O60641 (AP180_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	907 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Membrane › coated 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	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.

Ontologies

Keywords
Cellular component	Cell membrane Coated pit Membrane
Coding sequence diversity	Alternative splicing
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	clathrin coat assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	clathrin coat Inferred from electronic annotation. Source: InterPro coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 907	907	Clathrin coat assembly protein AP180		PRO_0000193864
Regions
	Domain	14 – 145	132	ENTH
	Compositional bias	361 – 583	223	Ala-rich
	Compositional bias	536 – 556	21	Thr-rich
	Compositional bias	809 – 897	89	Pro-rich
Amino acid modifications
	Modified residue	306	1	Phosphoserine By similarity
	Modified residue	312	1	Phosphothreonine By similarity
	Modified residue	313	1	Phosphoserine By similarity
	Modified residue	316	1	Phosphoserine By similarity
	Modified residue	602	1	Phosphoserine By similarity
	Modified residue	623	1	Phosphoserine By similarity
	Modified residue	629	1	Phosphoserine By similarity
	Glycosylation	310	1	O-linked (GlcNAc) By similarity
Natural variations
	Alternative sequence	59 – 907	849	Missing in isoform 2.		VSP_020997
	Alternative sequence	256 – 269	14	Missing in isoform 3.		VSP_020998
	Alternative sequence	293 – 295	3	NEG → K in isoform 3.		VSP_020999
	Alternative sequence	381 – 671	291	Missing in isoform 3.		VSP_021000
Experimental info
	Sequence conflict	4	1	Q → R in AAH60818. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1999. Version 2. Checksum: 23959C2B54F5EBF1	FASTA	907	92,502
	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
	Isoform 2 [UniParc]. Checksum: 22EBDA4093641147	FASTA	58	6,230
	10 20 30 40 50 MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQ
	Isoform 3 [UniParc]. Checksum: 0B92B5140631B77F	FASTA	600	63,128
	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 LKVAEAPSSL METLEQHLNT LEGKKPGNKS GAPSPLSKSS PATTVTSPNS 310 320 330 340 350 360 TPAKTIDTSP PVDLFATASA AVPVSTSKPS SDLLDLQPDF SSGGAAAAAA PAPPPPAGGA 370 380 390 400 410 420 TAWGGFGGSF MAPSPSPVTP AQNNLLQPNF EAAFGTTPST SSSSSFDPSV FDGLGDLLMP 430 440 450 460 470 480 TMAPAGQPAP VSMVPPSPAM AASKALGSDL DSSLASLVGN LGISGTTTKK GDLQWNAGEK 490 500 510 520 530 540 KLTGGANWQP KVAPATWSAG VPPSAPLQGA VPPTSSVPPV AGAPSVGQPG AGFGMPPAGT 550 560 570 580 590 600 GMPMMPQQPV MFAQPMMRPP FGAAAVPGTQ LSPSPTPASQ SPKKPPAKDP LADLNIKDFL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. AF054993 mRNA. Translation: AAC09352.1. BC060818 mRNA. Translation: AAH60818.1.
IPI	IPI00006612. IPI00646376. IPI00975977.
RefSeq	NP_001229721.1. NM_001242792.1. NP_001229722.1. NM_001242793.1. NP_001229723.1. NM_001242794.1. NP_001243646.1. NM_001256717.1. NP_001243647.1. NM_001256718.1. NP_055656.1. NM_014841.2.
UniGene	Hs.368046.
3D structure databases
ProteinModelPortal	O60641.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60641. 1 interaction.
MINT	MINT-3000172.
STRING	9606.ENSP00000195649.
PTM databases
PhosphoSite	O60641.
Proteomic databases
PaxDb	O60641.
PRIDE	O60641.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369694; ENSP00000358708; ENSG00000065609. ENST00000437520; ENSP00000413277; ENSG00000065609. ENST00000439399; ENSP00000400459; ENSG00000065609. ENST00000520213; ENSP00000428026; ENSG00000065609. ENST00000521743; ENSP00000428215; ENSG00000065609.
GeneID	9892.
KEGG	hsa:9892.
UCSC	uc003pka.3. human. uc003pkd.3. human.
Organism-specific databases
CTD	9892.
GeneCards	GC06M084319.
H-InvDB	HIX0006038.
HGNC	HGNC:14986. SNAP91.
HPA	CAB009745. HPA029632. HPA029633.
MIM	607923. gene.
neXtProt	NX_O60641.
PharmGKB	PA37956.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG267212.
HOGENOM	HOG000015763.
HOVERGEN	HBG049391.
InParanoid	O60641.
OMA	LMPTMAP.
Gene expression databases
ArrayExpress	O60641.
Bgee	O60641.
CleanEx	HS_SNAP91.
Genevestigator	O60641.
GermOnline	ENSG00000065609. Homo sapiens.
Family and domain databases
Gene3D	1.20.58.150. 1 hit. 1.25.40.90. 1 hit.
InterPro	IPR011417. ANTH_dom. IPR014712. Clathrin_Pinositid-bd_GAT-like. IPR008942. ENTH_VHS. IPR013809. Epsin-like_N. [Graphical view]
Pfam	PF07651. ANTH. 1 hit. [Graphical view]
SMART	SM00273. ENTH. 1 hit. [Graphical view]
SUPFAM	SSF48464. ENTH_VHS. 1 hit.
PROSITE	PS50942. ENTH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9892.
NextBio	37299.
SOURCE	Search...

Entry information

Entry name

AP180_HUMAN

Accession

Primary (citable) accession number: O60641
Secondary accession number(s): A8K0L7 , Q5JX13, Q68DL9, Q6P9D3, Q9NTY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	August 1, 1999
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.