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O60641 (AP180_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Clathrin coat assembly protein AP180
Alternative name(s):
91 kDa synaptosomal-associated protein
Clathrin coat-associated protein AP180
Phosphoprotein F1-20
Gene names
Name:SNAP91
Synonyms:KIAA0656
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length907 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats By similarity.

Subunit structure

Binds AP2A2. Interacts with AP2B1; clathrin competes with SNAP91 By similarity. Ref.7

Subcellular location

Cell membrane By similarity. Membranecoated pit; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane By similarity.

Domain

Possesses a three domain structure: the N-terminal 300 residues harbor a clathrin binding site, an acidic middle domain 450 residues, interrupted by an Ala-rich segment, and the C-terminal domain (166 residues).

Post-translational modification

Thr-310 can be modified by the addition of N-acetylglucosamine which can be further phosphorylated. There is no evidence for direct Thr-310 phosphorylation By similarity.

Sequence similarities

Belongs to the PICALM/SNAP91 family.

Contains 1 ENTH (epsin N-terminal homology) domain.

Sequence caution

The sequence BAA31631.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB89292.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH18201.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Necap1Q9CR952EBI-1105187,EBI-7592476From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60641-1)

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.
Isoform 2 (identifier: O60641-2)

The sequence of this isoform differs from the canonical sequence as follows:
     59-907: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: O60641-3)

The sequence of this isoform differs from the canonical sequence as follows:
     256-269: Missing.
     293-295: NEG → K
     381-671: Missing.
Isoform 4 (identifier: O60641-4)

The sequence of this isoform differs from the canonical sequence as follows:
     293-295: NEG → K
     616-643: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 907907Clathrin coat assembly protein AP180
PRO_0000193864

Regions

Domain14 – 145132ENTH
Compositional bias361 – 583223Ala-rich
Compositional bias536 – 55621Thr-rich
Compositional bias809 – 89789Pro-rich

Amino acid modifications

Modified residue3061Phosphoserine By similarity
Modified residue3131Phosphoserine By similarity
Modified residue6021Phosphoserine By similarity
Modified residue6231Phosphoserine By similarity
Modified residue6291Phosphoserine By similarity
Glycosylation3101O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence59 – 907849Missing in isoform 2.
VSP_020997
Alternative sequence256 – 26914Missing in isoform 3.
VSP_020998
Alternative sequence293 – 2953NEG → K in isoform 3 and isoform 4.
VSP_020999
Alternative sequence381 – 671291Missing in isoform 3.
VSP_021000
Alternative sequence616 – 64328Missing in isoform 4.
VSP_047049

Experimental info

Sequence conflict41Q → R in AAH60818. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1999. Version 2.
Checksum: 23959C2B54F5EBF1

FASTA90792,502
        10         20         30         40         50         60 
MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA 

        70         80         90        100        110        120 
DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM 

       130        140        150        160        170        180 
STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMA PEKLLKSMPI LQGQIDALLE 

       190        200        210        220        230        240 
FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF 

       250        260        270        280        290        300 
LTRMTRVSEF LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS 

       310        320        330        340        350        360 
PLSKSSPATT VTSPNSTPAK TIDTSPPVDL FATASAAVPV STSKPSSDLL DLQPDFSSGG 

       370        380        390        400        410        420 
AAAAAAPAPP PPAGGATAWG DLLGEDSLAA LSSVPSEAQI SDPFAPEPTP PTTTAEIATA 

       430        440        450        460        470        480 
SASASTTTTV TAVTAEVDLF GDAFAASPGE APAASEGAAA PATPTPVAAA LDACSGNDPF 

       490        500        510        520        530        540 
APSEGSAEAA PELDLFAMKP PETSVPVVTP TASTAPPVPA TAPSPAPAVA AAAAATTAAT 

       550        560        570        580        590        600 
AAATTTTTTS AATATTAPPA LDIFGDLFES TPEVAAAPKP DAAPSIDLFS TDAFSSPPQG 

       610        620        630        640        650        660 
ASPVPESSLT ADLLSVDAFA APSPATTASP AKVDSSGVID LFGDAFGSSA SEPQPASQAA 

       670        680        690        700        710        720 
SSSSASADLL AGFGGSFMAP SPSPVTPAQN NLLQPNFEAA FGTTPSTSSS SSFDPSVFDG 

       730        740        750        760        770        780 
LGDLLMPTMA PAGQPAPVSM VPPSPAMAAS KALGSDLDSS LASLVGNLGI SGTTTKKGDL 

       790        800        810        820        830        840 
QWNAGEKKLT GGANWQPKVA PATWSAGVPP SAPLQGAVPP TSSVPPVAGA PSVGQPGAGF 

       850        860        870        880        890        900 
GMPPAGTGMP MMPQQPVMFA QPMMRPPFGA AAVPGTQLSP SPTPASQSPK KPPAKDPLAD 


LNIKDFL 

« Hide

Isoform 2 [UniParc].

