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Q5JQC9 (AKAP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A-kinase anchor protein 4

Short name=AKAP-4
Alternative name(s):
A-kinase anchor protein 82 kDa
Short name=AKAP 82
Short name=hAKAP82
Major sperm fibrous sheath protein
Short name=HI
Protein kinase A-anchoring protein 4
Short name=PRKA4
Gene names
Name:AKAP4
Synonyms:AKAP82
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length854 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Major structural component of sperm fibrous sheath. Plays a role in sperm motility. Ref.2

Subunit structure

Interacts with PRKAR1A and PRKAR2A By similarity. UniProtKB Q60662

Subcellular location

Cell projectionciliumflagellum. Note: Localizes to the principle piece of the sperm flagellum. Ref.2

Tissue specificity

Testis specific; only expressed in round spermatids. Ref.1

Developmental stage

Post-meiotic phase of spermatogenesis. Ref.1

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 By similarity. UniProtKB Q60662

Sequence similarities

Belongs to the AKAP110 family.

Sequence caution

The sequence CAA75494.1 differs from that shown. Reason: Frameshift at several positions.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q5JQC9-1)

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 Ref.2 (identifier: Q5JQC9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.
Isoform 3 Ref.3 (identifier: Q5JQC9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.
     191-564: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 188188 Potential
PRO_0000248230
Chain189 – 854666A-kinase anchor protein 4 UniProtKB Q60662
PRO_0000248231

Regions

Region219 – 23214PKA-RI and PKA-RII subunit binding domain By similarity UniProtKB Q60662
Region336 – 34510PKA-RI-alpha subunit binding domain By similarity UniProtKB Q60662

Natural variations

Alternative sequence1 – 99Missing in isoform 2 and isoform 3. Ref.2 Ref.3
VSP_052142
Alternative sequence191 – 564374Missing in isoform 3. Ref.3
VSP_052143
Natural variant2331H → R.
Corresponds to variant rs17174078 [ dbSNP | Ensembl ].
VAR_048206
Natural variant6731A → G.
Corresponds to variant rs12012704 [ dbSNP | Ensembl ].
VAR_027266

Experimental info

Sequence conflict1231L → W in AAC79433. Ref.2
Sequence conflict1281A → E in AAC79433. Ref.2
Sequence conflict1461E → D in AAC79433. Ref.2
Sequence conflict1901S → N in CAI41558. Ref.3
Sequence conflict3691R → W in CAA75494. Ref.1
Sequence conflict428 – 4292KR → IL in AAC79433. Ref.2
Sequence conflict5171K → M in AAC79433. Ref.2
Sequence conflict5601T → I in CAA75494. Ref.1

Sequences

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

Last modified February 15, 2005. Version 1.
Checksum: E440CBE8AB9394F4

FASTA85494,477
        10         20         30         40         50         60 
MMAYSDTTMM SDDIDWLRSH RGVCKVDLYN PEGQQDQDRK VICFVDVSTL NVEDKDYKDA 

        70         80         90        100        110        120 
ASSSSEGNLN LGSLEEKEII VIKDTEKKDQ SKTEGSVCLF KQAPSDPVSV LNWLLSDLQK 

       130        140        150        160        170        180 
YALGFQHALS PSTSTCKHKV GDTEGEYHRA SSENCYSVYA DQVNIDYLMN RPQNLRLEMT 

       190        200        210        220        230        240 
AAKNTNNNQS PSAPPAKPPS TQRAVISPDG ECSIDDLSFY VNRLSSLVIQ MAHKEIKEKL 

       250        260        270        280        290        300 
EGKSKCLHHS ICPSPGNKER ISPRTPASKI ASEMAYEAVE LTAAEMRGTG EESREGGQKS 

       310        320        330        340        350        360 
FLYSELSNKS KSGDKQMSQR ESKEFADSIS KGLMVYANQV ASDMMVSLMK TLKVHSSGKP 

       370        380        390        400        410        420 
IPASVVLKRV LLRHTKEIVS DLIDSCMKNL HNITGVLMTD SDFVSAVKRN LFNQWKQNAT 

       430        440        450        460        470        480 
DIMEAMLKRL VSALIGEEKE TKSQSLSYAS LKAGSHDPKC RNQSLEFSTM KAEMKERDKG 

       490        500        510        520        530        540 
KMKSDPCKSL TSAEKVGEHI LKEGLTIWNQ KQGNSCKVAT KACSNKDEKG EKINASTDSL 

       550        560        570        580        590        600 
AKDLIVSALK LIQYHLTQQT KGKDTCEEDC PGSTMGYMAQ STQYEKCGGG QSAKALSVKQ 

       610        620        630        640        650        660 
LESHRAPGPS TCQKENQHLD SQKMDMSNIV LMLIQKLLNE NPFKCEDPCE GENKCSEPRA 

       670        680        690        700        710        720 
SKAASMSNRS DKAEEQCQEH QELDCTSGMK QANGQFIDKL VESVMKLCLI MAKYSNDGAA 

       730        740        750        760        770        780 
LAELEEQAAS ANKPNFRGTR CIHSGAMPQN YQDSLGHEVI VNNQCSTNSL QKQLQAVLQW 

       790        800        810        820        830        840 
IAASQFNVPM LYFMGDKDGQ LEKLPQVSAK AAEKGYSVGG LLQEVMKFAK ERQPDEAVGK 

       850 
VARKQLLDWL LANL 

« Hide

Isoform 2 [UniParc].

