Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O75969 (AKAP3_HUMAN)

Last modified November 25, 2008. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    A-kinase anchor protein 3
Alternative name(s):
    Protein kinase A-anchoring protein 3
      Short name=PRKA3
    A-kinase anchor protein 110 kDa
      Short name=AKAP 110
    Sperm oocyte-binding protein
    Fibrousheathin-1
    Fibrousheathin I
    Fibrous sheath protein of 95 kDa
      Short name=FSP95
    Cancer/testis antigen 82
      Short name=CT82
Gene names
Name: AKAP3
Synonyms: AKAP110, SOB1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length853 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction.

Subunit structure

Interacts with ROPN1 AND ROPN1L.

Subcellular location

AcrosomeBy similarity. Note= Ribs of the fibrous sheath in the principal piece of the sperm tail. Dorsal margin of the acrosomal segment.

Tissue specificity

Testis specific; only expressed in spermatids.

Domain

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

Post-translational modification

Phosphorylated on tyrosine residues.

Sequence similarities

Belongs to the AKAP110 family.

Ontologies

Keywords

   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processacrosome reaction Ref.3

Traceable author statement. Source: ProtInc

cell motion Ref.3

Traceable author statement. Source: ProtInc

   Cellular componentacrosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein kinase A binding Ref.3

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 853853A-kinase anchor protein 3
PRO_0000064526

Regions

Region124 – 13714PKA-RII subunit binding domain

Amino acid modifications

Modified residue2051Phosphoserine
Modified residue2081Phosphoserine
Modified residue4031Phosphoserine
Modified residue4041Phosphotyrosine
Modified residue4401Phosphoserine
Modified residue6121Phosphoserine
Modified residue6351Phosphoserine
Modified residue6361Phosphoserine

Natural variations

Natural variant8311R → C in a colorectal cancer sample; somatic mutation.
VAR_036428

Experimental info

Mutagenesis1311L → P: Abolishes interaction with ROPN1
Sequence conflict1181G → E AA sequence Ref.2
Sequence conflict2721E → D in AAD21218. Ref.1
Sequence conflict2821S → G in AAC35854. Ref.2
Sequence conflict4671K → N in AAC35854. Ref.2
Sequence conflict5001I → T in AAC35854. Ref.2
Sequence conflict5971F → S AA sequence Ref.2
Sequence conflict7001S → L in AAC35854. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O75969-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 8374FFF1009BEBEC

FASTA85394,736
        10         20         30         40         50         60 
MSEKVDWLQS QNGVCKVDVY SPGDNQAQDW KMDTSTDPVR VLSWLRRDLE KSTAEFQDVR 

        70         80         90        100        110        120 
FKPGESFGGE TSNSGDPHKG FSVDYYNTTT KGTPERLHFE MTHKEIPCQG PRAQLGNGSS 

       130        140        150        160        170        180 
VDEVSFYANR LTNLVIAMAR KEINEKIDGS ENKCVYQSLY MGNEPTPTKS LSKIASELVN 

       190        200        210        220        230        240 
ETVSACSRNA APDKAPGSGD RVSGSSQSPP NLKYKSTLKI KESTKERQGP DDKPPSKKSF 

       250        260        270        280        290        300 
FYKEVFESRN GDYAREGGRF FPRERKRFRG QERPDDFTAS VSEGIMTYAN SVVSDMMVSI 

       310        320        330        340        350        360 
MKTLKIQVKD TTIATILLKK VLLKHAKEVV SDLIDSFLRN LHSVTGTLMT DTQFVSAVKR 

       370        380        390        400        410        420 
TVFSHGSQKA TDIMDAMLRK LYNVMFAKKV PEHVRKAQDK AESYSLISMK GMGDPKNRNV 

       430        440        450        460        470        480 
NFAMKSETKL REKMYSEPKS EEETCAKTLG EHIIKEGLTL WHKSQQKECK SLGFQHAAFE 

       490        500        510        520        530        540 
APNTQRKPAS DISFEYPEDI GNLSLPPYPP EKPENFMYDS DSWAKDLIVS ALLLIQYHLA 

