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Protein

Activity-dependent neuroprotector homeobox protein

Gene

ADNP

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

Functioni

Potential transcription factor. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri74 – 9724C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri107 – 12923C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri165 – 18824C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri221 – 24424C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri447 – 46923C2H2-type 5; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri489 – 51022C2H2-type 6; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri512 – 53524C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri622 – 64726C2H2-type 8; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri662 – 68625C2H2-type 9; atypicalPROSITE-ProRule annotationAdd
BLAST
DNA bindingi754 – 81461HomeoboxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Activity-dependent neuroprotector homeobox protein
Alternative name(s):
Activity-dependent neuroprotective protein
Gene namesi
Name:ADNP
Synonyms:ADNP1, KIAA0784
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15766. ADNP.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Helsmoortel-van der Aa syndrome (HVDAS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by intellectual disability, autism spectrum disorder, and dysmorphic facial features including prominent forehead, high hairline, downslanting palpebral fissures, notched eyelids, broad nasal bridge, thin upper lip, and smooth philtrum.
See also OMIM:615873

Keywords - Diseasei

Autism spectrum disorder, Mental retardation

Organism-specific databases

MalaCardsiADNP.
MIMi615873. phenotype.
Orphaneti404448. ADNP-related multiple congenital anomalies-intellectual disability-autism spectrum disorder.
PharmGKBiPA24582.

Polymorphism and mutation databases

DMDMi24636245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11021102Activity-dependent neuroprotector homeobox proteinPRO_0000048807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981PhosphoserineCombined sources
Cross-linki144 – 144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki266 – 266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki279 – 279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki367 – 367Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki408 – 408Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei413 – 4131PhosphoserineCombined sources
Cross-linki427 – 427Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki600 – 600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki606 – 606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei608 – 6081PhosphoserineCombined sources
Cross-linki621 – 621Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei709 – 7091PhosphoserineCombined sources
Cross-linki716 – 716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki731 – 731Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei736 – 7361PhosphoserineCombined sources
Modified residuei738 – 7381PhosphoserineBy similarity
Modified residuei805 – 8051PhosphoserineCombined sources
Modified residuei876 – 8761PhosphoserineCombined sources
Modified residuei878 – 8781PhosphoserineCombined sources
Modified residuei886 – 8861PhosphoserineBy similarity
Modified residuei889 – 8891PhosphoserineBy similarity
Modified residuei921 – 9211PhosphoserineCombined sources
Cross-linki930 – 930Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei953 – 9531PhosphoserineCombined sources
Modified residuei955 – 9551PhosphoserineCombined sources
Modified residuei1035 – 10351N6-acetyllysine; alternateCombined sources
Cross-linki1035 – 1035Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1042 – 10421N6-acetyllysineCombined sources
Modified residuei1071 – 10711PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9H2P0.
MaxQBiQ9H2P0.
PaxDbiQ9H2P0.
PeptideAtlasiQ9H2P0.
PRIDEiQ9H2P0.

PTM databases

iPTMnetiQ9H2P0.
PhosphoSiteiQ9H2P0.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ9H2P0.
CleanExiHS_ADNP.
ExpressionAtlasiQ9H2P0. baseline and differential.
GenevisibleiQ9H2P0. HS.

Organism-specific databases

HPAiHPA006371.
HPA050560.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX1P839162EBI-1764854,EBI-78129
CBX3Q131852EBI-1764854,EBI-78176
CBX5P459732EBI-1764854,EBI-78219

Protein-protein interaction databases

BioGridi116967. 52 interactions.
DIPiDIP-47288N.
IntActiQ9H2P0. 34 interactions.
MINTiMINT-1626775.
STRINGi9606.ENSP00000342905.

Structurei

3D structure databases

ProteinModelPortaliQ9H2P0.
SMRiQ9H2P0. Positions 765-814.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni354 – 3618Neuroprotective peptide (NAP)1 Publication

Sequence similaritiesi

Contains 9 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri74 – 9724C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri107 – 12923C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri165 – 18824C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri221 – 24424C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri447 – 46923C2H2-type 5; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri489 – 51022C2H2-type 6; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri512 – 53524C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri622 – 64726C2H2-type 8; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri662 – 68625C2H2-type 9; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Homeobox, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IIIX. Eukaryota.
ENOG410XYDF. LUCA.
GeneTreeiENSGT00530000063631.
HOGENOMiHOG000232088.
HOVERGENiHBG024319.
InParanoidiQ9H2P0.
OMAiSTGVNMM.
OrthoDBiEOG7GJ6C7.
PhylomeDBiQ9H2P0.
TreeFamiTF328818.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF00046. Homeobox. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS50071. HOMEOBOX_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H2P0-1 [UniParc]FASTAAdd to basket

