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Protein

Alpha- and gamma-adaptin-binding protein p34

Gene

AAGAB

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

Functioni

May be involved in endocytic recycling of growth factor receptors such as EGFR.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha- and gamma-adaptin-binding protein p34
Gene namesi
Name:AAGAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:25662. AAGAB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Keratoderma, palmoplantar, punctate 1A (PPKP1A)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant dermatological disorder characterized by multiple hyperkeratotic, centrally indented, papules that develop in early adolescence, or later, and are irregularly distributed on the palms and soles (other palmoplantar keratoses have mostly diffuse hyperkeratinization). In mechanically irritated areas, confluent plaques can be found. Interfamilial and intrafamilial severity shows broad variation. In some cases, PPKP1 is associated with the development of early- and late-onset malignancies, including squamous cell carcinoma.

See also OMIM:148600

Keywords - Diseasei

Palmoplantar keratoderma

Organism-specific databases

MIMi148600. phenotype.
Orphaneti79501. Punctate palmoplantar keratoderma type 1.
PharmGKBiPA165478457.

Polymorphism and mutation databases

DMDMi62286981.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Alpha- and gamma-adaptin-binding protein p34PRO_0000058134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei310 – 3101Phosphoserine4 Publications
Modified residuei311 – 3111Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6PD74.
PaxDbiQ6PD74.
PeptideAtlasiQ6PD74.
PRIDEiQ6PD74.

PTM databases

PhosphoSiteiQ6PD74.

Expressioni

Tissue specificityi

Widely expressed, including in skin and keratinocytes, with highest levels in adrenal gland, rectum and thymus.2 Publications

Gene expression databases

BgeeiQ6PD74.
ExpressionAtlasiQ6PD74. baseline and differential.
GenevisibleiQ6PD74. HS.

Organism-specific databases

HPAiHPA039371.
HPA040174.

Interactioni

Subunit structurei

Associated with AP-1 and AP-2 complexes.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AP1S3Q96PC33EBI-719906,EBI-3923129
AP2S1P536803EBI-719906,EBI-297662
HEATR1Q96ES53EBI-719906,EBI-10285245

Protein-protein interaction databases

BioGridi122835. 15 interactions.
IntActiQ6PD74. 5 interactions.
MINTiMINT-1373784.
STRINGi9606.ENSP00000261880.

Structurei

3D structure databases

ProteinModelPortaliQ6PD74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG271587.
GeneTreeiENSGT00390000007218.
HOGENOMiHOG000115322.
InParanoidiQ6PD74.
OMAiVMKNDRN.
OrthoDBiEOG7DZ8PB.
PhylomeDBiQ6PD74.
TreeFamiTF328856.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR019341. Alpha/Gamma-adaptin-bd_p34.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF10199. Adaptin_binding. 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: Q6PD74-1) [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
MAAGVPCALV TSCSSVFSGD QLVQHILGTE DLIVEVTSND AVRFYPWTID
60 70 80 90 100
NKYYSADINL CVVPNKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP
110 120 130 140 150
LAKAWLPEVM ILVCDRVSED GINRQKAQEW CIKHGFELVE LSPEELPEED
160 170 180 190 200
DDFPESTGVK RIVQALNANV WSNVVMKNDR NQGFSLLNSL TGTNHSIGSA
210 220 230 240 250
DPCHPEQPHL PAADSTESLS DHRGGASNTT DAQVDSIVDP MLDLDIQELA
260 270 280 290 300
SLTTGGGDVE NFERLFSKLK EMKDKAATLP HEQRKVHAEK VAKAFWMAIG
310
GDRDEIEGLS SDEEH
Length:315
Mass (Da):34,594
Last modified:July 5, 2004 - v1
Checksum:iC1C765B4F9717E0B
GO
Isoform 2 (identifier: Q6PD74-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-109: Missing.

Note: No experimental confirmation available.
Show »
Length:206
Mass (Da):22,719
Checksum:i28477F7B5DDAB3A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261I → T in CAB66649 (PubMed:11230166).Curated
Sequence conflicti26 – 261I → T in CAG38571 (Ref. 3) Curated
Sequence conflicti77 – 771V → A in CAG38571 (Ref. 3) Curated
Sequence conflicti88 – 881Q → R in CAB66649 (PubMed:11230166).Curated
Sequence conflicti88 – 881Q → R in CAG38571 (Ref. 3) Curated
Sequence conflicti131 – 1311C → S in CAB66649 (PubMed:11230166).Curated
Sequence conflicti131 – 1311C → S in CAG38571 (Ref. 3) Curated
Sequence conflicti265 – 2651L → P in CAB66649 (PubMed:11230166).Curated
Sequence conflicti265 – 2651L → P in CAG38571 (Ref. 3) Curated
Sequence conflicti313 – 3131E → G in CAB66649 (PubMed:11230166).Curated
Sequence conflicti313 – 3131E → G in CAG38571 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321I → L.3 Publications
Corresponds to variant rs7173826 [ dbSNP | Ensembl ].
VAR_021533

