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P56377 (AP1S2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-1 complex subunit sigma-2
Alternative name(s):
Adapter-related protein complex 1 subunit sigma-1B
Adaptor protein complex AP-1 subunit sigma-1B
Clathrin assembly protein complex 1 sigma-1B small chain
Golgi adaptor HA1/AP1 adaptin sigma-1B subunit
Sigma 1B subunit of AP-1 clathrin
Sigma-adaptin 1B
Sigma1B-adaptin
Gene names
Name:AP1S2
ORF Names:DC22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length157 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). Binds to MUC1. Ref.8

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

Widely expressed.

Involvement in disease

Mental retardation, X-linked 59 (MRX59) [MIM:300630]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX59 consists of a mild-to-profound mental retardation. Other features includes hypotonia early in life and delay in walking.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the adaptor complexes small subunit family.

Sequence caution

The sequence AAG44595.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P56377-1)

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: P56377-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPAGCPPHSTTASLPQHGDRGFPFAAAAAAGQAPPRPRPAAAM
     143-157: EAETPRSVLEEIGLT → KTETMYHSKSFIGFKKAY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157AP-1 complex subunit sigma-2
PRO_0000193799

Natural variations

Alternative sequence11M → MPAGCPPHSTTASLPQHGDR GFPFAAAAAAGQAPPRPRPA AAM in isoform 2.
VSP_053671
Alternative sequence143 – 15715EAETP…EIGLT → KTETMYHSKSFIGFKKAY in isoform 2.
VSP_053672

Experimental info

Sequence conflict11M → L in AAG44595. Ref.2
Sequence conflict72 – 743DQD → ESRN in AAC72946. Ref.7
Sequence conflict96 – 983SVC → QCL in AAC72946. Ref.7
Sequence conflict1431E → EE in AAG44595. Ref.2

Sequences

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

Last modified July 15, 1998. Version 1.
Checksum: DD9F59119909D89C

FASTA15718,615
        10         20         30         40         50         60 
MQFMLLFSRQ GKLRLQKWYV PLSDKEKKKI TRELVQTVLA RKPKMCSFLE WRDLKIVYKR 

        70         80         90        100        110        120 
YASLYFCCAI EDQDNELITL EIIHRYVELL DKYFGSVCEL DIIFNFEKAY FILDEFLLGG 

       130        140        150 
EVQETSKKNV LKAIEQADLL QEEAETPRSV LEEIGLT 

« Hide

Isoform 2 [UniParc].

Checksum: 69C7E1AE4CB98F02
Show »

FASTA20223,225

References

« Hide 'large scale' references
[1]"Identification and characterization of novel clathrin adaptor-related proteins."
Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.
J. Biol. Chem. 273:24693-24700(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Novel genes expressed in human dendritic cell."
Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Dendritic cell.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"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 2).
Tissue: Brain.
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 1).
Tissue: Skin and Uterus.
[7]"Full-insert sequence of mapped XREF EST."
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-98 (ISOFORM 1).
[8]"MUC1 membrane trafficking is modulated by multiple interactions."
Kinlough C.L., Poland P.A., Bruns J.B., Harkleroad K.L., Hughey R.P.
J. Biol. Chem. 279:53071-53077(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUC1.
[9]"Mutations in the gene encoding the sigma 2 subunit of the adaptor protein 1 complex, AP1S2, cause X-linked mental retardation."
Tarpey P.S., Stevens C., Teague J., Edkins S., O'Meara S., Avis T., Barthorpe S., Buck G., Butler A., Cole J., Dicks E., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Menzies A. expand/collapse author list , Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., West S., Widaa S., Yates A., Catford R., Butler J., Mallya U., Moon J., Luo Y., Dorkins H., Thompson D., Easton D.F., Wooster R., Bobrow M., Carpenter N., Simensen R.J., Schwartz C.E., Stevenson R.E., Turner G., Partington M., Gecz J., Stratton M.R., Futreal P.A., Raymond F.L.
Am. J. Hum. Genet. 79:1119-1124(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRX59.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015320 mRNA. Translation: BAA33392.1.
AF251295 mRNA. Translation: AAG44595.1. Different initiation.
BT006738 mRNA. Translation: AAP35384.1.
AK299921 mRNA. Translation: BAG61756.1.
AC004106 Genomic DNA. No translation available.
BC001117 mRNA. Translation: AAH01117.1.
BC071867 mRNA. Translation: AAH71867.1.
AF091077 mRNA. Translation: AAC72946.1.
CCDSCCDS14173.1.
RefSeqNP_003907.3. NM_003916.4. [P56377-1]
XP_005274669.1. XM_005274612.2. [P56377-2]
UniGeneHs.121592.

3D structure databases

ProteinModelPortalP56377.
SMRP56377. Positions 1-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114419. 6 interactions.
MINTMINT-3021368.
STRING9606.ENSP00000328789.

PTM databases

PhosphoSiteP56377.

Polymorphism databases

DMDM3023308.

Proteomic databases

MaxQBP56377.
PaxDbP56377.
PRIDEP56377.

Protocols and materials databases

DNASU8905.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329235; ENSP00000328789; ENSG00000182287. [P56377-1]
ENST00000421527; ENSP00000414714; ENSG00000182287. [P56377-2]
GeneID8905.
KEGGhsa:8905.
UCSCuc004cxi.4. human. [P56377-1]

Organism-specific databases

CTD8905.
GeneCardsGC0XM015843.
HGNCHGNC:560. AP1S2.
HPAHPA049894.
MIM300629. gene.
300630. phenotype.
neXtProtNX_P56377.
Orphanet85335. Fried syndrome.
1568. intellectual disability, X-linked - Dandy-Walker malformation - basal ganglia disease - Seizures.
PharmGKBPA24851.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5030.
HOGENOMHOG000185227.
HOVERGENHBG050517.
KOK12394.
OMADMKVVYK.
OrthoDBEOG7S7SGC.
PhylomeDBP56377.
TreeFamTF312921.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP56377.
BgeeP56377.
CleanExHS_AP1S2.
GenevestigatorP56377.

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

GeneWikiAP1S2.
GenomeRNAi8905.
NextBio33457.
PROP56377.
SOURCESearch...

Entry information

Entry nameAP1S2_HUMAN
AccessionPrimary (citable) accession number: P56377
Secondary accession number(s): B4DSU4, O95326, Q9H2N6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 139 of the entry and version 1 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 X

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