Checksum: 22EBDA4093641147
Show »

FASTA586,230
Isoform 3 [UniParc].

Checksum: 0B92B5140631B77F
Show »

FASTA60063,128
Isoform 4 [UniParc].

Checksum: A9A46C044BE55582
Show »

FASTA87789,656

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Cerebellum.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [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 3).
Tissue: Testis.
[6]Yu W., Gibbs R.A.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-907.
Tissue: Brain.
[7]"Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2B1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014556 mRNA. Translation: BAA31631.2. Different initiation.
AK289582 mRNA. Translation: BAF82271.1.
CR749348 mRNA. Translation: CAH18201.1. Sequence problems.
AL109915 Genomic DNA. Translation: CAB89292.1. Sequence problems.
AL109915 Genomic DNA. Translation: CAI19453.1.
AL136972 Genomic DNA. No translation available.
AF054993 mRNA. Translation: AAC09352.1.
BC060818 mRNA. Translation: AAH60818.1.
CCDSCCDS47455.1. [O60641-1]
CCDS56437.1. [O60641-3]
CCDS56438.1. [O60641-4]
RefSeqNP_001229721.1. NM_001242792.1. [O60641-1]
NP_001229722.1. NM_001242793.1. [O60641-4]
NP_001229723.1. NM_001242794.1. [O60641-3]
NP_001243646.1. NM_001256717.1.
NP_001243647.1. NM_001256718.1.
NP_055656.1. NM_014841.2. [O60641-1]
XP_005248827.1. XM_005248770.2. [O60641-1]
XP_006715678.1. XM_006715615.1. [O60641-1]
UniGeneHs.368046.

3D structure databases

ProteinModelPortalO60641.
SMRO60641. Positions 18-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115222. 5 interactions.
IntActO60641. 2 interactions.
MINTMINT-3000172.
STRING9606.ENSP00000195649.

PTM databases

PhosphoSiteO60641.

Proteomic databases

MaxQBO60641.
PaxDbO60641.
PRIDEO60641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369694; ENSP00000358708; ENSG00000065609. [O60641-1]
ENST00000437520; ENSP00000413277; ENSG00000065609. [O60641-3]
ENST00000439399; ENSP00000400459; ENSG00000065609. [O60641-1]
ENST00000520213; ENSP00000428026; ENSG00000065609. [O60641-3]
ENST00000520302; ENSP00000428511; ENSG00000065609. [O60641-4]
ENST00000521743; ENSP00000428215; ENSG00000065609. [O60641-1]
GeneID9892.
KEGGhsa:9892.
UCSCuc003pka.3. human. [O60641-1]
uc003pkd.3. human. [O60641-3]

Organism-specific databases

CTD9892.
GeneCardsGC06M084319.
H-InvDBHIX0006038.
HGNCHGNC:14986. SNAP91.
HPACAB009745.
HPA029632.
HPA029633.
MIM607923. gene.
neXtProtNX_O60641.
PharmGKBPA37956.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267212.
HOGENOMHOG000015763.
HOVERGENHBG049391.
InParanoidO60641.
OMAXRISGAP.
OrthoDBEOG76QFM8.
PhylomeDBO60641.
TreeFamTF314861.

Gene expression databases

ArrayExpressO60641.
BgeeO60641.
CleanExHS_SNAP91.
GenevestigatorO60641.

Family and domain databases

Gene3D1.20.58.150. 1 hit.
1.25.40.90. 1 hit.
InterProIPR011417. ANTH_dom.
IPR014712. Clathrin_Pinositid-bd_GAT-like.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
[Graphical view]
PfamPF07651. ANTH. 1 hit.
[Graphical view]
SMARTSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSNAP91.
GenomeRNAi9892.
NextBio37299.
PROO60641.
SOURCESearch...

Entry information

Entry nameAP180_HUMAN
AccessionPrimary (citable) accession number: O60641
Secondary accession number(s): A8K0L7 expand/collapse secondary AC list , E5RI02, Q5JX13, Q68DL9, Q6P9D3, Q9NTY7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: August 1, 1999
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM