Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adaptin ear-binding coat-associated protein 1

Gene

Necap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in endocytosis.By similarity1 Publication

GO - Biological processi

  • endocytosis Source: UniProtKB
  • protein transport Source: UniProtKB-KW

Keywordsi

Biological processEndocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-432722 Golgi Associated Vesicle Biogenesis
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Adaptin ear-binding coat-associated protein 1
Alternative name(s):
NECAP endocytosis-associated protein 1
Short name:
NECAP-1
Gene namesi
Name:Necap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1914852 Necap1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi270S → D: Loss of binding to AP-2 and can bind to AP-1; when associated with G-273. 1
Mutagenesisi272W → A, F or Y: Loss of binding to AP-2. 1 Publication1
Mutagenesisi273V → A, D, E or I: No effect on binding to AP-2. 1 Publication1
Mutagenesisi273V → G: Loss of binding to AP-2 and can bind to AP-1; when associated with D-270. 1 Publication1
Mutagenesisi273V → L, N, P or S: Loss of binding to AP-2. 1 Publication1
Mutagenesisi274Q → A, M, N, S or T: No effect on binding to AP-2. 1 Publication1
Mutagenesisi275F → A, F or Y: Loss of binding to AP-2. 1 Publication1
Mutagenesisi275F → W: No effect on binding to AP-2. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002130681 – 275Adaptin ear-binding coat-associated protein 1Add BLAST275

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei211PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9CR95
PaxDbiQ9CR95
PRIDEiQ9CR95

PTM databases

iPTMnetiQ9CR95
PhosphoSitePlusiQ9CR95

Expressioni

Tissue specificityi

Expressed primarily in brain (at protein level).1 Publication

Developmental stagei

Expressed in the brain and spinal cord at 14.5 dpc (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000030327
CleanExiMM_NECAP1
ExpressionAtlasiQ9CR95 baseline and differential
GenevisibleiQ9CR95 MM

Interactioni

Subunit structurei

Interacts with AP1G1 and AP2A1 components of the adapter protein complexes AP-1 and AP-2. Interacts with the GAE domain proteins GGA1, GGA2 and GGA3.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

DIPiDIP-44062N
IntActiQ9CR95, 16 interactors
MINTiQ9CR95
STRINGi10090.ENSMUSP00000032477

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 21Combined sources7
Beta strandi27 – 30Combined sources4
Helixi33 – 36Combined sources4
Beta strandi39 – 41Combined sources3
Beta strandi43 – 50Combined sources8
Beta strandi53 – 61Combined sources9
Beta strandi70 – 74Combined sources5
Beta strandi82 – 84Combined sources3
Beta strandi92 – 98Combined sources7
Turni99 – 101Combined sources3
Beta strandi102 – 109Combined sources8
Helixi113 – 127Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TQZNMR-A1-133[»]
ProteinModelPortaliQ9CR95
SMRiQ9CR95
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CR95

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi252 – 255WXXF motif 14
Motifi272 – 275WXXF motif 24

Domaini

The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Selective binding to the GAE domains of AP-1 or to the alpha-ear domain of AP-2 is tuned by the acidic context surrounding the motif and the properties of the second residue of the motif itself. The WXXF motif 1, which is preceded by an acidic residue and has a glycine in second position mediates specific interaction with AP-1. The WXXF motif 2, which is followed by the C-terminal carboxyl group negative charge, allows specific interaction with AP-2.

Sequence similaritiesi

Belongs to the NECAP family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2500 Eukaryota
ENOG41113PS LUCA
GeneTreeiENSGT00390000009359
HOVERGENiHBG060621
InParanoidiQ9CR95
KOiK20069
OMAiERTDSFD
OrthoDBiEOG091G0PZV
PhylomeDBiQ9CR95
TreeFamiTF314482

Family and domain databases

CDDicd13228 PHear_NECAP, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR012466 NECAP_PHear
IPR011993 PH-like_dom_sf
PfamiView protein in Pfam
PF07933 DUF1681, 1 hit

Sequencei

Sequence statusi: Complete.

Q9CR95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAELEYESV LCVKPDVSVY RIPPRASNRG YRASDWKLDQ PDWTGRLRIT
60 70 80 90 100
SKGKIAYIKL EDKVSGELFA QAPVEQYPGI AVETVTDSSR YFVIRIQDGT
110 120 130 140 150
GRSAFIGIGF TDRGDAFDFN VSLQDHFKWV KQETEISKES QEMDNRPKLD
160 170 180 190 200
LGFKEGQTIK LSIGNITAKK GGASKPRASG TGGLSLLPPP PGGKVTIPPP
210 220 230 240 250
SSSVAISNHV TPPPIPKSNH GGNDSDILLD LDSPAPVSTS APAPVSTSND
260 270
LWGDFSTASS SVPNQAPQPS NWVQF
Length:275
Mass (Da):29,639
Last modified:July 5, 2004 - v2
Checksum:iB238B083746FF915
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004805 mRNA Translation: BAB23577.2
AK005263 mRNA Translation: BAB23915.2
AK081598 mRNA Translation: BAC38266.1
AK168500 mRNA Translation: BAE40385.1
BC011466 mRNA Translation: AAH11466.2
BK000656 mRNA Translation: DAA01433.1
CCDSiCCDS20505.1
RefSeqiNP_080543.2, NM_026267.2
UniGeneiMm.288114

Genome annotation databases

EnsembliENSMUST00000032477; ENSMUSP00000032477; ENSMUSG00000030327
GeneIDi67602
KEGGimmu:67602
UCSCiuc009dpt.1 mouse

Similar proteinsi

Entry informationi

Entry nameiNECP1_MOUSE
AccessioniPrimary (citable) accession number: Q9CR95
Secondary accession number(s): Q3TH13, Q78JW3, Q8C4P1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: March 28, 2018
This is version 120 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health