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Protein

AP-1 complex subunit beta-1

Gene

Ap1b1

Organism
Mus musculus (Mouse)
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

  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein transporter activity Source: InterPro

GO - Biological processi

  • intracellular protein transport Source: MGI
  • vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_303468. Lysosome Vesicle Biogenesis.
REACT_316383. MHC class II antigen presentation.
REACT_342454. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1 complex subunit beta-1
Alternative name(s):
Adaptor protein complex AP-1 subunit beta-1
Adaptor-related protein complex 1 subunit beta-1
Beta-1-adaptin
Beta-adaptin 1
Clathrin assembly protein complex 1 beta large chain
Golgi adaptor HA1/AP1 adaptin beta subunit
Gene namesi
Name:Ap1b1
Synonyms:Adtb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1096368. Ap1b1.

Subcellular locationi

GO - Cellular componenti

  • clathrin adaptor complex Source: InterPro
  • clathrin-coated vesicle membrane Source: UniProtKB-SubCell
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 943942AP-1 complex subunit beta-1PRO_0000193739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei265 – 2651N6-acetyllysineBy similarity
Modified residuei318 – 3181N6-acetyllysineBy similarity
Modified residuei574 – 5741Nitrated tyrosine1 Publication

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiO35643.
PaxDbiO35643.
PRIDEiO35643.

PTM databases

PhosphoSiteiO35643.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiO35643.
CleanExiMM_AP1B1.
ExpressionAtlasiO35643. baseline and differential.
GenevisibleiO35643. MM.

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).

Protein-protein interaction databases

BioGridi198122. 6 interactions.
IntActiO35643. 6 interactions.
MINTiMINT-1870179.
STRINGi10090.ENSMUSP00000009234.

Structurei

3D structure databases

ProteinModelPortaliO35643.
SMRiO35643. Positions 14-583, 711-943.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi576 – 722147Pro-rich (stalk region)Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiO35643.
OMAiQIFYDIS.
TreeFamiTF300318.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1150. 1 hit.
3.30.310.10. 1 hit.
InterProiIPR026739. AP_beta.
IPR016342. AP_complex_bsu_1_2_4.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015151. B-adaptin_app_sub_C.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR013037. Clathrin_b-adaptin_app_Ig-like.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PANTHERiPTHR11134. PTHR11134. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
PF09066. B2-adapt-app_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002291. AP_complex_beta. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDSKYFTTT KKGEIFELKA ELNSDKKEKK KEAVKKVIAS MTVGKDVSAL
60 70 80 90 100
FPDVVNCMQT DNLELKKLVY LYLMNYAKSQ PDMAIMAVNT FVKDCEDPNP
110 120 130 140 150
LIRALAVRTM GCIRVDKITE YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD
160 170 180 190 200
INAQLVEDQG FLDTLKDLIS DSNPMVVANA VAALSEIAES HPSSNLLDLN
210 220 230 240 250
PQSINKLLTA LNECTEWGQI FILDCLANYM PKDDREAQSI CERVTPRLSH
260 270 280 290 300
ANSAVVLSAV KVLMKFMEML SKDLDYYATL LKKLAPPLVT LLSAEPELQY
310 320 330 340 350
VALRNINLIV QKRPEILKHE MKVFFVKYND PIYVKLEKLD IMIRLASQAN
360 370 380 390 400
IAQVLAELKE YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ
410 420 430 440 450
TKVNYVVQEA IVVIKDIFRK YPNKYESVIA TLCENLDSLD EPEARAAMIW
460 470 480 490 500
IVGEYAERID NADELLESFL EGFHDESTQV QLQLLTAIVK LFLKKPTETQ
510 520 530 540 550
ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVAAKEV VLAEKPLISE
560 570 580 590 600
ETDLIEPTLL DELICYIGTL ASVYHKPPNA FVEGGRGVVH KSLPPRTASS
610 620 630 640 650
ESTESPETAP AGAPAGDQPD VIPAQGDLLG DLLNLDLGPP VSGPPLAASS
660 670 680 690 700
VQMGAVDLLG GGLDSLIGDS NFGAPSASVA AAPAPARLGA PISSGLSDLF
710 720 730 740 750
DLTSGVGTLS GSYVAPKAVW LPAMKAKGLE ISGTFTRQAG SISMDLQLTN
760 770 780 790 800
KALQVMTDFA IQFNRNSFGL APAAPLQVHV PLSPNQTVEI SLPLNTVGSV
810 820 830 840 850
LKMEPLNNLQ VAVKNNIDVF YFSTLYPLHV LFVEDGKMDR QMFLATWKDI
860 870 880 890 900
ANENEAQFQI RDCPLNTEAA SNKLQSSNIF TVAKRNVEGQ DMLYQSLKLT
910 920 930 940
NGIWVLAELR IQPGNPSFTL SLKCRAPEVS QHVYQAYETI LKN
Length:943
Mass (Da):103,935
Last modified:July 27, 2011 - v2
Checksum:i5DD1951EAAC20225
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti227 – 2271A → D in CAA69224 (PubMed:9271666).Curated
Sequence conflicti288 – 2881L → P in AAH08513 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07919 mRNA. Translation: CAA69224.1.
AK159273 mRNA. Translation: BAE34952.1.
CH466574 Genomic DNA. Translation: EDL40509.1.
BC008513 mRNA. Translation: AAH08513.1.
CCDSiCCDS36100.1.
RefSeqiNP_031480.2. NM_007454.3.
UniGeneiMm.274816.