« Hide

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

QA
Length:1,102
Mass (Da):123,563
Last modified:March 1, 2001 - v1
Checksum:i4132E3EF814AF43B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13433.1.
PIRiT12546.
RefSeqiNP_001269460.1. NM_001282531.1.
NP_001269461.1. NM_001282532.1.
NP_056154.1. NM_015339.3.
NP_852107.1. NM_181442.2.
XP_011527049.1. XM_011528747.1.
UniGeneiHs.293736.
Hs.570355.

Genome annotation databases

EnsembliENST00000349014; ENSP00000342905; ENSG00000101126.
ENST00000371602; ENSP00000360662; ENSG00000101126.
ENST00000396029; ENSP00000379346; ENSG00000101126.
ENST00000396032; ENSP00000379349; ENSG00000101126.
ENST00000621696; ENSP00000483881; ENSG00000101126.
GeneIDi23394.
KEGGihsa:23394.
UCSCiuc002xvt.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13433.1.
PIRiT12546.
RefSeqiNP_001269460.1. NM_001282531.1.
NP_001269461.1. NM_001282532.1.
NP_056154.1. NM_015339.3.
NP_852107.1. NM_181442.2.
XP_011527049.1. XM_011528747.1.
UniGeneiHs.293736.
Hs.570355.

3D structure databases

ProteinModelPortaliQ9H2P0.
SMRiQ9H2P0. Positions 765-814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116967. 52 interactions.
DIPiDIP-47288N.
IntActiQ9H2P0. 34 interactions.
MINTiMINT-1626775.
STRINGi9606.ENSP00000342905.

PTM databases

iPTMnetiQ9H2P0.
PhosphoSiteiQ9H2P0.

Polymorphism and mutation databases

DMDMi24636245.

Proteomic databases

EPDiQ9H2P0.
MaxQBiQ9H2P0.
PaxDbiQ9H2P0.
PeptideAtlasiQ9H2P0.
PRIDEiQ9H2P0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349014; ENSP00000342905; ENSG00000101126.
ENST00000371602; ENSP00000360662; ENSG00000101126.
ENST00000396029; ENSP00000379346; ENSG00000101126.
ENST00000396032; ENSP00000379349; ENSG00000101126.
ENST00000621696; ENSP00000483881; ENSG00000101126.
GeneIDi23394.
KEGGihsa:23394.
UCSCiuc002xvt.3. human.

Organism-specific databases

CTDi23394.
GeneCardsiADNP.
HGNCiHGNC:15766. ADNP.
HPAiHPA006371.
HPA050560.
MalaCardsiADNP.
MIMi611386. gene.
615873. phenotype.
neXtProtiNX_Q9H2P0.
Orphaneti404448. ADNP-related multiple congenital anomalies-intellectual disability-autism spectrum disorder.
PharmGKBiPA24582.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIIX. Eukaryota.
ENOG410XYDF. LUCA.
GeneTreeiENSGT00530000063631.
HOGENOMiHOG000232088.
HOVERGENiHBG024319.
InParanoidiQ9H2P0.
OMAiSTGVNMM.
OrthoDBiEOG7GJ6C7.
PhylomeDBiQ9H2P0.
TreeFamiTF328818.

Miscellaneous databases

ChiTaRSiADNP. human.
GenomeRNAii23394.
PROiQ9H2P0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H2P0.
CleanExiHS_ADNP.
ExpressionAtlasiQ9H2P0. baseline and differential.
GenevisibleiQ9H2P0. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF00046. Homeobox. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS50071. HOMEOBOX_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-709; SER-736; SER-876 AND SER-878, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 AND SER-953, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-409; SER-608; SER-709; SER-736; SER-921; SER-953 AND SER-955, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: INVOLVEMENT IN HVDAS.
  20. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-279; LYS-408; LYS-716; LYS-731; LYS-930 AND LYS-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-266; LYS-367; LYS-408; LYS-427; LYS-621; LYS-716; LYS-731 AND LYS-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-600; LYS-606; LYS-930 AND LYS-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADNP_HUMAN
AccessioniPrimary (citable) accession number: Q9H2P0
Secondary accession number(s): E1P5Y2
, O94881, Q5BKU2, Q9UG34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 142 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

Miscellaneous

When isolated from the sequence, neuroprotective peptide (NAP) provides neuroprotection against the beta-amyloid peptide.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.