Q02040 (AK17A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	695 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell activation Non-traceable author statement Ref.2. Source: UniProtKB RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of RNA splicing Inferred from mutant phenotype Ref.10. Source: UniProtKB regulation of transcription, DNA-templated Non-traceable author statement Ref.2. Source: UniProtKB signal transduction Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	nuclear speck Inferred from direct assay Ref.8. Source: UniProtKB nucleus Inferred from direct assay Ref.10. Source: UniProtKB spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Inferred from direct assay PubMed 22681889. Source: UniProtKB protein binding Inferred from physical interaction Ref.8. Source: IntAct protein kinase A binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ZRANB2	O95218	4	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 695	695	A-kinase anchor protein 17A		PRO_0000022692
Regions
	Domain	147 – 256	110	RRM
	Region	83 – 112	30	PKA-RI and PKA-RII subunit binding domain
	Region	425 – 454	30	PKA-RI-alpha subunit binding domain
	Compositional bias	587 – 695	109	Arg-rich
Amino acid modifications
	Modified residue	537	1	Phosphoserine Ref.7 Ref.11
	Modified residue	633	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	385 – 445	61	AVKLR…ILLSK → VGGSLCSRQPRPGCPQCPPL KCGRRHGAVSPPAAAVATKP ALMPRMTAPSREGVALVCRS R in isoform 3.		VSP_024947
	Alternative sequence	385	1	A → L in isoform 2.		VSP_004490
	Alternative sequence	386 – 695	310	Missing in isoform 2.		VSP_004491
	Alternative sequence	446 – 695	250	Missing in isoform 3.		VSP_024948
	Natural variant	194	1	P → S. Ref.4 Corresponds to variant rs17852504 [ dbSNP | Ensembl ].		VAR_055353
Experimental info
	Mutagenesis	438 – 439	2	LL → PP: Abolishes binding to PKA-RI; when associated with 445-P-P-446. Ref.10
	Mutagenesis	445 – 446	2	KK → PP: Abolishes binding to PKA-RI; when associated with 438-P-P-439. Ref.10
	Sequence conflict	443	1	L → Q in AAA36187. Ref.2
	Sequence conflict	500	1	P → A in AAA61303. Ref.1
	Sequence conflict	500	1	P → A in AAI10497. Ref.4
	Sequence conflict	502	1	H → P in AAA36187. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 639E88ECA8006CF2	FASTA	695	80,735
	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
	Isoform 2 [UniParc]. Checksum: 4C1E253616C969A6	FASTA	385	45,248
	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 RKLLLAQRNL QSIRLIAELL SRAKL
	Isoform 3 [UniParc]. Checksum: 049E8E08BF58DF27	FASTA	445	51,409
	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 SRAKVGGSLC SRQPRPGCPQ CPPLKCGRRH GAVSPPAAAV 430 440 ATKPALMPRM TAPSREGVAL VCRSR

References

	« Hide 'large scale' referencesShow '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. , 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.
CCDS	CCDS14116.1. [Q02040-1]
PIR	A46419. I54325.
RefSeq	NP_005079.2. NM_005088.2. [Q02040-1]
UniGene	Hs.522572.
3D structure databases
ProteinModelPortal	Q02040.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	113860. 6 interactions.
IntAct	Q02040. 4 interactions.
MINT	MINT-1443812.
PTM databases
PhosphoSite	Q02040.
Polymorphism databases
DMDM	146291102.
Proteomic databases
MaxQB	Q02040.
PaxDb	Q02040.
PRIDE	Q02040.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000313871; ENSP00000324827; ENSG00000197976. [Q02040-1] ENST00000474361; ENSP00000435479; ENSG00000197976. [Q02040-2]
GeneID	8227.
KEGG	hsa:8227.
UCSC	uc004cqa.3. human. [Q02040-1] uc010ncx.1. human. [Q02040-3]
Organism-specific databases
CTD	8227.
GeneCards	GC0XP001710.
HGNC	HGNC:18783. AKAP17A.
HPA	HPA043247.
MIM	312095. gene. 465000. gene.
neXtProt	NX_Q02040.
PharmGKB	PA162402969.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG271981.
InParanoid	Q02040.
KO	K13169.
OMA	HNHQFST.
OrthoDB	EOG7353WR.
PhylomeDB	Q02040.
TreeFam	TF320443.
Gene expression databases
Bgee	Q02040.
CleanEx	HS_SFRS17A.
Genevestigator	Q02040.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. [Graphical view]
ProtoNet	Search...
Other
GeneWiki	SFRS17A.
GenomeRNAi	8227.
NextBio	30970.
PRO	Q02040.
SOURCE	Search...

Entry information

Entry name

AK17A_HUMAN

Accession

Primary (citable) accession number: Q02040
Secondary accession number(s): Q02832 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.