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Protein

Adaptin ear-binding coat-associated protein 1

Gene

Necap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in endocytosis.By similarity1 Publication

GO - Biological processi

  • endocytosis Source: UniProtKB
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-432722. Golgi Associated Vesicle Biogenesis.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1914852. Necap1.

Subcellular locationi

GO - Cellular componenti

  • clathrin vesicle coat Source: UniProtKB
  • coated pit Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi270 – 2701S → D: Loss of binding to AP-2 and can bind to AP-1; when associated with G-273.
Mutagenesisi272 – 2721W → A, F or Y: Loss of binding to AP-2. 1 Publication
Mutagenesisi273 – 2731V → A, D, E or I: No effect on binding to AP-2. 1 Publication
Mutagenesisi273 – 2731V → G: Loss of binding to AP-2 and can bind to AP-1; when associated with D-270. 1 Publication
Mutagenesisi273 – 2731V → L, N, P or S: Loss of binding to AP-2. 1 Publication
Mutagenesisi274 – 2741Q → A, M, N, S or T: No effect on binding to AP-2. 1 Publication
Mutagenesisi275 – 2751F → A, F or Y: Loss of binding to AP-2. 1 Publication
Mutagenesisi275 – 2751F → W: No effect on binding to AP-2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 275275Adaptin ear-binding coat-associated protein 1PRO_0000213068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9CR95.
MaxQBiQ9CR95.
PaxDbiQ9CR95.
PRIDEiQ9CR95.

PTM databases

iPTMnetiQ9CR95.
PhosphoSiteiQ9CR95.

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

BgeeiQ9CR95.
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

WithEntry#Exp.IntActNotes
AMPHP494186EBI-7592476,EBI-7121510From a different organism.
AmphO088387EBI-7592476,EBI-80080From a different organism.
Bin1O088398EBI-7592476,EBI-80095From a different organism.
Dab2P980782EBI-7592476,EBI-1391846
HIP1O002913EBI-7592476,EBI-473886From a different organism.
SNAP91O606412EBI-7592476,EBI-1105187From a different organism.

Protein-protein interaction databases

DIPiDIP-44062N.
IntActiQ9CR95. 12 interactions.
MINTiMINT-4125077.
STRINGi10090.ENSMUSP00000032477.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 217Combined sources
Beta strandi27 – 304Combined sources
Helixi33 – 364Combined sources
Beta strandi39 – 413Combined sources
Beta strandi43 – 508Combined sources
Beta strandi53 – 619Combined sources
Beta strandi70 – 745Combined sources
Beta strandi82 – 843Combined sources
Beta strandi92 – 987Combined sources
Turni99 – 1013Combined sources
Beta strandi102 – 1098Combined sources
Helixi113 – 12715Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9CR95.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi252 – 2554WXXF motif 1
Motifi272 – 2754WXXF motif 2

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.
OMAiESQEMDN.
OrthoDBiEOG76X61J.
PhylomeDBiQ9CR95.
TreeFamiTF314482.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012466. NECAP-1_N.
IPR011993. PH_dom-like.
[Graphical view]
PfamiPF07933. DUF1681. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 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.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-44062N.
IntActiQ9CR95. 12 interactions.
MINTiMINT-4125077.
STRINGi10090.ENSMUSP00000032477.

PTM databases

iPTMnetiQ9CR95.
PhosphoSiteiQ9CR95.

Proteomic databases

EPDiQ9CR95.
MaxQBiQ9CR95.
PaxDbiQ9CR95.
PRIDEiQ9CR95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi25977.
MGIiMGI:1914852. Necap1.

Phylogenomic databases

eggNOGiKOG2500. Eukaryota.
ENOG41113PS. LUCA.
GeneTreeiENSGT00390000009359.
HOVERGENiHBG060621.
InParanoidiQ9CR95.
KOiK20069.
OMAiESQEMDN.
OrthoDBiEOG76X61J.
PhylomeDBiQ9CR95.
TreeFamiTF314482.

Enzyme and pathway databases

ReactomeiR-MMU-432722. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiNecap1. mouse.
EvolutionaryTraceiQ9CR95.
PROiQ9CR95.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CR95.
CleanExiMM_NECAP1.
ExpressionAtlasiQ9CR95. baseline and differential.
GenevisibleiQ9CR95. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012466. NECAP-1_N.
IPR011993. PH_dom-like.
[Graphical view]
PfamiPF07933. DUF1681. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryonic head, Embryonic heart and Lung.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  3. "Identification of a family of endocytic proteins that define a new alpha-adaptin ear-binding motif."
    Ritter B., Philie J., Girard M., Tung E.C., Blondeau F., McPherson P.S.
    EMBO Rep. 4:1089-1095(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, INTERACTION WITH AP1G1 AND AP2A1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
  4. "Two WXXF-based motifs in NECAPs define the specificity of accessory protein binding to AP-1 and AP-2."
    Ritter B., Denisov A.Y., Philie J., Deprez C., Tung E.C., Gehring K., McPherson P.S.
    EMBO J. 23:3701-3710(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TRP-272; VAL-273; GLN-274 AND PHE-275, INTERACTION WITH AP2A1; AP2A2 AND AP1G1.
  5. "Definition of the consensus motif recognized by gamma-adaptin ear domains."
    Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.
    J. Biol. Chem. 279:8018-8028(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GGA1; GGA2; GGA3 AND AP1G1.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas and Testis.
  7. "NECAP1 loss of function leads to a severe infantile epileptic encephalopathy."
    Alazami A.M., Hijazi H., Kentab A.Y., Alkuraya F.S.
    J. Med. Genet. 51:224-228(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "Solution structure of NECAP1 protein."
    Denisov A.Y., Ritter B., McPherson P.S., Gehring K.
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-133.

Entry informationi

Entry nameiNECP1_MOUSE
AccessioniPrimary (citable) accession number: Q9CR95
Secondary accession number(s): Q3TH13, Q78JW3, Q8C4P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.