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Q5JQC9

- AKAP4_HUMAN

UniProt

Q5JQC9 - AKAP4_HUMAN

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Protein

A-kinase anchor protein 4

Gene

AKAP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Major structural component of sperm fibrous sheath. Plays a role in sperm motility.1 Publication

GO - Molecular functioni

  1. protein kinase A binding Source: UniProtKB

GO - Biological processi

  1. cell projection organization Source: UniProtKB-KW
  2. cellular component movement Source: ProtInc
  3. protein localization Source: Ensembl
  4. signal transduction Source: ProtInc
  5. single fertilization Source: ProtInc
  6. sperm motility Source: UniProtKB
  7. transmembrane receptor protein serine/threonine kinase signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:AKAP4Imported
Synonyms:AKAP82
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:374. AKAP4.

Subcellular locationi

Cell projectionciliumflagellum 1 Publication
Note: Localizes to the principle piece of the sperm flagellum.

GO - Cellular componenti

  1. cAMP-dependent protein kinase complex Source: UniProtKB
  2. cytoskeleton Source: ProtInc
  3. motile cilium Source: UniProtKB
  4. nucleus Source: UniProt
  5. perinuclear region of cytoplasm Source: Ensembl
  6. sperm fibrous sheath Source: Ensembl
  7. sperm principal piece Source: Ensembl
  8. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Flagellum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24668.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 188188Sequence AnalysisPRO_0000248230Add
BLAST
Chaini189 – 854666A-kinase anchor protein 4By similarityPRO_0000248231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001Phosphoserine1 Publication
Modified residuei303 – 3031Phosphotyrosine1 Publication
Modified residuei304 – 3041Phosphoserine1 Publication
Modified residuei447 – 4471Phosphoserine1 Publication
Modified residuei450 – 4501Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5JQC9.
PaxDbiQ5JQC9.
PRIDEiQ5JQC9.

PTM databases

PhosphoSiteiQ5JQC9.

Expressioni

Tissue specificityi

Testis specific; only expressed in round spermatids.1 Publication

Developmental stagei

Post-meiotic phase of spermatogenesis.1 Publication

Gene expression databases

BgeeiQ5JQC9.
CleanExiHS_AKAP4.
GenevestigatoriQ5JQC9.

Organism-specific databases

HPAiHPA005949.
HPA020046.

Interactioni

Subunit structurei

Interacts with PRKAR1A and PRKAR2A.By similarity

Protein-protein interaction databases

BioGridi114377. 6 interactions.
STRINGi9606.ENSP00000351327.

Structurei

3D structure databases

ProteinModelPortaliQ5JQC9.
SMRiQ5JQC9. Positions 771-852.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 23214PKA-RI and PKA-RII subunit binding domainBy similarityAdd
BLAST
Regioni336 – 34510PKA-RI-alpha subunit binding domainBy similarity

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.By similarity

Sequence similaritiesi

Belongs to the AKAP110 family.Curated

Phylogenomic databases

eggNOGiNOG40269.
GeneTreeiENSGT00420000029845.
HOGENOMiHOG000220883.
HOVERGENiHBG050478.
InParanoidiQ5JQC9.
KOiK16521.
OMAiGEHILKE.
PhylomeDBiQ5JQC9.
TreeFamiTF105403.

Family and domain databases

InterProiIPR020799. AKAP_110.
IPR018292. AKAP_110_C.
IPR018459. RII_binding_1.
IPR008382. SPHK1-interactor_AKAP_110.
[Graphical view]
PANTHERiPTHR10226. PTHR10226. 1 hit.
PfamiPF05716. AKAP_110. 1 hit.
PF10522. RII_binding_1. 1 hit.
[Graphical view]
SMARTiSM00807. AKAP_110. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q5JQC9-1) [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