Genome annotation databases

EnsembliENSMUST00000009234; ENSMUSP00000009234; ENSMUSG00000009090.
GeneIDi11764.
UCSCiuc007hvo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07919 mRNA. Translation: CAA69224.1.
AK159273 mRNA. Translation: BAE34952.1.
CH466574 Genomic DNA. Translation: EDL40509.1.
BC008513 mRNA. Translation: AAH08513.1.
CCDSiCCDS36100.1.
RefSeqiNP_031480.2. NM_007454.3.
UniGeneiMm.274816.

3D structure databases

ProteinModelPortaliO35643.
SMRiO35643. Positions 14-583, 711-943.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198122. 6 interactions.
IntActiO35643. 6 interactions.
MINTiMINT-1870179.
STRINGi10090.ENSMUSP00000009234.

PTM databases

PhosphoSiteiO35643.

Proteomic databases

MaxQBiO35643.
PaxDbiO35643.
PRIDEiO35643.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000009234; ENSMUSP00000009234; ENSMUSG00000009090.
GeneIDi11764.
UCSCiuc007hvo.2. mouse.

Organism-specific databases

CTDi162.
MGIiMGI:1096368. Ap1b1.

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiO35643.
OMAiQIFYDIS.
TreeFamiTF300318.

Enzyme and pathway databases

ReactomeiREACT_303468. Lysosome Vesicle Biogenesis.
REACT_316383. MHC class II antigen presentation.
REACT_342454. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiAp1b1. mouse.
NextBioi279521.
PROiO35643.
SOURCEiSearch...

Gene expression databases

BgeeiO35643.
CleanExiMM_AP1B1.
ExpressionAtlasiO35643. baseline and differential.
GenevisibleiO35643. MM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1150. 1 hit.
3.30.310.10. 1 hit.
InterProiIPR026739. AP_beta.
IPR016342. AP_complex_bsu_1_2_4.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015151. B-adaptin_app_sub_C.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR013037. Clathrin_b-adaptin_app_Ig-like.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PANTHERiPTHR11134. PTHR11134. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
PF09066. B2-adapt-app_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002291. AP_complex_beta. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the mouse beta-prime adaptin gene; cDNA sequence, genomic structure, and chromosomal localization."
    Guilbaud C., Peyrard M., Fransson I., Clifton S.W., Roe B.A., Carter N.P., Dumanski J.P.
    Mamm. Genome 8:651-656(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Embryonic 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.
    , 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.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Mammary gland.
  5. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiAP1B1_MOUSE
AccessioniPrimary (citable) accession number: O35643
Secondary accession number(s): Q3TXG4, Q922E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.