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Protein

AP-1 complex subunit sigma-2

Gene

AP1S2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_121399. MHC class II antigen presentation.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1 complex subunit sigma-2
Alternative name(s):
Adaptor protein complex AP-1 subunit sigma-1B
Adaptor-related protein complex 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 namesi
Name:AP1S2
ORF Names:DC22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:560. AP1S2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Pettigrew syndrome (PGS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndrome characterized by mental retardation and additional highly variable features, including choreoathetosis, hydrocephalus, Dandy-Walker malformation, seizures, and iron or calcium deposition in the brain. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.

See also OMIM:304340

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi304340. phenotype.
Orphaneti85335. Fried syndrome.
1568. X-linked intellectual disability - Dandy-Walker malformation - basal ganglia disease - Seizures.
PharmGKBiPA24851.

Polymorphism and mutation databases

DMDMi3023308.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157AP-1 complex subunit sigma-2PRO_0000193799Add
BLAST

Proteomic databases

MaxQBiP56377.
PaxDbiP56377.
PRIDEiP56377.

PTM databases

PhosphoSiteiP56377.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiP56377.
CleanExiHS_AP1S2.
ExpressionAtlasiP56377. baseline and differential.
GenevisibleiP56377. HS.

Organism-specific databases

HPAiHPA049894.
HPA060945.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
AP1G1O43747-23EBI-1054374,EBI-10185819

Protein-protein interaction databases

BioGridi114419. 10 interactions.
IntActiP56377. 2 interactions.
MINTiMINT-3021368.
STRINGi9606.ENSP00000328789.

Structurei

3D structure databases

ProteinModelPortaliP56377.
SMRiP56377. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5030.
GeneTreeiENSGT00530000062839.
HOGENOMiHOG000185227.
HOVERGENiHBG050517.
InParanoidiP56377.
OrthoDBiEOG7S7SGC.
PhylomeDBiP56377.
TreeFamiTF312921.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P56377-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQFMLLFSRQ GKLRLQKWYV PLSDKEKKKI TRELVQTVLA RKPKMCSFLE
60 70 80 90 100
WRDLKIVYKR YASLYFCCAI EDQDNELITL EIIHRYVELL DKYFGSVCEL
110 120 130 140 150
DIIFNFEKAY FILDEFLLGG EVQETSKKNV LKAIEQADLL QEEAETPRSV

LEEIGLT
Length:157
Mass (Da):18,615
Last modified:July 15, 1998 - v1
Checksum:iDD9F59119909D89C
GO
Isoform 2 (identifier: P56377-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:202
Mass (Da):23,225
Checksum:i69C7E1AE4CB98F02
GO

Sequence cautioni

The sequence AAG44595.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → L in AAG44595 (Ref. 2) Curated
Sequence conflicti72 – 743DQD → ESRN in AAC72946 (Ref. 7) Curated
Sequence conflicti96 – 983SVC → QCL in AAC72946 (Ref. 7) Curated
Sequence conflicti143 – 1431E → EE in AAG44595 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPAGCPPHSTTASLPQHGDR GFPFAAAAAAGQAPPRPRPA AAM in isoform 2. 1 PublicationVSP_053671
Alternative sequencei143 – 15715EAETP…EIGLT → KTETMYHSKSFIGFKKAY in isoform 2. 1 PublicationVSP_053672Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14173.1. [P56377-1]
RefSeqiNP_003907.3. NM_003916.4. [P56377-1]
XP_011543901.1. XM_011545599.1. [P56377-2]
UniGeneiHs.121592.

Genome annotation databases

EnsembliENST00000329235; ENSP00000328789; ENSG00000182287.
GeneIDi8905.
UCSCiuc004cxi.4. human. [P56377-1]
uc011mit.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14173.1. [P56377-1]
RefSeqiNP_003907.3. NM_003916.4. [P56377-1]
XP_011543901.1. XM_011545599.1. [P56377-2]
UniGeneiHs.121592.

3D structure databases

ProteinModelPortaliP56377.
SMRiP56377. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114419. 10 interactions.
IntActiP56377. 2 interactions.
MINTiMINT-3021368.
STRINGi9606.ENSP00000328789.

PTM databases

PhosphoSiteiP56377.

Polymorphism and mutation databases

DMDMi3023308.

Proteomic databases

MaxQBiP56377.
PaxDbiP56377.
PRIDEiP56377.

Protocols and materials databases

DNASUi8905.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329235; ENSP00000328789; ENSG00000182287.
GeneIDi8905.
UCSCiuc004cxi.4. human. [P56377-1]
uc011mit.3. human.

Organism-specific databases

CTDi8905.
GeneCardsiGC0XM015843.
HGNCiHGNC:560. AP1S2.
HPAiHPA049894.
HPA060945.
MIMi300629. gene.
304340. phenotype.
neXtProtiNX_P56377.
Orphaneti85335. Fried syndrome.
1568. X-linked intellectual disability - Dandy-Walker malformation - basal ganglia disease - Seizures.
PharmGKBiPA24851.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5030.
GeneTreeiENSGT00530000062839.
HOGENOMiHOG000185227.
HOVERGENiHBG050517.
InParanoidiP56377.
OrthoDBiEOG7S7SGC.
PhylomeDBiP56377.
TreeFamiTF312921.

Enzyme and pathway databases

ReactomeiREACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_121399. MHC class II antigen presentation.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiAP1S2. human.
GeneWikiiAP1S2.
GenomeRNAii8905.
NextBioi33457.
PROiP56377.
SOURCEiSearch...

Gene expression databases

BgeeiP56377.
CleanExiHS_AP1S2.
ExpressionAtlasiP56377. baseline and differential.
GenevisibleiP56377. HS.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: INVOLVEMENT IN PGS.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAP1S2_HUMAN
AccessioniPrimary (citable) accession number: P56377
Secondary accession number(s): B4DSU4, O95326, Q9H2N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: July 22, 2015
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.