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Protein
Submitted name:

AP-2 complex subunit mu

Gene

AP2M1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei366 – 3661Phosphatidylinositol lipid headgroupUniRule annotation
Binding sitei368 – 3681Phosphatidylinositol lipid headgroupUniRule annotation
Binding sitei370 – 3701Phosphatidylinositol lipid headgroupUniRule annotation
Binding sitei379 – 3791Phosphatidylinositol lipid headgroupUniRule annotation
Binding sitei381 – 3811Phosphatidylinositol lipid headgroupUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transportSAAS annotation, Transport

Keywords - Ligandi

Lipid-bindingUniRule annotation

Enzyme and pathway databases

SignaLinkiE9PFW3.

Names & Taxonomyi

Protein namesi
Submitted name:
AP-2 complex subunit muImported
Gene namesi
Name:AP2M1Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:564. AP2M1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

EPDiE9PFW3.
PRIDEiE9PFW3.

Expressioni

Gene expression databases

BgeeiE9PFW3.
ExpressionAtlasiE9PFW3. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliE9PFW3.
SMRiE9PFW3. Positions 1-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 459265MHD (mu homology)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adaptor complexes medium subunit family.SAAS annotation
Contains MHD (mu homology) domain.SAAS annotation

Phylogenomic databases

GeneTreeiENSGT00530000062779.
OMAiVWKIPRI.
PhylomeDBiE9PFW3.

Family and domain databases

InterProiIPR001392. Clathrin_mu.
IPR018240. Clathrin_mu_CS.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PfamiPF00928. Adap_comp_sub. 1 hit.
[Graphical view]
PIRSFiPIRSF005992. Clathrin_mu. 1 hit.
PRINTSiPR00314. CLATHRINADPT.
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS00990. CLAT_ADAPTOR_M_1. 1 hit.
PS00991. CLAT_ADAPTOR_M_2. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9PFW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGGLFIYNH KGEVLISRVY RDDIGSRQAA DSAVFSSSGP FPGEWLEANR
60 70 80 90 100
RNAVDAFRVN VIHARQQVRS PVTNIARTSF FHVKRSNIWL AAVTKQNVNA
110 120 130 140 150
AMVFEFLYKM CDVMAAYFGK ISEENIKNNF VLIYELLDEI LDFGYPQNSE
160 170 180 190 200
TGALKTFITQ QGIKSQHQTK EEQSQITSQV TGQIGWRREG IKYRRNELFL
210 220 230 240 250
DVLESVNLLM SPQGQVLSAH VSGRVVMKSY LSGMPECKFG MNDKIVIEKQ
260 270 280 290 300
GKGTADETSK SGKQSIAIDD CTFHQCVRLS KFDSERSISF IPPDGEFELM
310 320 330 340 350
RYRTTKDIIL PFRVIPLVRE VGRTKLEVKV VIKSNFKPSL LAQKIEVRIP
360 370 380 390 400
TPLNTSGVQV ICMKGKAKYK ASENAIVWKI KRMAGMKESQ ISAEIELLPT
410 420 430 440 450
NDKKKWARPP ISMNFEVPFA PSGLKVRYLK VFEPKLNYSD HDVIKWVRYI
460
GRSGIYETRC
Length:460
Mass (Da):52,304
Last modified:April 5, 2011 - v1
Checksum:iB693E3B0195DAC5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC131235 Genomic DNA. No translation available.
RefSeqiNP_001298127.1. NM_001311198.1.
UniGeneiHs.518460.

Genome annotation databases

EnsembliENST00000411763; ENSP00000403362; ENSG00000161203.
GeneIDi1173.
UCSCiuc062qrq.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC131235 Genomic DNA. No translation available.
RefSeqiNP_001298127.1. NM_001311198.1.
UniGeneiHs.518460.

3D structure databases

ProteinModelPortaliE9PFW3.
SMRiE9PFW3. Positions 1-460.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

EPDiE9PFW3.
PRIDEiE9PFW3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000411763; ENSP00000403362; ENSG00000161203.
GeneIDi1173.
UCSCiuc062qrq.1. human.

Organism-specific databases

CTDi1173.
HGNCiHGNC:564. AP2M1.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000062779.
OMAiVWKIPRI.
PhylomeDBiE9PFW3.

Enzyme and pathway databases

SignaLinkiE9PFW3.

Miscellaneous databases

ChiTaRSiAP2M1. human.
GenomeRNAii1173.

Gene expression databases

BgeeiE9PFW3.
ExpressionAtlasiE9PFW3. baseline and differential.

Family and domain databases

InterProiIPR001392. Clathrin_mu.
IPR018240. Clathrin_mu_CS.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PfamiPF00928. Adap_comp_sub. 1 hit.
[Graphical view]
PIRSFiPIRSF005992. Clathrin_mu. 1 hit.
PRINTSiPR00314. CLATHRINADPT.
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS00990. CLAT_ADAPTOR_M_1. 1 hit.
PS00991. CLAT_ADAPTOR_M_2. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  5. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "N-terminome analysis of the human mitochondrial proteome."
    Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.
    Proteomics 15:2519-2524(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiE9PFW3_HUMAN
AccessioniPrimary (citable) accession number: E9PFW3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: June 8, 2016
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.