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Q02040 (AK17A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A-kinase anchor protein 17A

Short name=AKAP-17A
Alternative name(s):
721P
B-lymphocyte antigen
Protein XE7
Protein kinase A-anchoring protein 17A
Short name=PRKA17A
Splicing factor, arginine/serine-rich 17A
Gene names
Name:AKAP17A
Synonyms:CXYorf3, DXYS155E, SFRS17A, XE7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Splice factor regulating alternative splice site selection for certain mRNA precursors. Mediates regulation of pre-mRNA splicing in a PKA-dependent manner. Ref.8 Ref.10

Subunit structure

Monomer. Component of the spliceosome. Interacts with ZRANB2 and SFRS1/ASF through its Arg/Ser-rich domain. Interacts with RI and RII subunits of PKA. Ref.5 Ref.8 Ref.10

Subcellular location

Nucleus speckle Ref.8 Ref.10.

Tissue specificity

Widely expressed. Found in heart, brain, lung, liver, skeletal muscle, kidney and pancreas. Expressed in activated B-cells and placenta. Expressed in all cell lines tested including Jurkat-TAg, U-937 and HEK293 cells. Ref.10

Domain

RI-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Ref.10

Miscellaneous

The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Caution

Was originally (Ref.2) thought to be a cell surface protein involved in B-cell activation.

Sequence caution

The sequence AAA36187.1 differs from that shown. Reason: Frameshift at position 461.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZRANB2O952184EBI-1042725,EBI-1051583

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q02040-1)

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.
Isoform 2 (identifier: Q02040-2)

The sequence of this isoform differs from the canonical sequence as follows:
     385-385: A → L
     386-695: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: Q02040-3)

The sequence of this isoform differs from the canonical sequence as follows:
     385-445: AVKLREQEQK...ERLLSILLSK → VGGSLCSRQP...EGVALVCRSR
     446-695: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 695695A-kinase anchor protein 17A
PRO_0000022692

Regions

Domain147 – 256110RRM
Region83 – 11230PKA-RI and PKA-RII subunit binding domain
Region425 – 45430PKA-RI-alpha subunit binding domain
Compositional bias587 – 695109Arg-rich

Amino acid modifications

Modified residue5371Phosphoserine Ref.7 Ref.11
Modified residue6331Phosphoserine Ref.11

Natural variations

Alternative sequence385 – 44561AVKLR…ILLSK → VGGSLCSRQPRPGCPQCPPL KCGRRHGAVSPPAAAVATKP ALMPRMTAPSREGVALVCRS R in isoform 3.
VSP_024947
Alternative sequence3851A → L in isoform 2.
VSP_004490
Alternative sequence386 – 695310Missing in isoform 2.
VSP_004491
Alternative sequence446 – 695250Missing in isoform 3.
VSP_024948
Natural variant1941P → S. Ref.4
Corresponds to variant rs17852504 [ dbSNP | Ensembl ].
VAR_055353

Experimental info

Mutagenesis438 – 4392LL → PP: Abolishes binding to PKA-RI; when associated with 445-P-P-446. Ref.10
Mutagenesis445 – 4462KK → PP: Abolishes binding to PKA-RI; when associated with 438-P-P-439. Ref.10
Sequence conflict4431L → Q in AAA36187. Ref.2
Sequence conflict5001P → A in AAA61303. Ref.1
Sequence conflict5001P → A in AAI10497. Ref.4
Sequence conflict5021H → P in AAA36187. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 639E88ECA8006CF2

FASTA69580,735
        10         20         30         40         50         60 
MAAATIVHDT SEAVELCPAY GLYLKPITKM TISVALPQLK QPGKSISNWE VMERLKGMVQ 

        70         80         90        100        110        120 
NHQFSTLRIS KSTMDFIRFE GEVENKSLVK SFLACLDGKT IKLSGFSDIL KVRAAEFKID 

       130        140        150        160        170        180 
FPTRHDWDSF FRDAKDMNET LPGERPDTIH LEGLPCKWFA LKESGSEKPS EDVLVKVFEK 

       190        200        210        220        230        240 
FGEIRNVDIP MLDPYREEMT GRNFHTFSFG GHLNFEAYVQ YREYMGFIQA MSALRGMKLM 

       250        260        270        280        290        300 
YKGEDGKAVA CNIKVSFDST KHLSDASIKK RQLERQKLQE LEQQREEQKR REKEAEERQR 

       310        320        330        340        350        360 
AEERKQKELE ELERERKREE KLRKREQKQR DRELRRNQKK LEKLQAEEQK QLQEKIKLEE 

       370        380        390        400        410        420 
RKLLLAQRNL QSIRLIAELL SRAKAVKLRE QEQKEEKLRL QQQEERRRLQ EAELRRVEEE 

