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Protein

A-kinase anchor protein 8-like

Gene

AKAP8L

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

Functioni

Could play a role in constitutive transport element (CTE)-mediated gene expression. Does not seem to be implicated in the binding of regulatory subunit II of PKA. May be involved in nuclear envelope breakdown and chromatin condensation. May regulate the initiation phase of DNA replication when associated with TMPO-beta.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri389 – 41325C2H2 AKAP95-type 1Add
BLAST
Zinc fingeri482 – 50726C2H2 AKAP95-type 2Add
BLAST

GO - Molecular functioni

  • DEAD/H-box RNA helicase binding Source: UniProtKB
  • DNA binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 8-like
Short name:
AKAP8-like protein
Alternative name(s):
Helicase A-binding protein 95
Short name:
HAP95
Homologous to AKAP95 protein
Short name:
HA95
Neighbor of A-kinase-anchoring protein 95
Short name:
Neighbor of AKAP95
Gene namesi
Name:AKAP8L
Synonyms:NAKAP, NAKAP95
ORF Names:HRIHFB2018
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:29857. AKAP8L.

Subcellular locationi

  • Nucleus matrix
  • Cytoplasm

  • Note: Colocalizes with PRPF40A in the nuclear matrix (By similarity). Nuclear at steady state but shuttles between the nucleus and cytoplasm. Associated with the nuclear matrix.By similarity

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134867364.

Polymorphism and mutation databases

BioMutaiAKAP8L.
DMDMi296439446.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 646646A-kinase anchor protein 8-likePRO_0000075384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571N6-acetyllysine1 Publication
Modified residuei283 – 2831Phosphoserine2 Publications
Modified residuei292 – 2921Phosphothreonine1 Publication
Modified residuei297 – 2971Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine or threonine residues possibly by PKA.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9ULX6.
PaxDbiQ9ULX6.
PRIDEiQ9ULX6.

PTM databases

PhosphoSiteiQ9ULX6.

Expressioni

Tissue specificityi

Expressed in the brain cortex (at protein level).1 Publication

Gene expression databases

BgeeiQ9ULX6.
CleanExiHS_AKAP8L.
ExpressionAtlasiQ9ULX6. baseline and differential.
GenevisibleiQ9ULX6. HS.

Organism-specific databases

HPAiHPA042485.
HPA042546.

Interactioni

Subunit structurei

Interacts with PRPF40A (By similarity). Binds to the C-terminal of RNA helicase A and to TMPO-beta. Interacts with RNF43.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P299913EBI-357530,EBI-8826747From a different organism.
RNF43Q68DV72EBI-357530,EBI-1647060

Protein-protein interaction databases

BioGridi117940. 31 interactions.
DIPiDIP-27541N.
IntActiQ9ULX6. 16 interactions.
MINTiMINT-1134534.
STRINGi9606.ENSP00000380557.

Structurei

3D structure databases

ProteinModelPortaliQ9ULX6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi274 – 2796Nuclear localization signalSequence Analysis
Motifi362 – 3643Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 5212Gly/Tyr-richAdd
BLAST
Compositional biasi589 – 5979Pro-rich
Compositional biasi602 – 6087Pro-rich

Sequence similaritiesi

Belongs to the AKAP95 family.Curated
Contains 2 C2H2 AKAP95-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri389 – 41325C2H2 AKAP95-type 1Add
BLAST
Zinc fingeri482 – 50726C2H2 AKAP95-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG47695.
HOGENOMiHOG000169111.
HOVERGENiHBG104297.
InParanoidiQ9ULX6.
KOiK15978.
OMAiDTNANPS.
OrthoDBiEOG79SDWZ.
PhylomeDBiQ9ULX6.
TreeFamiTF105407.

Family and domain databases

InterProiIPR007071. AKAP95.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERiPTHR12190. PTHR12190. 1 hit.
PfamiPF04988. AKAP95. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ULX6-1) [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
MSYTGFVQGS ETTLQSTYSD TSAQPTCDYG YGTWNSGTNR GYEGYGYGYG
60 70 80 90 100
YGQDNTTNYG YGMATSHSWE MPSSDTNANT SASGSASADS VLSRINQRLD
110 120 130 140 150
MVPHLETDMM QGGVYGSGGE RYDSYESCDS RAVLSERDLY RSGYDYSELD
160 170 180 190 200
PEMEMAYEGQ YDAYRDQFRM RGNDTFGPRA QGWARDARSG RPMASGYGRM
210 220 230 240 250
WEDPMGARGQ CMSGASRLPS LFSQNIIPEY GMFQGMRGGG AFPGGSRFGF
260 270 280 290 300
GFGNGMKQMR RTWKTWTTAD FRTKKKKRKQ GGSPDEPDSK ATRTDCSDNS
310 320 330 340 350
DSDNDEGTEG EATEGLEGTE AVEKGSRVDG EDEEGKEDGR EEGKEDPEKG
360 370 380 390 400
ALTTQDENGQ TKRKLQAGKK SQDKQKKRQR DRMVERIQFV CSLCKYRTFY
410 420 430 440 450
EDEMASHLDS KFHKEHFKYV GTKLPKQTAD FLQEYVTNKT KKTEELRKTV
460 470 480 490 500
EDLDGLIHQI YRDQDLTQEI AMEHFVKKVE AAHCAACDLF IPMQFGIIQK
510 520 530 540 550
HLKTMDHNRN RRLMMEQSKK SSLMVARSIL NNKLISKKLE RYLKGENPFT
560 570 580 590 600
DSPEEEKEQE EAEGGALDEG AQGEAAGISE GAEGVPAQPP VPPEPAPGAV
610 620 630 640
SPPPPPPPEE EEEGAVPLLG GALQRQIRGI PGLDVEDDEE GGGGAP
Length:646
Mass (Da):71,649
Last modified:May 18, 2010 - v3
Checksum:iEED855A81BB06585
GO
Isoform 2 (identifier: Q9ULX6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-121: Missing.

Show »
Length:585
Mass (Da):65,230
Checksum:i460F073AC534A1B9
GO

Sequence cautioni

The sequence AAF86048.1 differs from that shown. Reason: Frameshift at position 553. Curated
The sequence BAA34791.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001D → N in AAF86048 (PubMed:10748171).Curated
Sequence conflicti189 – 1891S → N in AAF86048 (PubMed:10748171).Curated
Sequence conflicti351 – 3588ALTTQDEN → EFSWGAWC in BAA34791 (PubMed:9853615).Curated
Sequence conflicti599 – 61618AVSPP…EEGAV → GRVAATAAAPRRRRRRAPW in AAF86048 (PubMed:10748171).CuratedAdd
BLAST
Sequence conflicti641 – 6466GGGGAP → EGRRGRPV in AAF86048 (PubMed:10748171).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti458 – 4581H → Q.7 Publications
Corresponds to variant rs2058322 [ dbSNP | Ensembl ].
VAR_068822

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei61 – 12161Missing in isoform 2. 1 PublicationVSP_044426Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025905 mRNA. Translation: BAA85003.1.
AJ243467 mRNA. Translation: CAB65092.1.
AF199414 mRNA. Translation: AAF86048.1. Frameshift.
AK295956 mRNA. Translation: BAG58736.1.
AB451326 mRNA. Translation: BAG70140.1.
AB451469 mRNA. Translation: BAG70283.1.
AC005785 Genomic DNA. No translation available.
AC006128 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84475.1.
BC000713 mRNA. Translation: AAH00713.1.
AB015332 mRNA. Translation: BAA34791.1. Different initiation.
CCDSiCCDS46005.1. [Q9ULX6-1]
RefSeqiNP_001278407.1. NM_001291478.1.
NP_055186.3. NM_014371.3.
UniGeneiHs.399800.

Genome annotation databases

EnsembliENST00000397410; ENSP00000380557; ENSG00000011243.
ENST00000595465; ENSP00000470952; ENSG00000011243.
GeneIDi26993.
KEGGihsa:26993.
UCSCiuc002naw.1. human. [Q9ULX6-1]
uc010xoh.1. human. [Q9ULX6-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025905 mRNA. Translation: BAA85003.1.
AJ243467 mRNA. Translation: CAB65092.1.
AF199414 mRNA. Translation: AAF86048.1. Frameshift.
AK295956 mRNA. Translation: BAG58736.1.
AB451326 mRNA. Translation: BAG70140.1.
AB451469 mRNA. Translation: BAG70283.1.
AC005785 Genomic DNA. No translation available.
AC006128 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84475.1.
BC000713 mRNA. Translation: AAH00713.1.
AB015332 mRNA. Translation: BAA34791.1. Different initiation.
CCDSiCCDS46005.1. [Q9ULX6-1]
RefSeqiNP_001278407.1. NM_001291478.1.
NP_055186.3. NM_014371.3.
UniGeneiHs.399800.

3D structure databases

ProteinModelPortaliQ9ULX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117940. 31 interactions.
DIPiDIP-27541N.
IntActiQ9ULX6. 16 interactions.
MINTiMINT-1134534.
STRINGi9606.ENSP00000380557.

PTM databases

PhosphoSiteiQ9ULX6.

Polymorphism and mutation databases

BioMutaiAKAP8L.
DMDMi296439446.

Proteomic databases

MaxQBiQ9ULX6.
PaxDbiQ9ULX6.
PRIDEiQ9ULX6.

Protocols and materials databases

DNASUi26993.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397410; ENSP00000380557; ENSG00000011243.
ENST00000595465; ENSP00000470952; ENSG00000011243.
GeneIDi26993.
KEGGihsa:26993.
UCSCiuc002naw.1. human. [Q9ULX6-1]
uc010xoh.1. human. [Q9ULX6-2]

Organism-specific databases

CTDi26993.
GeneCardsiGC19M015490.
H-InvDBHIX0014850.
HIX0115658.
HGNCiHGNC:29857. AKAP8L.
HPAiHPA042485.
HPA042546.
MIMi609475. gene.
neXtProtiNX_Q9ULX6.
PharmGKBiPA134867364.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47695.
HOGENOMiHOG000169111.
HOVERGENiHBG104297.
InParanoidiQ9ULX6.
KOiK15978.
OMAiDTNANPS.
OrthoDBiEOG79SDWZ.
PhylomeDBiQ9ULX6.
TreeFamiTF105407.

Miscellaneous databases

ChiTaRSiAKAP8L. human.
GeneWikiiAKAP8L.
GenomeRNAii26993.
NextBioi35472456.
PROiQ9ULX6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULX6.
CleanExiHS_AKAP8L.
ExpressionAtlasiQ9ULX6. baseline and differential.
GenevisibleiQ9ULX6. HS.

Family and domain databases

InterProiIPR007071. AKAP95.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERiPTHR12190. PTHR12190. 1 hit.
PfamiPF04988. AKAP95. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of a novel human gene NAKAP95, neighbor of A-kinase anchoring protein 95 (AKAP95) on chromosome 19p13.11-p13.12 region."
    Seki N., Ueki N., Yano K., Saito T., Masuho Y., Muramatsu M.-A.
    J. Hum. Genet. 45:31-37(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "Identification, cloning and characterization of a novel nuclear protein, HA95, homologous to A-kinase anchoring protein 95."
    Orstavik S., Eide T., Collas P., Han I.O., Tasken K., Kieff E., Jahnsen T., Skalhegg B.S.
    Biol. Cell 92:27-37(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-458.
  3. "A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element."
    Westberg C., Yang J.-P., Tang H., Reddy T.R., Wong-Staal F.
    J. Biol. Chem. 275:21396-21401(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-458.
    Tissue: Placenta and T-cell lymphoma.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-458.
    Tissue: Substantia nigra.
  5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-458.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-458.
  8. "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), VARIANT GLN-458.
    Tissue: Placenta.
  9. "Selection system for genes encoding nuclear-targeted proteins."
    Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
    Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-358 (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  10. "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication."
    Martins S., Eikvar S., Furukawa K., Collas P.
    J. Cell Biol. 160:177-188(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMPO-BETA.
  11. "In vitro modulation of the interaction between HA95 and LAP2beta by cAMP signaling."
    Martins S.B., Marstad A., Collas P.
    Biochemistry 42:10456-10461(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  12. "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: implications for nuclear toxicity in Huntington's disease pathogenesis."
    Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.
    NeuroMolecular Med. 7:297-310(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. "A cancer-associated RING finger protein, RNF43, is a ubiquitin ligase that interacts with a nuclear protein, HAP95."
    Sugiura T., Yamaguchi A., Miyamoto K.
    Exp. Cell Res. 314:1519-1528(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF43.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292 AND SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAKP8L_HUMAN
AccessioniPrimary (citable) accession number: Q9ULX6
Secondary accession number(s): B4DJ74
, B5BU90, O94792, Q96J58, Q9NRQ0, Q9UGM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 18, 2010
Last modified: June 24, 2015
This is version 144 of the entry and version 3 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 19
    Human chromosome 19: 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.