
Repeat181 – 21030ANK 4
Repeat214 – 24330ANK 5
Repeat246 – 27530ANK 6
Domain696 – 76267SAM 1
Domain770 – 83768SAM 2
Domain936 – 1091156PID
Compositional bias2 – 5554Gly-rich

Amino acid modifications

Modified residue21N-acetylglycine Ref.5
Modified residue3181Phosphothreonine Ref.8
Modified residue6221Phosphoserine Ref.8
Modified residue6241Phosphoserine By similarity
Modified residue6261Phosphoserine By similarity
Modified residue6471Phosphoserine Ref.8 Ref.13
Modified residue6611Phosphoserine Ref.8 Ref.11 Ref.13
Modified residue6631Phosphoserine Ref.10 Ref.11 Ref.13

Natural variations

Natural variant3551A → D.
Corresponds to variant rs6930932 [ dbSNP | Ensembl ].
VAR_048282
Natural variant6941L → S. Ref.1 Ref.3 Ref.4 Ref.10
Corresponds to variant rs820085 [ dbSNP | Ensembl ].
VAR_021168

Secondary structure

.............. 1134
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92625 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: E519844AD56EE414

FASTA1,134123,108
        10         20         30         40         50         60 
MGKEQELLEA ARTGHLPAVE KLLSGKRLSS GFGGGGGGGS GGGGGGSGGG GGGLGSSSHP 

        70         80         90        100        110        120 
LSSLLSMWRG PNVNCVDSTG YTPLHHAALN GHKDVVEVLL RNDALTNVAD SKGCYPLHLA 

       130        140        150        160        170        180 
AWKGDAQIVR LLIHQGPSHT RVNEQNNDNE TALHCAAQYG HTEVVKVLLE ELTDPTMRNN 

       190        200        210        220        230        240 
KFETPLDLAA LYGRLEVVKM LLNAHPNLLS CNTKKHTPLH LAARNGHKAV VQVLLDAGMD 

       250        260        270        280        290        300 
SNYQTEMGSA LHEAALFGKT DVVQILLAAG TDVNIKDNHG LTALDTVREL PSQKSQQIAA 

       310        320        330        340        350        360 
LIEDHMTGKR STKEVDKTPP PQPPLISSMD SISQKSQGDV EKAVTELIID FDANAEEEGP 

       370        380        390        400        410        420 
YEALYNAISC HSLDSMASGR SSDQDSTNKE AEAAGVKPAG VRPRERPPPP AKPPPDEEEE 

       430        440        450        460        470        480 
DHIDKKYFPL TASEVLSMRP RIHGSAAREE DEHPYELLLT AETKKVVLVD GKTKDHRRSS 

       490        500        510        520        530        540 
SSRSQDSAEG QDGQVPEQFS GLLHGSSPVC EVGQDPFQLL CTAGQSHPDG SPQQGACHKA 

       550        560        570        580        590        600 
SMQLEETGVH APGASQPSAL DQSKRVGYLT GLPTTNSRSH PETLTHTASP HPGGAEEGDR 

       610        620        630        640        650        660 
SGARSRAPPT SKPKAELKLS RSLSKSDSDL LTCSPTEDAT MGSRSESLSN CSIGKKRLEK 

       670        680        690        700        710        720 
SPSFASEWDE IEKIMSSIGE GIDFSQERQK ISGLRTLEQS VGEWLESIGL QQYESKLLLN 

       730        740        750        760        770        780 
GFDDVHFLGS NVMEEQDLRD IGISDPQHRR KLLQAARSLP KVKALGYDGN SPPSVPSWLD 

       790        800        810        820        830        840 
SLGLQDYVHS FLSSGYSSID TVKNLWELEL VNVLKVQLLG HRKRIIASLA DRPYEEPPQK 

       850        860        870        880        890        900 
PPRFSQLRCQ DLLSQTSSPL SQNDSCTGRS ADLLLPPGDT GRRRHDSLHD PAAPSRAERF 

       910        920        930        940        950        960 
RIQEEHREAK LTLRPPSLAA PYAPVQSWQH QPEKLIFESC GYEANYLGSM LIKDLRGTES 

       970        980        990       1000       1010       1020 
TQDACAKMRK STEHMKKIPT IILSITYKGV KFIDASNKNV IAEHEIRNIS CAAQDPEDLC 