       430        440        450        460        470        480 
KERALGLQRK ERELRERLLS ILLSKKPDDS HTHDELGVAH ADLLQPVLDI LQTVSSGCVS 

       490        500        510        520        530        540 
ATTLHPLGGQ PPAGAPKESP AHPEADGAPK SVNGSVAEEA PCKEVQSSCR VVPEDGSPEK 

       550        560        570        580        590        600 
RCPGGVLSCI PDNNQQPKGI PACEQNVSRK DTRSEQDKCN REPSKGRGRA TGDGLADRHK 

       610        620        630        640        650        660 
RERSRARRAS SREDGRPRKE RRPHKKHAYK DDSPRRRSTS PDHTRSRRSH SKDRHRRERS 

       670        680        690 
RERRGSASRK HSRHRRRSER SRSRSPSRHR STWNR 

« Hide

Isoform 2 [UniParc].

Checksum: 4C1E253616C969A6
Show »

FASTA38545,248
Isoform 3 [UniParc].

Checksum: 049E8E08BF58DF27
Show »

FASTA44551,409

References

« Hide 'large scale' references
[1]"Structure and expression of the human pseudoautosomal gene XE7."
Ellison J.W., Ramos C., Yen P.H., Shapiro L.J.
Hum. Mol. Genet. 1:691-696(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning and sequencing of a trophoblast-endothelial-activated lymphocyte surface protein: cDNA sequence and genomic structure."
Voland J.R., Wyzykowski R.J., Huang M., Dutton R.W.
Proc. Natl. Acad. Sci. U.S.A. 89:10425-10429(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 3), VARIANT SER-194.
Tissue: Blood.
[5]"Large-scale proteomic analysis of the human spliceosome."
Rappsilber J., Ryder U., Lamond A.I., Mann M.
Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH THE SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[7]"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 SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265."
Mangs A.H., Speirs H.J.L., Goy C., Adams D.J., Markus M.A., Morris B.J.
Nucleic Acids Res. 34:4976-4986(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZRANB2 AND SFRS1.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Splicing factor arginine/serine-rich 17A (SFRS17A) is an A-kinase anchoring protein that targets protein kinase A to splicing factor compartments."
Jarnaess E., Stokka A.J., Kvissel A.K., Skalhegg B.S., Torgersen K.M., Scott J.D., Carlson C.R., Tasken K.
J. Biol. Chem. 284:35154-35164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, MUTAGENESIS OF 438-LEU-LEU-439 AND 445-LYS-LYS-446.
[11]"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-537 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L03426 mRNA. Translation: AAA61303.1.
L03426 mRNA. Translation: AAA61304.1.
M99578 mRNA. Translation: AAA36187.1. Frameshift.
AL683807 Genomic DNA. Translation: CAI41499.1.
AL683807 Genomic DNA. Translation: CAI41501.1.
BC028151 mRNA. Translation: AAH28151.1.
BC110496 mRNA. Translation: AAI10497.1.
BC110497 mRNA. Translation: AAI10498.1.
CCDSCCDS14116.1. [Q02040-1]
PIRA46419.
I54325.
RefSeqNP_005079.2. NM_005088.2. [Q02040-1]
UniGeneHs.522572.

3D structure databases

ProteinModelPortalQ02040.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113860. 6 interactions.
IntActQ02040. 4 interactions.
MINTMINT-1443812.

PTM databases

PhosphoSiteQ02040.

Polymorphism databases

DMDM146291102.

Proteomic databases

MaxQBQ02040.
PaxDbQ02040.
PRIDEQ02040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313871; ENSP00000324827; ENSG00000197976. [Q02040-1]
ENST00000474361; ENSP00000435479; ENSG00000197976. [Q02040-2]
GeneID8227.
KEGGhsa:8227.
UCSCuc004cqa.3. human. [Q02040-1]
uc010ncx.1. human. [Q02040-3]

Organism-specific databases

CTD8227.
GeneCardsGC0XP001710.
HGNCHGNC:18783. AKAP17A.
HPAHPA043247.
MIM312095. gene.
465000. gene.
neXtProtNX_Q02040.
PharmGKBPA162402969.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271981.
InParanoidQ02040.
KOK13169.
OMAHNHQFST.
OrthoDBEOG7353WR.
PhylomeDBQ02040.
TreeFamTF320443.

Gene expression databases

BgeeQ02040.
CleanExHS_SFRS17A.
GenevestigatorQ02040.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSFRS17A.
GenomeRNAi8227.
NextBio30970.
PROQ02040.
SOURCESearch...

Entry information

Entry nameAK17A_HUMAN
AccessionPrimary (citable) accession number: Q02040
Secondary accession number(s): Q02832 expand/collapse secondary AC list , Q2TB98, Q5JQ74, Q5JQ76, Q8N6U9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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

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 X

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