       550        560        570        580        590        600 
QGGRRDARSF VEAAGTTNFP ANEPPVAPDE SCLKSAPIVG DQEQAEKKDL RSVFFNFIRN 

       610        620        630        640        650        660 
LLSETIFKRD QSPEPKVPEQ PVKEDRKLCE RPLASSPPRL YEDDETPGAL SGLTKMAVSQ 

       670        680        690        700        710        720 
IDGHMSGQMV EHLMNSVMKL CVIIAKSCDA SLAELGDDKS GDASRLTSAF PDSLYECLPA 

       730        740        750        760        770        780 
KGTGSAEAVL QNAYQAIHNE MRGTSGQPPE GCAAPTVIVS NHNLTDTVQN KQLQAVLQWV 

       790        800        810        820        830        840 
AASELNVPIL YFAGDDEGIQ EKLLQLSAAA VDKGCSVGEV LQSVLRYEKE RQLNEAVGNV 

       850 
TPLQLLDWLM VNL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of SOB1, a new testis-specific cDNA encoding a human sperm protein probably involved in oocyte recognition."
Lefevre A., Duquenne C., Rousseau-Merck M.-F., Rogier E., Finaz C.
Biochem. Biophys. Res. Commun. 259:60-66(1999) [PubMed: 10334916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Testis.
[2]"FSP95, a testis-specific 95-kilodalton fibrous sheath antigen that undergoes tyrosine phosphorylation in capacitated human spermatozoa."
Mandal A., Naaby-Hansen S., Wolkowicz M.J., Klotz K., Shetty J., Retief J.D., Coonrod S.A., Kinter M., Sherman N., Cesar F., Flickinger C.J., Herr J.C.
Biol. Reprod. 61:1184-1197(1999) [PubMed: 10529264] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Testis.
[3]"Isolation and molecular characterization of AKAP110, a novel, sperm-specific protein kinase A-anchoring protein."
Vijayaraghavan S., Liberty G.A., Mohan J., Winfrey V.P., Olson G.E., Carr D.W.
Mol. Endocrinol. 13:705-717(1999) [PubMed: 10319321] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[4]"Identification of sperm-specific proteins that interact with A-kinase anchoring proteins in a manner similar to the type II regulatory subunit of PKA."
Carr D.W., Fujita A., Stentz C.L., Liberty G.A., Olson G.E., Narumiya S.
J. Biol. Chem. 276:17332-17338(2001) [PubMed: 11278869] [Abstract]
Cited for: INTERACTION WITH ROPN1 AND ROPN1L, MUTAGENESIS OF LEU-131.
[5]"Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation."
Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F., Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F., Visconti P.E.
J. Biol. Chem. 278:11579-11589(2003) [PubMed: 12509440] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-208; SER-403; TYR-404; SER-440; SER-612; SER-635 AND SER-636, MASS SPECTROMETRY.
Tissue: Sperm.
[6]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-831.
+Additional computationally mapped references.

Cross-references

Sequence databases

U85715 mRNA. Translation: AAD21218.1.
AF087003 mRNA. Translation: AAC35854.1.
AF093408 mRNA. Translation: AAC63371.1.
RefSeqNP_006413.2.
UniGeneHs.98397

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteO75969.

Genome annotation databases

EnsemblENSG00000111254. Homo sapiens. [Contig view]
GeneID10566.
KEGGhsa:10566.

Organism-specific databases

H-InvDBHIX0026339.
HGNCHGNC:373. AKAP3.
MIM604689. gene.
PharmGKBPA24667.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMO75969.
HOVERGENO75969.

Gene expression databases

ArrayExpressO75969.
CleanExHS_AKAP3.
GermOnlineENSG00000111254. Homo sapiens.

Family and domain databases

InterProIPR008382. AKAP_110.
[Graphical view]
PANTHERPTHR10226. AKAP_110. 1 hit.
PfamPF05716. AKAP_110. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio40101.
SOURCESearch...

Entry information

Entry nameAKAP3_HUMAN
AccessionPrimary (citable) accession number: O75969
Secondary accession number(s): O75945, Q9UM61
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1998
Last modified: November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents