Q9ULX6 (AKP8L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	AKAP8L
Synonyms:	NAKAP, NAKAP95
ORF Names:	HRIHFB2018

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	646 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with PRPF40A By similarity. Binds to the C-terminal of RNA helicase A and to TMPO-beta. Interacts with RNF43. Ref.10 Ref.13
Subcellular location	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. Ref.9 Ref.12
Tissue specificity	Expressed in the brain cortex (at protein level). Ref.12
Post-translational modification	Phosphorylated on serine or threonine residues possibly by PKA. Ref.11
Sequence similarities	Belongs to the AKAP95 family. Contains 2 C2H2 AKAP95-type zinc fingers.
Sequence caution	The sequence AAF86048.1 differs from that shown. Reason: Frameshift at position 553. The sequence BAA34791.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	DEAD/H-box RNA helicase binding Traceable author statement Ref.3. Source: UniProtKB DNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNF43	Q68DV7	2	EBI-357530,EBI-1647060

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9ULX6-1)

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 (identifier: Q9ULX6-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 646	646	A-kinase anchor protein 8-like		PRO_0000075384
Regions
	Zinc finger	389 – 413	25	C2H2 AKAP95-type 1
	Zinc finger	482 – 507	26	C2H2 AKAP95-type 2
	Motif	274 – 279	6	Nuclear localization signal Potential
	Motif	362 – 364	3	Nuclear localization signal Potential
	Compositional bias	41 – 52	12	Gly/Tyr-rich
	Compositional bias	589 – 597	9	Pro-rich
	Compositional bias	602 – 608	7	Pro-rich
Amino acid modifications
	Modified residue	257	1	N6-acetyllysine Ref.16
	Modified residue	283	1	Phosphoserine Ref.14 Ref.17 Ref.18
	Modified residue	292	1	Phosphothreonine Ref.15
	Modified residue	297	1	Phosphoserine Ref.15
Natural variations
	Alternative sequence	61 – 121	61	Missing in isoform 2.		VSP_044426
	Natural variant	458	1	H → Q. Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.19 Corresponds to variant rs2058322 [ dbSNP | Ensembl ].		VAR_068822
Experimental info
	Sequence conflict	100	1	D → N in AAF86048. Ref.3
	Sequence conflict	189	1	S → N in AAF86048. Ref.3
	Sequence conflict	351 – 358	8	ALTTQDEN → EFSWGAWC in BAA34791. Ref.9
	Sequence conflict	599 – 616	18	AVSPP…EEGAV → GRVAATAAAPRRRRRRAPW in AAF86048. Ref.3
	Sequence conflict	641 – 646	6	GGGGAP → EGRRGRPV in AAF86048. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: EED855A81BB06585	FASTA	646	71,649
	10 20 30 40 50 60 MSYTGFVQGS ETTLQSTYSD TSAQPTCDYG YGTWNSGTNR GYEGYGYGYG YGQDNTTNYG 70 80 90 100 110 120 YGMATSHSWE MPSSDTNANT SASGSASADS VLSRINQRLD MVPHLETDMM QGGVYGSGGE 130 140 150 160 170 180 RYDSYESCDS RAVLSERDLY RSGYDYSELD PEMEMAYEGQ YDAYRDQFRM RGNDTFGPRA 190 200 210 220 230 240 QGWARDARSG RPMASGYGRM WEDPMGARGQ CMSGASRLPS LFSQNIIPEY GMFQGMRGGG 250 260 270 280 290 300 AFPGGSRFGF GFGNGMKQMR RTWKTWTTAD FRTKKKKRKQ GGSPDEPDSK ATRTDCSDNS 310 320 330 340 350 360 DSDNDEGTEG EATEGLEGTE AVEKGSRVDG EDEEGKEDGR EEGKEDPEKG ALTTQDENGQ 370 380 390 400 410 420 TKRKLQAGKK SQDKQKKRQR DRMVERIQFV CSLCKYRTFY EDEMASHLDS KFHKEHFKYV 430 440 450 460 470 480 GTKLPKQTAD FLQEYVTNKT KKTEELRKTV EDLDGLIHQI YRDQDLTQEI AMEHFVKKVE 490 500 510 520 530 540 AAHCAACDLF IPMQFGIIQK HLKTMDHNRN RRLMMEQSKK SSLMVARSIL NNKLISKKLE 550 560 570 580 590 600 RYLKGENPFT DSPEEEKEQE EAEGGALDEG AQGEAAGISE GAEGVPAQPP VPPEPAPGAV 610 620 630 640 SPPPPPPPEE EEEGAVPLLG GALQRQIRGI PGLDVEDDEE GGGGAP