        10         20         30         40         50
MMAYSDTTMM SDDIDWLRSH RGVCKVDLYN PEGQQDQDRK VICFVDVSTL
60 70 80 90 100
NVEDKDYKDA ASSSSEGNLN LGSLEEKEII VIKDTEKKDQ SKTEGSVCLF
110 120 130 140 150
KQAPSDPVSV LNWLLSDLQK YALGFQHALS PSTSTCKHKV GDTEGEYHRA
160 170 180 190 200
SSENCYSVYA DQVNIDYLMN RPQNLRLEMT AAKNTNNNQS PSAPPAKPPS
210 220 230 240 250
TQRAVISPDG ECSIDDLSFY VNRLSSLVIQ MAHKEIKEKL EGKSKCLHHS
260 270 280 290 300
ICPSPGNKER ISPRTPASKI ASEMAYEAVE LTAAEMRGTG EESREGGQKS
310 320 330 340 350
FLYSELSNKS KSGDKQMSQR ESKEFADSIS KGLMVYANQV ASDMMVSLMK
360 370 380 390 400
TLKVHSSGKP IPASVVLKRV LLRHTKEIVS DLIDSCMKNL HNITGVLMTD
410 420 430 440 450
SDFVSAVKRN LFNQWKQNAT DIMEAMLKRL VSALIGEEKE TKSQSLSYAS
460 470 480 490 500
LKAGSHDPKC RNQSLEFSTM KAEMKERDKG KMKSDPCKSL TSAEKVGEHI
510 520 530 540 550
LKEGLTIWNQ KQGNSCKVAT KACSNKDEKG EKINASTDSL AKDLIVSALK
560 570 580 590 600
LIQYHLTQQT KGKDTCEEDC PGSTMGYMAQ STQYEKCGGG QSAKALSVKQ
610 620 630 640 650
LESHRAPGPS TCQKENQHLD SQKMDMSNIV LMLIQKLLNE NPFKCEDPCE
660 670 680 690 700
GENKCSEPRA SKAASMSNRS DKAEEQCQEH QELDCTSGMK QANGQFIDKL
710 720 730 740 750
VESVMKLCLI MAKYSNDGAA LAELEEQAAS ANKPNFRGTR CIHSGAMPQN
760 770 780 790 800
YQDSLGHEVI VNNQCSTNSL QKQLQAVLQW IAASQFNVPM LYFMGDKDGQ
810 820 830 840 850
LEKLPQVSAK AAEKGYSVGG LLQEVMKFAK ERQPDEAVGK VARKQLLDWL

LANL
Length:854
Mass (Da):94,477
Last modified:February 15, 2005 - v1
Checksum:iE440CBE8AB9394F4
GO
Isoform 21 Publication (identifier: Q5JQC9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.

Show »
Length:845
Mass (Da):93,445
Checksum:iEBB124BFF6BF3C31
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231L → W in AAC79433. (PubMed:9822690)Curated
Sequence conflicti128 – 1281A → E in AAC79433. (PubMed:9822690)Curated
Sequence conflicti146 – 1461E → D in AAC79433. (PubMed:9822690)Curated
Sequence conflicti369 – 3691R → W in CAA75494. (PubMed:9514854)Curated
Sequence conflicti428 – 4292KR → IL in AAC79433. (PubMed:9822690)Curated
Sequence conflicti517 – 5171K → M in AAC79433. (PubMed:9822690)Curated
Sequence conflicti560 – 5601T → I in CAA75494. (PubMed:9514854)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331H → R.
Corresponds to variant rs17174078 [ dbSNP | Ensembl ].
VAR_048206
Natural varianti673 – 6731A → G.
Corresponds to variant rs12012704 [ dbSNP | Ensembl ].
VAR_027266

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99Missing in isoform 2. 1 PublicationVSP_052142

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15195 mRNA. Translation: CAA75494.1. Sequence problems.
AF072756 mRNA. Translation: AAC79433.1.
FO393402 Genomic DNA. No translation available.
BC126250 mRNA. Translation: AAI26251.1.
BC126252 mRNA. Translation: AAI26253.1.
CCDSiCCDS14329.1. [Q5JQC9-1]
CCDS14330.1. [Q5JQC9-2]
PIRiJC5986.
RefSeqiNP_003877.2. NM_003886.2. [Q5JQC9-1]
NP_647450.1. NM_139289.1. [Q5JQC9-2]
UniGeneiHs.97633.

