Reviewed, UniProtKB/Swiss-Prot Q5JQC9 (AKAP4_HUMAN)

Names and origin

Protein names

Recommended name:
    A-kinase anchor protein 4
Alternative name(s):
    Protein kinase A-anchoring protein 4
      Short name=PRKA4
    A-kinase anchor protein 82 kDa
      Short name=AKAP 82
      Short name=hAKAP82
    Major sperm fibrous sheath protein
      Short name=HI

Gene names

Name:	AKAP4
Synonyms:	AKAP82

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	854 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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 projection › cilium › flagellum. 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.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cell projection Cilium Flagellum
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell projection organization Inferred from electronic annotation. Source: UniProtKB-KW single fertilization Ref.2 Traceable author statement. Source: ProtInc sperm motility Ref.2 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cAMP-dependent protein kinase complex Ref.2 Non-traceable author statement. Source: UniProtKB cilium Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Ref.2 Traceable author statement. Source: ProtInc microtubule-based flagellum Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	protein kinase A binding Ref.2 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – ?		Potential UniProtKB Q60662
	Propeptide	? – 188		Potential UniProtKB Q60662		PRO_0000248230
	Chain	189 – 854	666	A-kinase anchor protein 4 UniProtKB Q60662		PRO_0000248231
Regions
	Region	219 – 232	14	PKA-RI and PKA-RII subunit binding domain By similarity UniProtKB Q60662
	Region	336 – 345	10	PKA-RI-alpha subunit binding domain By similarity UniProtKB Q60662
Amino acid modifications
	Modified residue	62	1	Phosphoserine Ref.5
	Modified residue	63	1	Phosphoserine Ref.5
	Modified residue	64	1	Phosphoserine Ref.5
	Modified residue	65	1	Phosphoserine Ref.5
	Modified residue	151	1	Phosphoserine Ref.5
	Modified residue	265	1	Phosphothreonine Ref.5
	Modified residue	268	1	Phosphoserine Ref.5
	Modified residue	272	1	Phosphoserine Ref.5
	Modified residue	293	1	Phosphoserine Ref.5
	Modified residue	300	1	Phosphoserine Ref.5
	Modified residue	303	1	Phosphotyrosine Ref.5
	Modified residue	304	1	Phosphoserine Ref.5
	Modified residue	447	1	Phosphoserine Ref.5
	Modified residue	448	1	Phosphotyrosine Ref.5
	Modified residue	450	1	Phosphoserine Ref.5
	Modified residue	492	1	Phosphoserine Ref.5
	Modified residue	536	1	Phosphoserine Ref.5
	Modified residue	539	1	Phosphoserine Ref.5
	Modified residue	665	1	Phosphoserine Ref.5
	Modified residue	667	1	Phosphoserine Ref.5
Natural variations
	Alternative sequence	1 – 9	9	Missing in isoform 2 and isoform 3. Ref.2 Ref.3		VSP_052142
	Alternative sequence	191 – 564	374	Missing in isoform 3. Ref.3		VSP_052143
	Natural variant	233	1	H → R: dbSNP rs17174078.		VAR_048206
	Natural variant	673	1	A → G: dbSNP rs12012704.		VAR_027266
Experimental info
	Sequence conflict	123	1	L → W in AAC79433. Ref.2
	Sequence conflict	128	1	A → E in AAC79433. Ref.2
	Sequence conflict	146	1	E → D in AAC79433. Ref.2
	Sequence conflict	190	1	S → N in CAI41558. Ref.3
	Sequence conflict	369	1	R → W in CAA75494. Ref.1
	Sequence conflict	428 – 429	2	KR → IL in AAC79433. Ref.2
	Sequence conflict	517	1	K → M in AAC79433. Ref.2
	Sequence conflict	560	1	T → I in CAA75494. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: E440CBE8AB9394F4	FASTA	854	94,477
	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
	Isoform 2. Checksum: EBB124BFF6BF3C31	FASTA	845	93,445
	10 20 30 40 50 60 MSDDIDWLRS HRGVCKVDLY NPEGQQDQDR KVICFVDVST LNVEDKDYKD AASSSSEGNL 70 80 90 100 110 120 NLGSLEEKEI IVIKDTEKKD QSKTEGSVCL FKQAPSDPVS VLNWLLSDLQ KYALGFQHAL 130 140 150 160 170 180 SPSTSTCKHK VGDTEGEYHR ASSENCYSVY ADQVNIDYLM NRPQNLRLEM TAAKNTNNNQ 190 200 210 220 230 240 SPSAPPAKPP STQRAVISPD GECSIDDLSF YVNRLSSLVI QMAHKEIKEK LEGKSKCLHH 250 260 270 280 290 300 SICPSPGNKE RISPRTPASK IASEMAYEAV ELTAAEMRGT GEESREGGQK SFLYSELSNK 310 320 330 340 350 360 SKSGDKQMSQ RESKEFADSI SKGLMVYANQ VASDMMVSLM KTLKVHSSGK PIPASVVLKR 370 380 390 400 410 420 VLLRHTKEIV SDLIDSCMKN LHNITGVLMT DSDFVSAVKR NLFNQWKQNA TDIMEAMLKR 430 440 450 460 470 480 LVSALIGEEK ETKSQSLSYA SLKAGSHDPK CRNQSLEFST MKAEMKERDK GKMKSDPCKS 490 500 510 520 530 540 LTSAEKVGEH ILKEGLTIWN QKQGNSCKVA TKACSNKDEK GEKINASTDS LAKDLIVSAL 550 560 570 580 590 600 KLIQYHLTQQ TKGKDTCEED CPGSTMGYMA QSTQYEKCGG GQSAKALSVK QLESHRAPGP 610 620 630 640 650 660 STCQKENQHL DSQKMDMSNI VLMLIQKLLN ENPFKCEDPC EGENKCSEPR ASKAASMSNR 670 680 690 700 710 720 SDKAEEQCQE HQELDCTSGM KQANGQFIDK LVESVMKLCL IMAKYSNDGA ALAELEEQAA 730 740 750 760 770 780 SANKPNFRGT RCIHSGAMPQ NYQDSLGHEV IVNNQCSTNS LQKQLQAVLQ WIAASQFNVP 790 800 810 820 830 840 MLYFMGDKDG QLEKLPQVSA KAAEKGYSVG GLLQEVMKFA KERQPDEAVG KVARKQLLDW LLANL
	Isoform 3. Checksum: 3617CE60B2689445	FASTA	471	52,263
	10 20 30 40 50 60 MSDDIDWLRS HRGVCKVDLY NPEGQQDQDR KVICFVDVST LNVEDKDYKD AASSSSEGNL 70 80 90 100 110 120 NLGSLEEKEI IVIKDTEKKD QSKTEGSVCL FKQAPSDPVS VLNWLLSDLQ KYALGFQHAL 130 140 150 160 170 180 SPSTSTCKHK VGDTEGEYHR ASSENCYSVY ADQVNIDYLM NRPQNLRLEM TAAKNTNNNQ 190 200 210 220 230 240 STCEEDCPGS TMGYMAQSTQ YEKCGGGQSA KALSVKQLES HRAPGPSTCQ KENQHLDSQK 250 260 270 280 290 300 MDMSNIVLML IQKLLNENPF KCEDPCEGEN KCSEPRASKA ASMSNRSDKA EEQCQEHQEL 310 320 330 340 350 360 DCTSGMKQAN GQFIDKLVES VMKLCLIMAK YSNDGAALAE LEEQAASANK PNFRGTRCIH 370 380 390 400 410 420 SGAMPQNYQD SLGHEVIVNN QCSTNSLQKQ LQAVLQWIAA SQFNVPMLYF MGDKDGQLEK 430 440 450 460 470 LPQVSAKAAE KGYSVGGLLQ EVMKFAKERQ PDEAVGKVAR KQLLDWLLAN L

References

	« Hide 'large scale' referencesShow '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: 9514854] [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: 9822690] [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. , 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: 15772651] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[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-62; SER-63; SER-64; SER-65; SER-151; THR-265; SER-268; SER-272; SER-293; SER-300; TYR-303; SER-304; SER-447; TYR-448; SER-450; SER-492; SER-536; SER-539; SER-665 AND SER-667, MASS SPECTROMETRY. Tissue: Sperm.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00157860. IPI00333264. IPI00552135.
PIR	JC5986.
RefSeq	NP_003877.2. NP_647450.1.
UniGene	Hs.97633
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q5JQC9.
Proteomic databases
PRIDE	Q5JQC9.
Genome annotation databases
Ensembl	ENSG00000147081. Homo sapiens. [Contig view]
GeneID	8852.
KEGG	hsa:8852.
Organism-specific databases
GeneCards	GC0XM049842.
HGNC	HGNC:374. AKAP4.
HPA	HPA005949.
MIM	300185. gene.
PharmGKB	PA24668.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q5JQC9.
OMA	Q5JQC9. KRVLLKH.
Gene expression databases
ArrayExpress	Q5JQC9.
Bgee	Q5JQC9.
CleanEx	HS_AKAP4.
GermOnline	ENSG00000147081. Homo sapiens.
Family and domain databases
InterPro	IPR008382. AKAP_110. IPR018292. AKAP_110_C. IPR018459. RII_binding_1. [Graphical view]
PANTHER	PTHR10226. AKAP_110. 1 hit.
Pfam	PF05716. AKAP_110. 1 hit. PF10522. RII_binding_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	33231.
SOURCE	Search...

Entry information

Entry name

AKAP4_HUMAN

Accession

Primary (citable) accession number: Q5JQC9
Secondary accession number(s): A0AV85 , O60904, O95246, Q5JQD1, Q5JQD2, Q5JQD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	February 15, 2005
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)