	Isoform 2 [UniParc]. Checksum: 460F073AC534A1B9	FASTA	585	65,230
	10 20 30 40 50 60 MSYTGFVQGS ETTLQSTYSD TSAQPTCDYG YGTWNSGTNR GYEGYGYGYG YGQDNTTNYG 70 80 90 100 110 120 YDSYESCDSR AVLSERDLYR SGYDYSELDP EMEMAYEGQY DAYRDQFRMR GNDTFGPRAQ 130 140 150 160 170 180 GWARDARSGR PMASGYGRMW EDPMGARGQC MSGASRLPSL FSQNIIPEYG MFQGMRGGGA 190 200 210 220 230 240 FPGGSRFGFG FGNGMKQMRR TWKTWTTADF RTKKKKRKQG GSPDEPDSKA TRTDCSDNSD 250 260 270 280 290 300 SDNDEGTEGE ATEGLEGTEA VEKGSRVDGE DEEGKEDGRE EGKEDPEKGA LTTQDENGQT 310 320 330 340 350 360 KRKLQAGKKS QDKQKKRQRD RMVERIQFVC SLCKYRTFYE DEMASHLDSK FHKEHFKYVG 370 380 390 400 410 420 TKLPKQTADF LQEYVTNKTK KTEELRKTVE DLDGLIHQIY RDQDLTQEIA MEHFVKKVEA 430 440 450 460 470 480 AHCAACDLFI PMQFGIIQKH LKTMDHNRNR RLMMEQSKKS SLMVARSILN NKLISKKLER 490 500 510 520 530 540 YLKGENPFTD SPEEEKEQEE AEGGALDEGA QGEAAGISEG AEGVPAQPPV PPEPAPGAVS 550 560 570 580 PPPPPPPEEE EEGAVPLLGG ALQRQIRGIP GLDVEDDEEG GGGAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292 AND SER-297, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, MASS SPECTROMETRY.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-458, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00297455.
RefSeq	NP_055186.2. NM_014371.2.
UniGene	Hs.399800.
3D structure databases
ProteinModelPortal	Q9ULX6.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27541N.
IntAct	Q9ULX6. 10 interactions.
MINT	MINT-1134534.
STRING	9606.ENSP00000380557.
PTM databases
PhosphoSite	Q9ULX6.
Polymorphism databases
DMDM	296439446.
Proteomic databases
PaxDb	Q9ULX6.
PRIDE	Q9ULX6.
Protocols and materials databases
DNASU	26993.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000397410; ENSP00000380557; ENSG00000011243. ENST00000595465; ENSP00000470952; ENSG00000011243.
GeneID	26993.
KEGG	hsa:26993.
UCSC	uc002naw.1. human. uc010xoh.1. human.
Organism-specific databases
CTD	26993.
GeneCards	GC19M015490.
H-InvDB	HIX0014850. HIX0115658.
HGNC	HGNC:29857. AKAP8L.
HPA	HPA042485. HPA042546.
MIM	609475. gene.
neXtProt	NX_Q9ULX6.
PharmGKB	PA134867364.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG47695.
HOGENOM	HOG000169111.
HOVERGEN	HBG104297.
InParanoid	Q9ULX6.
KO	K15978.
OMA	WEMPSSD.
OrthoDB	EOG434W6D.
Gene expression databases
ArrayExpress	Q9ULX6.
Bgee	Q9ULX6.
CleanEx	HS_AKAP8L.
Genevestigator	Q9ULX6.
GermOnline	ENSG00000011243. Homo sapiens.
Family and domain databases
InterPro	IPR007071. AKAP95. IPR015880. Znf_C2H2-like. [Graphical view]
PANTHER	PTHR12190. PTHR12190. 1 hit.
Pfam	PF04988. AKAP95. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AKAP8L. human.
GenomeRNAi	26993.
NextBio	35472456.
SOURCE	Search...

Entry information

Entry name

AKP8L_HUMAN

Accession

Primary (citable) accession number: Q9ULX6
Secondary accession number(s): B4DJ74 , B5BU90, O94792, Q96J58, Q9NRQ0, Q9UGM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 18, 2010
Last modified:	May 29, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.