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 109109Missing in isoform 2. 1 PublicationVSP_054597Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136715 mRNA. Translation: CAB66649.1.
AK021568 mRNA. Translation: BAB13845.1.
AK294402 mRNA. Translation: BAG57655.1.
CR533540 mRNA. Translation: CAG38571.1.
AC012568 Genomic DNA. No translation available.
AC110292 Genomic DNA. No translation available.
BC001975 mRNA. Translation: AAH01975.1.
BC047026 mRNA. Translation: AAH47026.1.
BC058886 mRNA. Translation: AAH58886.1.
CCDSiCCDS42050.1. [Q6PD74-1]
CCDS61679.1. [Q6PD74-2]
RefSeqiNP_001258814.1. NM_001271885.1. [Q6PD74-2]
NP_001258815.1. NM_001271886.1. [Q6PD74-2]
NP_078942.3. NM_024666.4. [Q6PD74-1]
XP_011520322.1. XM_011522020.1. [Q6PD74-2]
UniGeneiHs.254642.
Hs.602761.

Genome annotation databases

EnsembliENST00000261880; ENSP00000261880; ENSG00000103591.
ENST00000542650; ENSP00000440735; ENSG00000103591. [Q6PD74-2]
ENST00000561452; ENSP00000453263; ENSG00000103591. [Q6PD74-2]
GeneIDi79719.
KEGGihsa:79719.
UCSCiuc002aqk.5. human. [Q6PD74-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136715 mRNA. Translation: CAB66649.1.
AK021568 mRNA. Translation: BAB13845.1.
AK294402 mRNA. Translation: BAG57655.1.
CR533540 mRNA. Translation: CAG38571.1.
AC012568 Genomic DNA. No translation available.
AC110292 Genomic DNA. No translation available.
BC001975 mRNA. Translation: AAH01975.1.
BC047026 mRNA. Translation: AAH47026.1.
BC058886 mRNA. Translation: AAH58886.1.
CCDSiCCDS42050.1. [Q6PD74-1]
CCDS61679.1. [Q6PD74-2]
RefSeqiNP_001258814.1. NM_001271885.1. [Q6PD74-2]
NP_001258815.1. NM_001271886.1. [Q6PD74-2]
NP_078942.3. NM_024666.4. [Q6PD74-1]
XP_011520322.1. XM_011522020.1. [Q6PD74-2]
UniGeneiHs.254642.
Hs.602761.

3D structure databases

ProteinModelPortaliQ6PD74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122835. 15 interactions.
IntActiQ6PD74. 5 interactions.
MINTiMINT-1373784.
STRINGi9606.ENSP00000261880.

PTM databases

PhosphoSiteiQ6PD74.

Polymorphism and mutation databases

DMDMi62286981.

Proteomic databases

MaxQBiQ6PD74.
PaxDbiQ6PD74.
PeptideAtlasiQ6PD74.
PRIDEiQ6PD74.

Protocols and materials databases

DNASUi79719.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261880; ENSP00000261880; ENSG00000103591.
ENST00000542650; ENSP00000440735; ENSG00000103591. [Q6PD74-2]
ENST00000561452; ENSP00000453263; ENSG00000103591. [Q6PD74-2]
GeneIDi79719.
KEGGihsa:79719.
UCSCiuc002aqk.5. human. [Q6PD74-1]

Organism-specific databases

CTDi79719.
GeneCardsiGC15M067493.
HGNCiHGNC:25662. AAGAB.
HPAiHPA039371.
HPA040174.
MIMi148600. phenotype.
614888. gene.
neXtProtiNX_Q6PD74.
Orphaneti79501. Punctate palmoplantar keratoderma type 1.
PharmGKBiPA165478457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG271587.
GeneTreeiENSGT00390000007218.
HOGENOMiHOG000115322.
InParanoidiQ6PD74.
OMAiVMKNDRN.
OrthoDBiEOG7DZ8PB.
PhylomeDBiQ6PD74.
TreeFamiTF328856.

Miscellaneous databases

ChiTaRSiAAGAB. human.
GeneWikiiFLJ11506.
GenomeRNAii79719.
NextBioi35471658.
PROiQ6PD74.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PD74.
ExpressionAtlasiQ6PD74. baseline and differential.
GenevisibleiQ6PD74. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR019341. Alpha/Gamma-adaptin-bd_p34.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF10199. Adaptin_binding. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-132.
    Tissue: Fetal kidney.
  2. "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] (ISOFORMS 1 AND 2), VARIANT LEU-132.
    Tissue: Amygdala and Embryo.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-132.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Cervix and Uterus.
  6. "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-310 AND SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-310 AND SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-310 AND SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-310 AND SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: INVOLVEMENT IN PPKP1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. Cited for: INVOLVEMENT IN PPKP1A, FUNCTION, IDENTIFICATION IN AP-1 AND AP-2 COMPLEXES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAAGAB_HUMAN
AccessioniPrimary (citable) accession number: Q6PD74
Secondary accession number(s): B4DG44
, Q6FI86, Q7Z5X9, Q9H0P1, Q9HAK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 99 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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

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.