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Q9UKG1

- DP13A_HUMAN

UniProt

Q9UKG1 - DP13A_HUMAN

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Protein

DCC-interacting protein 13-alpha

Gene
APPL1, APPL, DIP13A, KIAA1428
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction.2 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. protein binding Source: UniProtKB
  3. protein kinase B binding Source: BHF-UCL

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cell cycle Source: UniProtKB-KW
  3. cell proliferation Source: UniProtKB
  4. insulin receptor signaling pathway Source: BHF-UCL
  5. positive regulation of apoptotic process Source: Reactome
  6. regulation of apoptotic process Source: Reactome
  7. regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  8. regulation of glucose import Source: BHF-UCL
  9. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

ReactomeiREACT_22128. Role of DCC in regulating apoptosis.
SignaLinkiQ9UKG1.

Names & Taxonomyi

Protein namesi
Recommended name:
DCC-interacting protein 13-alpha
Short name:
Dip13-alpha
Alternative name(s):
Adapter protein containing PH domain, PTB domain and leucine zipper motif 1
Gene namesi
Name:APPL1
Synonyms:APPL, DIP13A, KIAA1428
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:24035. APPL1.

Subcellular locationi

Early endosome membrane; Peripheral membrane protein. Nucleus
Note: Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: BHF-UCL
  3. early endosome membrane Source: UniProtKB-SubCell
  4. endosome membrane Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. nucleus Source: UniProtKB
  7. vesicle membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162376755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 709709DCC-interacting protein 13-alphaPRO_0000079985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei399 – 3991Phosphothreonine1 Publication
Modified residuei401 – 4011Phosphoserine1 Publication
Modified residuei410 – 4101Phosphoserine; by PKA1 Publication

Post-translational modificationi

Phosophorylation at Ser-410 by PKA severely impairs binding to OCRL.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UKG1.
PaxDbiQ9UKG1.
PeptideAtlasiQ9UKG1.
PRIDEiQ9UKG1.

PTM databases

PhosphoSiteiQ9UKG1.

Expressioni

Tissue specificityi

High levels in heart, ovary, pancreas and skeletal muscle.1 Publication

Gene expression databases

ArrayExpressiQ9UKG1.
BgeeiQ9UKG1.
CleanExiHS_APPL1.
GenevestigatoriQ9UKG1.

Organism-specific databases

HPAiHPA011138.

Interactioni

Subunit structurei

Binds RAB5A/Rab5 through an N-terminal domain. This interaction is essential for its recruitment to endosomal membranes as well as its role in cell proliferation. Binds DCC and the catalytic domain of the inactive form of AKT2 through its PID domain. Binds PIK3CA and subunits of the NuRD/MeCP1 complex. Interacts with OCRL and INPP5B.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-741243,EBI-741243
ACTN2P356092EBI-741243,EBI-77797
ADIPOR1Q96A546EBI-741243,EBI-1632076
Adipor1Q91VH13EBI-741243,EBI-992398From a different organism.
ADIPOR2Q86V243EBI-741243,EBI-1769445
DSTQ030013EBI-741243,EBI-310758
DYSFO759232EBI-741243,EBI-2799016
EGFRP005332EBI-741243,EBI-297353
HDAC3O153792EBI-741243,EBI-607682
RAB21Q9UL2510EBI-741243,EBI-1056039
RAB5AP2033917EBI-741243,EBI-399437
SYNE2Q8WXH03EBI-741243,EBI-2372294

Protein-protein interaction databases

BioGridi117522. 33 interactions.
DIPiDIP-29322N.
IntActiQ9UKG1. 48 interactions.
MINTiMINT-1177965.
STRINGi9606.ENSP00000288266.

Structurei

Secondary structure

1
709
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Turni12 – 143
Helixi16 – 6651
Helixi67 – 704
Helixi81 – 11030
Helixi112 – 1209
Helixi122 – 15130
Beta strandi152 – 1543
Helixi157 – 21761
Helixi220 – 25738
Helixi259 – 2613
Beta strandi262 – 2654
Turni268 – 2703
Beta strandi281 – 2866
Beta strandi298 – 3058
Beta strandi308 – 3125
Beta strandi320 – 3245
Beta strandi329 – 3335
Beta strandi339 – 3457
Beta strandi348 – 3503
Helixi360 – 37415
Beta strandi499 – 51214
Helixi519 – 53416
Beta strandi542 – 55514
Turni557 – 5593
Beta strandi562 – 5676
Helixi568 – 5703
Beta strandi571 – 5777
Beta strandi580 – 59011
Beta strandi600 – 61011
Helixi612 – 62918

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJ8X-ray1.84A/B492-644[»]
2ELAX-ray2.00A/B493-646[»]
2ELBX-ray2.60A1-376[»]
2Q12X-ray1.79A5-265[»]
2Q13X-ray2.05A5-385[»]
2Z0NX-ray1.95A1-275[»]
2Z0OX-ray2.58A1-385[»]
ProteinModelPortaliQ9UKG1.
SMRiQ9UKG1. Positions 4-378, 499-645.

Miscellaneous databases

EvolutionaryTraceiQ9UKG1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 37599PHAdd
BLAST
Domaini496 – 656161PIDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 428428Required for RAB5A binding1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili215 – 25945 Reviewed predictionAdd
BLAST
Coiled coili621 – 67353 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi403 – 41412F&HAdd
BLAST

Domaini

Overexpression of an N-terminal domain (residues 1-319) or a C-terminal region (residues 273-709) has a proapoptotic effect.1 Publication
The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential for binding to OCRL and INPP5B (1 Publication).

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 PID domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG69757.
HOGENOMiHOG000285988.
HOVERGENiHBG051394.
InParanoidiQ9UKG1.
KOiK08733.
OMAiSDVETMQ.
OrthoDBiEOG79PJPK.
PhylomeDBiQ9UKG1.
TreeFamiTF328669.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
2.30.29.30. 2 hits.
InterProiIPR027267. AH/BAR-dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS01179. PID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UKG1-1 [UniParc]FASTAAdd to Basket

« Hide

MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA    50
QNELSAATHL TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH 100
AVLSTQLADA MMFPITQFKE RDLKEILTLK EVFQIASNDH DAAINRYSRL 150
SKKRENDKVK YEVTEDVYTS RKKQHQTMMH YFCALNTLQY KKKIALLEPL 200
LGYMQAQISF FKMGSENLNE QLEEFLANIG TSVQNVRREM DSDIETMQQT 250
IEDLEVASDP LYVPDPDPTK FPVNRNLTRK AGYLNARNKT GLVSSTWDRQ 300
FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK 350
KSSILQAESK KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP 400
SPSFQQRHES LRPAAGQSRP PTARTSSSGS LGSESTNLAA LSLDSLVAPD 450
TPIQFDIISP VCEDQPGQAK AFGQGGRRTN PFGESGGSTK SETEDSILHQ 500
LFIVRFLGSM EVKSDDHPDV VYETMRQILA ARAIHNIFRM TESHLLVTCD 550
CLKLIDPQTQ VTRLTFPLPC VVLYATHQEN KRLFGFVLRT SSGRSESNLS 600
SVCYIFESNN EGEKICDSVG LAKQIALHAE LDRRASEKQK EIERVKEKQQ 650
KELNKQKQIE KDLEEQSRLI AASSRPNQAS SEGQFVVLSS SQSEESDLGE 700
GGKKRESEA 709
Length:709
Mass (Da):79,663
Last modified:May 1, 2000 - v1
Checksum:i4CABECFCF4BB110D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti108 – 1081A → V.
Corresponds to variant rs4381906 [ dbSNP | Ensembl ].
VAR_050958
Natural varianti643 – 6431E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035909
Natural varianti700 – 7001E → G.
Corresponds to variant rs11544593 [ dbSNP | Ensembl ].
VAR_050959

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF169797 mRNA. Translation: AAF04012.1.
AF424738 mRNA. Translation: AAL17835.1.
AB037849 mRNA. Translation: BAA92666.2.
BC028599 mRNA. Translation: AAH28599.1.
CCDSiCCDS2882.1.
RefSeqiNP_036228.1. NM_012096.2.
UniGeneiHs.476415.

Genome annotation databases

EnsembliENST00000288266; ENSP00000288266; ENSG00000157500.
GeneIDi26060.
KEGGihsa:26060.
UCSCiuc003dio.3. human.