Genome annotation databases

EnsembliENST00000358526; ENSP00000351327; ENSG00000147081. [Q5JQC9-1]
ENST00000376064; ENSP00000365232; ENSG00000147081. [Q5JQC9-2]
GeneIDi8852.
KEGGihsa:8852.
UCSCiuc004dou.1. human. [Q5JQC9-1]

Polymorphism databases

DMDMi74741729.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15195 mRNA. Translation: CAA75494.1 . Sequence problems.
AF072756 mRNA. Translation: AAC79433.1 .
FO393402 Genomic DNA. No translation available.
BC126250 mRNA. Translation: AAI26251.1 .
BC126252 mRNA. Translation: AAI26253.1 .
CCDSi CCDS14329.1. [Q5JQC9-1 ]
CCDS14330.1. [Q5JQC9-2 ]
PIRi JC5986.
RefSeqi NP_003877.2. NM_003886.2. [Q5JQC9-1 ]
NP_647450.1. NM_139289.1. [Q5JQC9-2 ]
UniGenei Hs.97633.

3D structure databases

ProteinModelPortali Q5JQC9.
SMRi Q5JQC9. Positions 771-852.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114377. 6 interactions.
STRINGi 9606.ENSP00000351327.

PTM databases

PhosphoSitei Q5JQC9.

Polymorphism databases

DMDMi 74741729.

Proteomic databases

MaxQBi Q5JQC9.
PaxDbi Q5JQC9.
PRIDEi Q5JQC9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358526 ; ENSP00000351327 ; ENSG00000147081 . [Q5JQC9-1 ]
ENST00000376064 ; ENSP00000365232 ; ENSG00000147081 . [Q5JQC9-2 ]
GeneIDi 8852.
KEGGi hsa:8852.
UCSCi uc004dou.1. human. [Q5JQC9-1 ]

Organism-specific databases

CTDi 8852.
GeneCardsi GC0XM049955.
HGNCi HGNC:374. AKAP4.
HPAi HPA005949.
HPA020046.
MIMi 300185. gene.
neXtProti NX_Q5JQC9.
PharmGKBi PA24668.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40269.
GeneTreei ENSGT00420000029845.
HOGENOMi HOG000220883.
HOVERGENi HBG050478.
InParanoidi Q5JQC9.
KOi K16521.
OMAi GEHILKE.
PhylomeDBi Q5JQC9.
TreeFami TF105403.

Miscellaneous databases

ChiTaRSi AKAP4. human.
GeneWikii AKAP4.
GenomeRNAii 8852.
NextBioi 33231.
PROi Q5JQC9.
SOURCEi Search...

Gene expression databases

Bgeei Q5JQC9.
CleanExi HS_AKAP4.
Genevestigatori Q5JQC9.

Family and domain databases

InterProi IPR020799. AKAP_110.
IPR018292. AKAP_110_C.
IPR018459. RII_binding_1.
IPR008382. SPHK1-interactor_AKAP_110.
[Graphical view ]
PANTHERi PTHR10226. PTHR10226. 1 hit.
Pfami PF05716. AKAP_110. 1 hit.
PF10522. RII_binding_1. 1 hit.
[Graphical view ]
SMARTi SM00807. AKAP_110. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: TestisImported.
  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.
    , 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] (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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; TYR-303; SER-304; SER-447 AND SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Sperm.

Entry informationi

Entry nameiAKAP4_HUMAN
AccessioniPrimary (citable) accession number: Q5JQC9
Secondary accession number(s): A0AV85
, O60904, O95246, Q5JQD1, Q5JQD2, Q5JQD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 88 of the entry and version 1 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

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