Q9H2P0 (ADNP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Activity-dependent neuroprotector homeobox protein

Alternative name(s):
Activity-dependent neuroprotective protein

Gene names

Name:	ADNP
Synonyms:	ADNP1, KIAA0784

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	1102 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Potential transcription factor. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation.
Subcellular location	Nucleus Potential.
Tissue specificity	Widely expressed. Strong expression in heart, skeletal muscle, kidney and placenta. In brain, expression is stronger in the cerebellum and cortex regions. No expression detected in the colon. Strong increase of expression in colon and breast cancer tissues.
Miscellaneous	When isolated from the sequence, neuroprotective peptide (NAP) provides neuroprotection against the beta-amyloid peptide.
Sequence similarities	Contains 9 C2H2-type zinc fingers. Contains 1 homeobox DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Homeobox Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX1	P83916	2	EBI-1764854,EBI-78129
CBX3	Q13185	2	EBI-1764854,EBI-78176
CBX5	P45973	2	EBI-1764854,EBI-78219

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1102	1102	Activity-dependent neuroprotector homeobox protein		PRO_0000048807
Regions
	Zinc finger	74 – 97	24	C2H2-type 1
	Zinc finger	107 – 129	23	C2H2-type 2; atypical
	Zinc finger	165 – 188	24	C2H2-type 3
	Zinc finger	221 – 244	24	C2H2-type 4
	Zinc finger	447 – 469	23	C2H2-type 5; atypical
	Zinc finger	489 – 510	22	C2H2-type 6; atypical
	Zinc finger	512 – 535	24	C2H2-type 7
	Zinc finger	622 – 647	26	C2H2-type 8; atypical
	Zinc finger	662 – 686	25	C2H2-type 9; atypical
	DNA binding	754 – 814	61	Homeobox
	Region	354 – 361	8	Neuroprotective peptide (NAP)
Amino acid modifications
	Modified residue	98	1	Phosphoserine Ref.7 Ref.13 Ref.15
	Modified residue	409	1	Phosphoserine Ref.10 Ref.15
	Modified residue	413	1	Phosphoserine Ref.8
	Modified residue	709	1	Phosphoserine Ref.10 Ref.13
	Modified residue	736	1	Phosphoserine Ref.10 Ref.11
	Modified residue	805	1	Phosphoserine Ref.13
	Modified residue	876	1	Phosphoserine Ref.10
	Modified residue	878	1	Phosphoserine Ref.10
	Modified residue	921	1	Phosphoserine Ref.15
	Modified residue	953	1	Phosphoserine Ref.7 Ref.11 Ref.13 Ref.15
	Modified residue	955	1	Phosphoserine Ref.7 Ref.11 Ref.13
	Modified residue	1035	1	N6-acetyllysine Ref.12
	Modified residue	1042	1	N6-acetyllysine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Q9H2P0 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 4132E3EF814AF43B	FASTA	1,102	123,563
	10 20 30 40 50 60 MFQLPVNNLG SLRKARKTVK KILSDIGLEY CKEHIEDFKQ FEPNDFYLKN TTWEDVGLWD 70 80 90 100 110 120 PSLTKNQDYR TKPFCCSACP FSSKFFSAYK SHFRNVHSED FENRILLNCP YCTFNADKKT 130 140 150 160 170 180 LETHIKIFHA PNASAPSSSL STFKDKNKND GLKPKQADSV EQAVYYCKKC TYRDPLYEIV 190 200 210 220 230 240 RKHIYREHFQ HVAAPYIAKA GEKSLNGAVP LGSNAREESS IHCKRCLFMP KSYEALVQHV 250 260 270 280 290 300 IEDHERIGYQ VTAMIGHTNV VVPRSKPLML IAPKPQDKKS MGLPPRIGSL ASGNVRSLPS 310 320 330 340 350 360 QQMVNRLSIP KPNLNSTGVN MMSSVHLQQN NYGVKSVGQG YSVGQSMRLG LGGNAPVSIP 370 380 390 400 410 420 QQSQSVKQLL PSGNGRSYGL GSEQRSQAPA RYSLQSANAS SLSSGQLKSP SLSQSQASRV 430 440 450 460 470 480 LGQSSSKPAA AATGPPPGNT SSTQKWKICT ICNELFPENV YSVHFEKEHK AEKVPAVANY 490 500 510 520 530 540 IMKIHNFTSK CLYCNRYLPT DTLLNHMLIH GLSCPYCRST FNDVEKMAAH MRMVHIDEEM 550 560 570 580 590 600 GPKTDSTLSF DLTLQQGSHT NIHLLVTTYN LRDAPAESVA YHAQNNPPVP PKPQPKVQEK 610 620 630 640 650 660 ADIPVKSSPQ AAVPYKKDVG KTLCPLCFSI LKGPISDALA HHLRERHQVI QTVHPVEKKL 670 680 690 700 710 720 TYKCIHCLGV YTSNMTASTI TLHLVHCRGV GKTQNGQDKT NAPSRLNQSP SLAPVKRTYE 730 740 750 760 770 780 QMEFPLLKKR KLDDDSDSPS FFEEKPEEPV VLALDPKGHE DDSYEARKSF LTKYFNKQPY 790 800 810 820 830 840 PTRREIEKLA ASLWLWKSDI ASHFSNKRKK CVRDCEKYKP GVLLGFNMKE LNKVKHEMDF 850 860 870 880 890 900 DAEWLFENHD EKDSRVNASK TADKKLNLGK EDDSSSDSFE NLEEESNESG SPFDPVFEVE 910 920 930 940 950 960 PKISNDNPEE HVLKVIPEDA SESEEKLDQK EDGSKYETIH LTEEPTKLMH NASDSEVDQD 970 980 990 1000 1010 1020 DVVEWKDGAS PSESGPGSQQ VSDFEDNTCE MKPGTWSDES SQSEDARSSK PAAKKKATMQ 1030 1040 1050 1060 1070 1080 GDREQLKWKN SSYGKVEGFW SKDQSQWKNA SENDERLSNP QIEWQNSTID SEDGEQFDNM 1090 1100 TDGVAEPMHG SLAGVKLSSQ QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the human activity-dependent neuroprotective protein." Zamostiano R., Pinhasov A., Gelber E., Steingart R.A., Seroussi E., Giladi E., Bassan M., Wollman Y., Eyre H.J., Mulley J.C., Brenneman D.E., Gozes I. J. Biol. Chem. 276:708-714(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Lymph.