Polymorphism databases

DMDMi61213025.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF169797 mRNA. Translation: AAF04012.1 .
AF424738 mRNA. Translation: AAL17835.1 .
AB037849 mRNA. Translation: BAA92666.2 .
BC028599 mRNA. Translation: AAH28599.1 .
CCDSi CCDS2882.1.
RefSeqi NP_036228.1. NM_012096.2.
UniGenei Hs.476415.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EJ8 X-ray 1.84 A/B 492-644 [» ]
2ELA X-ray 2.00 A/B 493-646 [» ]
2ELB X-ray 2.60 A 1-376 [» ]
2Q12 X-ray 1.79 A 5-265 [» ]
2Q13 X-ray 2.05 A 5-385 [» ]
2Z0N X-ray 1.95 A 1-275 [» ]
2Z0O X-ray 2.58 A 1-385 [» ]
ProteinModelPortali Q9UKG1.
SMRi Q9UKG1. Positions 4-378, 499-645.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117522. 33 interactions.
DIPi DIP-29322N.
IntActi Q9UKG1. 48 interactions.
MINTi MINT-1177965.
STRINGi 9606.ENSP00000288266.

PTM databases

PhosphoSitei Q9UKG1.

Polymorphism databases

DMDMi 61213025.

Proteomic databases

MaxQBi Q9UKG1.
PaxDbi Q9UKG1.
PeptideAtlasi Q9UKG1.
PRIDEi Q9UKG1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288266 ; ENSP00000288266 ; ENSG00000157500 .
GeneIDi 26060.
KEGGi hsa:26060.
UCSCi uc003dio.3. human.

Organism-specific databases

CTDi 26060.
GeneCardsi GC03P057237.
HGNCi HGNC:24035. APPL1.
HPAi HPA011138.
MIMi 604299. gene.
neXtProti NX_Q9UKG1.
PharmGKBi PA162376755.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69757.
HOGENOMi HOG000285988.
HOVERGENi HBG051394.
InParanoidi Q9UKG1.
KOi K08733.
OMAi SDVETMQ.
OrthoDBi EOG79PJPK.
PhylomeDBi Q9UKG1.
TreeFami TF328669.

Enzyme and pathway databases

Reactomei REACT_22128. Role of DCC in regulating apoptosis.
SignaLinki Q9UKG1.

Miscellaneous databases

ChiTaRSi APPL1. human.
EvolutionaryTracei Q9UKG1.
GeneWikii APPL1.
GenomeRNAii 26060.
NextBioi 47954.
PROi Q9UKG1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UKG1.
Bgeei Q9UKG1.
CleanExi HS_APPL1.
Genevestigatori Q9UKG1.

Family and domain databases

Gene3Di 1.20.1270.60. 1 hit.
2.30.29.30. 2 hits.
InterProi IPR027267. AH/BAR-dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view ]
Pfami PF00640. PID. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS01179. PID. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2."
    Mitsuuchi Y., Johnson S.W., Sonoda G., Tanno S., Golemis E.A., Testa J.R.
    Oncogene 18:4891-4898(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH AKT2 AND PIK3CA.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DCC.
  3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "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: Testis.
  6. "APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment."
    Miaczynska M., Christoforidis S., Giner A., Shevchenko A., Uttenweiler-Joseph S., Habermann B., Wilm M., Parton R.G., Zerial M.
    Cell 116:445-456(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND NURD/MECP1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway."
    Erdmann K.S., Mao Y., McCrea H.J., Zoncu R., Lee S., Paradise S., Modregger J., Biemesderfer D., Toomre D., De Camilli P.
    Dev. Cell 13:377-390(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OCRL, F&H MOTIF, PHOSPHORYLATION AT SER-410.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1."
    Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.
    Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OCRL, SUBCELLULAR LOCATION.
  12. "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-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway."
    Noakes C.J., Lee G., Lowe M.
    Mol. Biol. Cell 22:606-623(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OCRL.
  15. "Recognition of the F&H motif by the Lowe syndrome protein OCRL."
    Pirruccello M., Swan L.E., Folta-Stogniew E., De Camilli P.
    Nat. Struct. Mol. Biol. 18:789-795(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OCRL, F&H MOTIF.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-643.

Entry informationi

Entry nameiDP13A_HUMAN
AccessioniPrimary (citable) accession number: Q9UKG1
Secondary accession number(s): Q9P2B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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