      1030       1040       1050       1060       1070       1080 
TFAYITKDLQ TSHHYCHVFS TVDVNLTYEI ILTLGQAFEV AYQLALQAQK SRATGASAAE 

      1090       1100       1110       1120       1130 
MIETKSSKPV PKPRVGVRKS ALEPPDMDQD AQSHASVSWV VDPKPDSKRS LSTN 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-694.
Tissue: Bone marrow.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-694.
[4]"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], VARIANT SER-694.
[5]"Cloning of a novel phosphotyrosine binding domain containing molecule, Odin, involved in signaling by receptor tyrosine kinases."
Pandey A., Blagoev B., Kratchmarova I., Fernandez M., Nielsen M., Kristiansen T.Z., Ohara O., Podtelejnikov A.V., Roche S., Lodish H.F., Mann M.
Oncogene 21:8029-8036(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 540-564, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION.
Tissue: Cervix carcinoma.
[6]"Identification of phosphotyrosine binding domain-containing proteins as novel downstream targets of the EphA8 signaling function."
Shin J., Gu C., Park E., Park S.
Mol. Cell. Biol. 27:8113-8126(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EFNA5-EPHA8 SIGNALING PATHWAY.
[7]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-622; SER-647 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, VARIANT [LARGE SCALE ANALYSIS] SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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 SER-661 AND SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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 SER-647; SER-661 AND SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor."
Mercurio F.A., Marasco D., Pirone L., Pedone E.M., Pellecchia M., Leone M.
Biochemistry 51:2136-2145(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 691-770, INTERACTION WITH EPHA2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86982 mRNA. Translation: BAA13218.1. Different initiation.
AL138721, AL033520, AL591002 Genomic DNA. Translation: CAI12437.1.
AL591002, AL033520, AL138721 Genomic DNA. Translation: CAI15138.1.
AL033520, AL138721, AL591002 Genomic DNA. Translation: CAI20281.1.
CH471081 Genomic DNA. Translation: EAX03804.1.
BC132832 mRNA. Translation: AAI32833.1.
RefSeqNP_056060.2. NM_015245.2.
UniGeneHs.656492.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LMRNMR-A691-770[»]
ProteinModelPortalQ92625.
SMRQ92625. Positions 3-362, 691-832, 933-1063.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116889. 13 interactions.
IntActQ92625. 5 interactions.
MINTMINT-1493202.
STRING9606.ENSP00000353518.

PTM databases

PhosphoSiteQ92625.

Polymorphism databases

DMDM62511243.

Proteomic databases

PaxDbQ92625.
PeptideAtlasQ92625.
PRIDEQ92625.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360359; ENSP00000353518; ENSG00000064999.
GeneID23294.
KEGGhsa:23294.
UCSCuc003ojx.4. human.

Organism-specific databases

CTD23294.
GeneCardsGC06P034857.
HGNCHGNC:20961. ANKS1A.
HPAHPA036768.
HPA036769.
MIM608994. gene.
neXtProtNX_Q92625.
PharmGKBPA134958476.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000033973.
HOVERGENHBG050506.
InParanoidQ92625.
OMATSCHSLD.
OrthoDBEOG78H3SN.
PhylomeDBQ92625.
TreeFamTF320582.

Gene expression databases

ArrayExpressQ92625.
BgeeQ92625.
CleanExHS_ANKS1A.
GenevestigatorQ92625.

Family and domain databases

Gene3D1.10.150.50. 2 hits.
1.25.40.20. 4 hits.
2.30.29.30. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamPF00023. Ank. 5 hits.
PF00640. PID. 1 hit.
PF00536. SAM_1. 2 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
SM00462. PTB. 1 hit.
SM00454. SAM. 2 hits.
[Graphical view]
SUPFAMSSF47769. SSF47769. 2 hits.
SSF48403. SSF48403. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS01179. PID. 1 hit.
PS50105. SAM_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANKS1A. human.
GeneWikiANKS1A.
GenomeRNAi23294.
NextBio45120.
PROQ92625.
SOURCESearch...

Entry information

Entry nameANS1A_HUMAN
AccessionPrimary (citable) accession number: Q92625
Secondary accession number(s): A2RUC1 expand/collapse secondary AC list , Q5JYI9, Q5SYR2, Q86WQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM