SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q02040

- AK17A_HUMAN

UniProt

Q02040 - AK17A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
A-kinase anchor protein 17A
Gene
AKAP17A, CXYorf3, DXYS155E, SFRS17A, XE7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Splice factor regulating alternative splice site selection for certain mRNA precursors. Mediates regulation of pre-mRNA splicing in a PKA-dependent manner.2 Publications

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. protein kinase A binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. RNA splicing Source: UniProtKB-KW
  3. mRNA processing Source: UniProtKB-KW
  4. regulation of RNA splicing Source: UniProtKB
  5. regulation of transcription, DNA-templated Source: UniProtKB
  6. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:AKAP17A
Synonyms:CXYorf3, DXYS155E, SFRS17A, XE7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:18783. AKAP17A.

Subcellular locationi

Nucleus speckle 2 Publications

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi438 – 4392LL → PP: Abolishes binding to PKA-RI; when associated with 445-P-P-446. 1 Publication
Mutagenesisi445 – 4462KK → PP: Abolishes binding to PKA-RI; when associated with 438-P-P-439. 1 Publication

Organism-specific databases

PharmGKBiPA162402969.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 695695A-kinase anchor protein 17A
PRO_0000022692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei537 – 5371Phosphoserine2 Publications
Modified residuei633 – 6331Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02040.
PaxDbiQ02040.
PRIDEiQ02040.

PTM databases

PhosphoSiteiQ02040.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ02040.
CleanExiHS_SFRS17A.
GenevestigatoriQ02040.

Organism-specific databases

HPAiHPA043247.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ZRANB2O952184EBI-1042725,EBI-1051583

Protein-protein interaction databases

BioGridi113860. 7 interactions.
IntActiQ02040. 4 interactions.
MINTiMINT-1443812.

Structurei

3D structure databases

ProteinModelPortaliQ02040.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 256110RRM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 11230PKA-RI and PKA-RII subunit binding domain
Add
BLAST
Regioni425 – 45430PKA-RI-alpha subunit binding domain
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi587 – 695109Arg-rich
Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG271981.
InParanoidiQ02040.
KOiK13169.
OMAiHNHQFST.
OrthoDBiEOG7353WR.
PhylomeDBiQ02040.
TreeFamiTF320443.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q02040-1) [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

MAAATIVHDT SEAVELCPAY GLYLKPITKM TISVALPQLK QPGKSISNWE    50
VMERLKGMVQ NHQFSTLRIS KSTMDFIRFE GEVENKSLVK SFLACLDGKT 100
IKLSGFSDIL KVRAAEFKID FPTRHDWDSF FRDAKDMNET LPGERPDTIH 150
LEGLPCKWFA LKESGSEKPS EDVLVKVFEK FGEIRNVDIP MLDPYREEMT 200
GRNFHTFSFG GHLNFEAYVQ YREYMGFIQA MSALRGMKLM YKGEDGKAVA 250
CNIKVSFDST KHLSDASIKK RQLERQKLQE LEQQREEQKR REKEAEERQR 300
AEERKQKELE ELERERKREE KLRKREQKQR DRELRRNQKK LEKLQAEEQK 350
QLQEKIKLEE RKLLLAQRNL QSIRLIAELL SRAKAVKLRE QEQKEEKLRL 400
QQQEERRRLQ EAELRRVEEE KERALGLQRK ERELRERLLS ILLSKKPDDS 450
HTHDELGVAH ADLLQPVLDI LQTVSSGCVS ATTLHPLGGQ PPAGAPKESP 500
AHPEADGAPK SVNGSVAEEA PCKEVQSSCR VVPEDGSPEK RCPGGVLSCI 550
PDNNQQPKGI PACEQNVSRK DTRSEQDKCN REPSKGRGRA TGDGLADRHK 600
RERSRARRAS SREDGRPRKE RRPHKKHAYK DDSPRRRSTS PDHTRSRRSH 650
SKDRHRRERS RERRGSASRK HSRHRRRSER SRSRSPSRHR STWNR 695
Length:695
Mass (Da):80,735
Last modified:May 1, 2007 - v2
Checksum:i639E88ECA8006CF2
GO
Isoform 2 (identifier: Q02040-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:385
Mass (Da):45,248
Checksum:i4C1E253616C969A6
GO
Isoform 3 (identifier: Q02040-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:445
Mass (Da):51,409
Checksum:i049E8E08BF58DF27
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti194 – 1941P → S.1 Publication
Corresponds to variant rs17852504 [ dbSNP | Ensembl ].
VAR_055353

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei385 – 44561AVKLR…ILLSK → VGGSLCSRQPRPGCPQCPPL KCGRRHGAVSPPAAAVATKP ALMPRMTAPSREGVALVCRS R in isoform 3.
VSP_024947Add
BLAST
Alternative sequencei385 – 3851A → L in isoform 2.
VSP_004490
Alternative sequencei386 – 695310Missing in isoform 2.
VSP_004491Add
BLAST
Alternative sequencei446 – 695250Missing in isoform 3.
VSP_024948Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti443 – 4431L → Q in AAA36187. 1 Publication
Sequence conflicti500 – 5001P → A in AAA61303. 1 Publication
Sequence conflicti500 – 5001P → A in AAI10497. 1 Publication
Sequence conflicti502 – 5021H → P in AAA36187. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14116.1. [Q02040-1]
PIRiA46419.
I54325.
RefSeqiNP_005079.2. NM_005088.2. [Q02040-1]
UniGeneiHs.522572.

Genome annotation databases

EnsembliENST00000313871; ENSP00000324827; ENSG00000197976. [Q02040-1]
ENST00000474361; ENSP00000435479; ENSG00000197976. [Q02040-2]
GeneIDi8227.
KEGGihsa:8227.
UCSCiuc004cqa.3. human. [Q02040-1]
uc010ncx.1. human. [Q02040-3]

Polymorphism databases

DMDMi146291102.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14116.1. [Q02040-1 ]
PIRi A46419.
I54325.
RefSeqi NP_005079.2. NM_005088.2. [Q02040-1 ]
UniGenei Hs.522572.

3D structure databases

ProteinModelPortali Q02040.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113860. 7 interactions.
IntActi Q02040. 4 interactions.
MINTi MINT-1443812.

PTM databases

PhosphoSitei Q02040.

Polymorphism databases

DMDMi 146291102.

Proteomic databases

MaxQBi Q02040.
PaxDbi Q02040.
PRIDEi Q02040.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313871 ; ENSP00000324827 ; ENSG00000197976 . [Q02040-1 ]
ENST00000474361 ; ENSP00000435479 ; ENSG00000197976 . [Q02040-2 ]
GeneIDi 8227.
KEGGi hsa:8227.
UCSCi uc004cqa.3. human. [Q02040-1 ]
uc010ncx.1. human. [Q02040-3 ]

Organism-specific databases

CTDi 8227.
GeneCardsi GC0XP001710.
HGNCi HGNC:18783. AKAP17A.
HPAi HPA043247.
MIMi 312095. gene.
465000. gene.
neXtProti NX_Q02040.
PharmGKBi PA162402969.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271981.
InParanoidi Q02040.
KOi K13169.
OMAi HNHQFST.
OrthoDBi EOG7353WR.
PhylomeDBi Q02040.
TreeFami TF320443.

Miscellaneous databases

GeneWikii SFRS17A.
GenomeRNAii 8227.
NextBioi 30970.
PROi Q02040.
SOURCEi Search...

Gene expression databases

Bgeei Q02040.
CleanExi HS_SFRS17A.
Genevestigatori Q02040.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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].

Entry informationi

Entry nameiAK17A_HUMAN
AccessioniPrimary (citable) accession number: Q02040
Secondary accession number(s): Q02832
, Q2TB98, Q5JQ74, Q5JQ76, Q8N6U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 1, 2007
Last modified: September 3, 2014
This is version 131 of the entry and version 2 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

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

External Data

Dasty 3

Similar proteinsi