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P61967 (AP1S1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-1 complex subunit sigma-1A
Alternative name(s):
Adapter-related protein complex 1 subunit sigma-1A
Adaptor protein complex AP-1 subunit sigma-1A
Clathrin assembly protein complex 1 sigma-1A small chain
Clathrin coat assembly protein AP19
Golgi adaptor HA1/AP1 adaptin sigma-1A subunit
HA1 19 kDa subunit
Sigma 1a subunit of AP-1 clathrin
Sigma-adaptin 1A
Sigma1A-adaptin
Gene names
Name:Ap1s1
Synonyms:Ap19
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.

Subunit structure

Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3).

Subcellular location

Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membraneclathrin-coated pit. Note: Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.

Tissue specificity

Detected in brain and embryonic stem cells.

Sequence similarities

Belongs to the adaptor complexes small subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158AP-1 complex subunit sigma-1A
PRO_0000193798

Amino acid modifications

Modified residue1471Phosphoserine By similarity

Secondary structure

........................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61967 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: E461937790406D8B

FASTA15818,733
        10         20         30         40         50         60 
MMRFMLLFSR QGKLRLQKWY LATSDKERKK MVRELMQVVL ARKPKMCSFL EWRDLKVVYK 

        70         80         90        100        110        120 
RYASLYFCCA IEGQDNELIT LELIHRYVEL LDKYFGSVCE LDIIFNFEKA YFILDEFLMG 

       130        140        150 
GDVQDTSKKS VLKAIEQADL LQEEDESPRS VLEEMGLA 

« Hide

References

« Hide 'large scale' references
[1]"AP17 and AP19, the mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their putative homolog in yeast."
Kirchhausen T., Davis A.C., Frucht S., O'Brine Greco B., Payne G.S., Tubb B.
J. Biol. Chem. 266:11153-11157(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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. expand/collapse author list , 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: Embryonic stem cell.
[3]"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: C57BL/6.
[4]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62418 mRNA. Translation: AAA37243.1.
AK002225 mRNA. Translation: BAB21947.1.
BC052692 mRNA. Translation: AAH52692.1.
CCDSCCDS39330.1.
PIRA40535.
RefSeqNP_031483.1. NM_007457.2.
UniGeneMm.833.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W63X-ray4.00Q/S/T/U/W/X1-158[»]
ProteinModelPortalP61967.
SMRP61967. Positions 1-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP61967. 3 interactions.
MINTMINT-1870317.

PTM databases

PhosphoSiteP61967.

Proteomic databases

MaxQBP61967.
PaxDbP61967.
PRIDEP61967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111080; ENSMUSP00000106709; ENSMUSG00000004849.
GeneID11769.
KEGGmmu:11769.
UCSCuc009abm.1. mouse.

Organism-specific databases

CTD1174.
MGIMGI:1098244. Ap1s1.

Phylogenomic databases

eggNOGCOG5030.
GeneTreeENSGT00530000062839.
HOGENOMHOG000185227.
HOVERGENHBG050517.
InParanoidP61967.
KOK12394.
OMAIGSGDNE.
OrthoDBEOG7S7SGC.
PhylomeDBP61967.
TreeFamTF312921.

Gene expression databases

ArrayExpressP61967.
BgeeP61967.
CleanExMM_AP1S1.
GenevestigatorP61967.

Family and domain databases

InterProIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERPTHR11753. PTHR11753. 1 hit.
PfamPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMSSF64356. SSF64356. 1 hit.
PROSITEPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61967.
NextBio279541.
PROP61967.
SOURCESearch...

Entry information

Entry nameAP1S1_MOUSE
AccessionPrimary (citable) accession number: P61967
Secondary accession number(s): P82267 expand/collapse secondary AC list , Q00382, Q9BTN4, Q9UDW9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot