Reviewed, UniProtKB/Swiss-Prot Q92625 (ANS1A_HUMAN)

Names and origin

Protein names

Recommended name:
    Ankyrin repeat and SAM domain-containing protein 1A
Alternative name(s):
    Odin

Gene names

Name:	ANKS1A
Synonyms:	ANKS1, KIAA0229

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1134 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a negative role in growth factor receptor signaling pathways.
Subcellular location	Cytoplasm. 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. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Sequence similarities	Contains 6 ANK repeats. Contains 1 PID domain. Contains 2 SAM (sterile alpha motif) domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YWHAG	P61981	1	EBI-1048612,EBI-359832

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 1134	1133	Ankyrin repeat and SAM domain-containing protein 1A		PRO_0000066921
Regions
	Repeat	79 – 108	30	ANK 1
	Repeat	112 – 141	30	ANK 2
	Repeat	148 – 177	30	ANK 3
	Repeat	181 – 210	30	ANK 4
	Repeat	214 – 243	30	ANK 5
	Repeat	246 – 275	30	ANK 6
	Domain	696 – 762	67	SAM 1
	Domain	770 – 837	68	SAM 2
	Domain	936 – 1091	156	PID
	Compositional bias	2 – 55	54	Gly-rich
Amino acid modifications
	Modified residue	2	1	N-acetylglycine Ref.5
	Modified residue	318	1	Phosphothreonine Ref.8
	Modified residue	622	1	Phosphoserine Ref.8
	Modified residue	624	1	Phosphoserine By similarity
	Modified residue	626	1	Phosphoserine Ref.8
	Modified residue	628	1	Phosphoserine By similarity
	Modified residue	647	1	Phosphoserine Ref.8 Ref.10
	Modified residue	661	1	Phosphoserine Ref.8 Ref.10
	Modified residue	663	1	Phosphoserine Ref.6 Ref.10 Ref.11
	Modified residue	666	1	Phosphoserine By similarity
	Modified residue	677	1	Phosphoserine Ref.11
	Modified residue	887	1	Phosphoserine Ref.7
Natural variations
	Natural variant	355	1	A → D: dbSNP rs6930932.		VAR_048282
	Natural variant	694	1	L → S: dbSNP rs820085. Ref.1 Ref.3 Ref.4		VAR_021168

Sequences

	Sequence		Length	Mass (Da)
	Q92625-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: E519844AD56EE414	FASTA	1,134	123,108
	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

References

	« Hide 'large scale' referencesShow '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: 9039502] [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. , 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: 14574404] [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. , 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: 15489334] [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: 12439753] [Abstract] Cited for: PROTEIN SEQUENCE OF 540-564, ACETYLATION AT GLY-2, MASS SPECTROMETRY, CHARACTERIZATION. Tissue: Cervix carcinoma.
[6]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY. Tissue: Platelet.
[7]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-622; SER-626; SER-647 AND SER-661, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647; SER-661 AND SER-663, MASS SPECTROMETRY.
[11]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND SER-677, MASS SPECTROMETRY. Tissue: T-cell.

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.
IPI	IPI00395663.
RefSeq	NP_056060.2.
UniGene	Hs.656492
3D structure databases
SMR	Q92625. Positions 5-267, 72-289, 692-760, 766-861, 914-1067.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92625. 1 interaction.
STRING	Q92625.
PTM databases
PhosphoSite	Q92625.
Proteomic databases
PeptideAtlas	Q92625.
PRIDE	Q92625.
Genome annotation databases
Ensembl	ENST00000360359; ENSP00000353518; ENSG00000064999; Homo sapiens. [Genome view]
GeneID	23294.
KEGG	hsa:23294.
UCSC	uc003ojx.2. human.
Organism-specific databases
CTD	23294.
GeneCards	GC06P034966.
HGNC	HGNC:20961. ANKS1A.
MIM	608994. gene.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG446292.
HOVERGEN	Q92625.
InParanoid	Q92625.
OMA	CSIGKKR.
PhylomeDB	Q92625.
Gene expression databases
ArrayExpress	Q92625.
Bgee	Q92625.
CleanEx	HS_ANKS1A.
Genevestigator	Q92625.
GermOnline	ENSG00000064999. Homo sapiens.
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR011993. PH_type. IPR006020. PTyr_interaction_dom. IPR001660. SAM. IPR010993. SAM_homology. IPR013761. SAM_type. IPR021129. SAM_type1. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit. G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:1.10.150.50. SAM_type. 2 hits.
Pfam	PF00023. Ank. 6 hits. PF00640. PID. 1 hit. PF00536. SAM_1. 2 hits. [Graphical view]
SMART	SM00248. ANK. 6 hits. SM00462. PTB. 1 hit. SM00454. SAM. 2 hits. [Graphical view]
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 6 hits. PS01179. PID. 1 hit. PS50105. SAM_DOMAIN. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	45120.
SOURCE	Search...

Entry information

Entry name

ANS1A_HUMAN

Accession

Primary (citable) accession number: Q92625
Secondary accession number(s): A2RUC1 , Q5JYI9, Q5SYR2, Q86WQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 83 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.