Checksum: EBB124BFF6BF3C31
Show »

FASTA84593,445
Isoform 3 [UniParc].

Checksum: 3617CE60B2689445
Show »

FASTA47152,263

References

« Hide 'large scale' references
[1]"Molecular cloning of human testis mRNA specifically expressed in haploid germ cells, having structural homology with the A-kinase anchoring proteins."
Mohapatra B., Verma S., Shankar S., Suri A.
Biochem. Biophys. Res. Commun. 244:540-545(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Testis.
[2]"An X-linked gene encodes a major human sperm fibrous sheath protein, hAKAP82. Genomic organization, protein kinase A-RII binding, and distribution of the precursor in the sperm tail."
Turner R.M.O., Johnson L.R., Haig-Ladewig L., Gerton G.L., Moss S.B.
J. Biol. Chem. 273:32135-32141(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
[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], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3).
[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] (ISOFORM 1).
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y15195 mRNA. Translation: CAA75494.1. Sequence problems.
AF072756 mRNA. Translation: AAC79433.1.
AL663119 Genomic DNA. Translation: CAI41557.1.
AL663119 Genomic DNA. Translation: CAI41558.1.
AL663119 Genomic DNA. Translation: CAI41559.1.
AL663119 Genomic DNA. Translation: CAI41561.1.
BC126250 mRNA. Translation: AAI26251.1.
BC126252 mRNA. Translation: AAI26253.1.
IPIIPI00157860.
IPI00333264.
IPI00552135.
PIRJC5986.
RefSeqNP_003877.2. NM_003886.2.
NP_647450.1. NM_139289.1.
UniGeneHs.97633.

3D structure databases

ProteinModelPortalQ5JQC9.
SMRQ5JQC9. Positions 771-853.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000351327.

PTM databases

PhosphoSiteQ5JQC9.

Polymorphism databases

DMDM74741729.

Proteomic databases

PaxDbQ5JQC9.
PRIDEQ5JQC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358526; ENSP00000351327; ENSG00000147081.
ENST00000376056; ENSP00000365224; ENSG00000147081.
ENST00000376064; ENSP00000365232; ENSG00000147081.
ENST00000437370; ENSP00000412279; ENSG00000147081.
ENST00000448865; ENSP00000402403; ENSG00000147081.
ENST00000594184; ENSP00000472101; ENSG00000269285.
ENST00000594628; ENSP00000471711; ENSG00000269285.
ENST00000594732; ENSP00000469992; ENSG00000269285.
ENST00000596010; ENSP00000470803; ENSG00000269285.
ENST00000601454; ENSP00000473209; ENSG00000269285.
GeneID8852.
KEGGhsa:8852.
UCSCuc004dou.1. human.

Organism-specific databases

CTD8852.
GeneCardsGC0XM049955.
HGNCHGNC:374. AKAP4.
HPAHPA005949.
HPA020046.
MIM300185. gene.
neXtProtNX_Q5JQC9.
PharmGKBPA24668.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40269.
HOGENOMHOG000220883.
HOVERGENHBG050478.
InParanoidQ5JQC9.
KOK16521.
OMASKGLMVY.
OrthoDBEOG4JQ3WX.
PhylomeDBQ5JQC9.

Gene expression databases

ArrayExpressQ5JQC9.
BgeeQ5JQC9.
CleanExHS_AKAP4.
GenevestigatorQ5JQC9.
GermOnlineENSG00000147081. Homo sapiens.

Family and domain databases

InterProIPR020799. AKAP_110.
IPR018292. AKAP_110_C.
IPR018459. RII_binding_1.
IPR008382. SPHK1-interactor_AKAP_110.
[Graphical view]
PANTHERPTHR10226. PTHR10226. 1 hit.
PfamPF05716. AKAP_110. 1 hit.
PF10522. RII_binding_1. 1 hit.
[Graphical view]
SMARTSM00807. AKAP_110. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAKAP4. human.
GenomeRNAi8852.
NextBio33231.
SOURCESearch...

Entry information

Entry nameAKAP4_HUMAN
AccessionPrimary (citable) accession number: Q5JQC9
Secondary accession number(s): A0AV85 expand/collapse secondary AC list , O60904, O95246, Q5JQD1, Q5JQD2, Q5JQD3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: February 15, 2005
Last modified: May 1, 2013
This is version 75 of the entry and version 1 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

Human chromosome X

Human chromosome X: 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