[5]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-1102. Tissue: Brain.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-1102. Tissue: Uterus.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-953 AND SER-955, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"NAP and D-SAL: neuroprotection against the beta amyloid peptide (1-42)." Gozes I., Divinski I., Piltzer I. BMC Neurosci. 9:S3-S3(2008) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF NAP PEPTIDE.
[10]	"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 SER-409; SER-709; SER-736; SER-876 AND SER-878, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736; SER-953 AND SER-955, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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-1035 AND LYS-1042, MASS SPECTROMETRY.
[13]	"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-98; SER-709; SER-805; SER-953 AND SER-955, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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-98; SER-409; SER-921 AND SER-953, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF250860 mRNA. Translation: AAG47651.1. AL034553 Genomic DNA. Translation: CAB53748.2. CH471077 Genomic DNA. Translation: EAW75611.1. CH471077 Genomic DNA. Translation: EAW75612.1. BC090933 mRNA. Translation: AAH90933.1. AB018327 mRNA. Translation: BAA34504.1. AL080163 mRNA. Translation: CAB45752.1.
IPI	IPI00022215.
PIR	T12546.
RefSeq	NP_056154.1. NM_015339.2. NP_852107.1. NM_181442.1.
UniGene	Hs.570355.
3D structure databases
ProteinModelPortal	Q9H2P0.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47288N.
IntAct	Q9H2P0. 8 interactions.
MINT	MINT-1626775.
STRING	9606.ENSP00000342905.
PTM databases
PhosphoSite	Q9H2P0.
Polymorphism databases
DMDM	24636245.
Proteomic databases
PaxDb	Q9H2P0.
PeptideAtlas	Q9H2P0.
PRIDE	Q9H2P0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000349014; ENSP00000342905; ENSG00000101126. ENST00000371602; ENSP00000360662; ENSG00000101126. ENST00000396029; ENSP00000379346; ENSG00000101126. ENST00000396032; ENSP00000379349; ENSG00000101126.
GeneID	23394.
KEGG	hsa:23394.
UCSC	uc002xvt.1. human.
Organism-specific databases
CTD	23394.
GeneCards	GC20M049505.
HGNC	HGNC:15766. ADNP.
HPA	HPA006371.
MIM	611386. gene.
neXtProt	NX_Q9H2P0.
PharmGKB	PA24582.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG41028.
HOGENOM	HOG000232088.
HOVERGEN	HBG024319.
InParanoid	Q9H2P0.
OMA	LGFNMKE.
OrthoDB	EOG4VHK5N.
PhylomeDB	Q9H2P0.
Gene expression databases
ArrayExpress	Q9H2P0.
Bgee	Q9H2P0.
CleanEx	HS_ADNP.
Genevestigator	Q9H2P0.
GermOnline	ENSG00000101126. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.60. 1 hit.
InterPro	IPR001356. Homeodomain. IPR009057. Homeodomain-like. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. [Graphical view]
Pfam	PF00046. Homeobox. 1 hit. [Graphical view]
SMART	SM00389. HOX. 1 hit. SM00355. ZnF_C2H2. 8 hits. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit.
PROSITE	PS00027. HOMEOBOX_1. False negative. PS50071. HOMEOBOX_2. 1 hit. PS00028. ZINC_FINGER_C2H2_1. 1 hit. PS50157. ZINC_FINGER_C2H2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ADNP. human.
GenomeRNAi	23394.
NextBio	45527.
SOURCE	Search...

Entry information

Entry name

ADNP_HUMAN

Accession

Primary (citable) accession number: Q9H2P0
Secondary accession number(s): E1P5Y2 , O94881, Q5BKU2, Q9UG34

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 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.