Reviewed,
UniProtKB/Swiss-Prot Q9UMZ2 (SYNRG_HUMAN)
Last modified
November 24, 2009.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Synergin gamma Alternative name(s): AP1 subunit gamma-binding protein 1 Gamma-synergin | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1314 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May play a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN). May act by linking the adapter protein complex AP-1 to other proteins. |
| Subunit structure | Interacts with SCAMP1 via its EH-domain By similarity. Interacts with GGA1, GGA2 and GGA3. Interacts with the AP1G1 and AP1G2 subunits of the adapter protein complexes AP-1. |
| Subcellular location | Cytoplasm By similarity. Golgi apparatus › trans-Golgi network membrane; Peripheral membrane protein By similarity. Note: Associates with membranes via the adapter protein complex AP-1. Colocalizes with AP1G1 By similarity. |
| Domain | The DFXDF motifs mediate the interaction with gamma-appendage subunits AP1G1 and AP1G2. Ref.5 |
| Sequence similarities | Contains 1 EH domain. |
| Sequence caution | The sequence AK126988 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Endocytosis Protein transport Transport |
| Cellular component | Cytoplasm Golgi apparatus Membrane |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil Repeat |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | endocytosis Inferred from electronic annotation. Source: UniProtKB-KW intracellular protein transport Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | AP-1 adaptor complex Ref.1 Traceable author statement. Source: ProtInc extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion 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: Q9UMZ2-1) 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: Q9UMZ2-3) The sequence of this isoform differs from the canonical sequence as follows: 198-275: Missing. | ||||||
| Isoform 3 (identifier: Q9UMZ2-4) The sequence of this isoform differs from the canonical sequence as follows: 198-275: Missing. 1260-1271: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1314 | 1314 | Synergin gamma | PRO_0000072387 | |||||
Regions | |||||||||
| Domain | 295 – 388 | 94 | EH | ||||||
| Region | 518 – 786 | 269 | Interaction with A1P1G1 and A1P1G2 | ||||||
| Coiled coil | 115 – 155 | 41 | Potential | ||||||
| Motif | 457 – 461 | 5 | DFXDF motif 1 | ||||||
| Motif | 690 – 694 | 5 | DFXDF motif 2 | ||||||
| Motif | 775 – 779 | 5 | DFXDF motif 3 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 473 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 513 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 744 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 752 | 1 | Phosphoserine Ref.9 Ref.6 Ref.8 | ||||||
| Modified residue | 756 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 852 | 1 | Phosphoserine | ||||||
| Modified residue | 855 | 1 | Phosphoserine | ||||||
| Modified residue | 909 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 919 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 935 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 936 | 1 | Phosphoserine | ||||||
| Modified residue | 1075 | 1 | Phosphoserine Ref.9 Ref.7 | ||||||
Natural variations | |||||||||
| Alternative sequence | 198 – 275 | 78 | Missing in isoform 2 and isoform 3. | VSP_023015 | |||||
| Alternative sequence | 1260 – 1271 | 12 | Missing in isoform 3. | VSP_023016 | |||||
| Natural variant | 40 | 1 | A → G: dbSNP rs12944821. | VAR_051395 | |||||
| Natural variant | 222 | 1 | T → A: dbSNP rs12602536. | VAR_051396 | |||||
Experimental info | |||||||||
| Sequence conflict | 40 | 1 | Missing in AAI17314. Ref.2 | ||||||
| Sequence conflict | 213 | 1 | S → P in AK126988. Ref.3 | ||||||
| Sequence conflict | 349 | 1 | K → R in AK126988. Ref.3 | ||||||
| Sequence conflict | 1123 | 1 | E → K in AAD49732. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin." Page L.J., Sowerby P.J., Lui W.W.Y., Robinson M.S. J. Cell Biol. 146:993-1004(1999) [PubMed: 10477754] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain. |
| [2] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Brain and Lymph. |
| [3] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-493 (ISOFORM 1). Tissue: Brain. |
| [4] | "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin." Takatsu H., Yoshino K., Nakayama K. Biochem. Biophys. Res. Commun. 271:719-725(2000) [PubMed: 10814529] [Abstract] Cited for: INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2. |
| [5] | "EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking." Mills I.G., Praefcke G.J.K., Vallis Y., Peter B.J., Olesen L.E., Gallop J.L., Butler P.J.G., Evans P.R., McMahon H.T. J. Cell Biol. 160:213-222(2003) [PubMed: 12538641] [Abstract] Cited for: DOMAIN, INTERACTION WITH AP1G1. |
| [6] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752 AND SER-756, MASS SPECTROMETRY. Tissue: Epithelium. |
| [7] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1075, MASS SPECTROMETRY. Tissue: Platelet. |
| [8] | "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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, MASS SPECTROMETRY. |
| [9] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-752; SER-909; SER-919; SER-935 AND SER-1075, MASS SPECTROMETRY. |
| [10] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-919; SER-935 AND SER-936, MASS SPECTROMETRY. |
| [11] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-752; SER-852 AND SER-855, MASS SPECTROMETRY. Tissue: T-cell. |
| [12] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-513 AND LYS-744, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF169548 mRNA. Translation: AAD49732.1. BC090930 mRNA. Translation: AAH90930.1. BC117313 mRNA. Translation: AAI17314.1. BC143478 mRNA. Translation: AAI43479.1. AK126988 mRNA. No translation available. | |
| IPI | IPI00297931. IPI00798416. IPI00827622. |
| RefSeq | NP_001157016.1. NP_001157017.1. NP_001157018.1. NP_001157019.1. NP_009178.3. NP_542117.3. NP_942583.1. |
| UniGene | Hs.655178 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9UMZ2. |
PTM databases | |
| PhosphoSite | Q9UMZ2. |
Proteomic databases | |
| PRIDE | Q9UMZ2. |
Genome annotation databases | |
| Ensembl | ENST00000339208; ENSP00000343610; ENSG00000006114; Homo sapiens. [Genome view] ENST00000346661; ENSP00000005279; ENSG00000006114; Homo sapiens. [Genome view] |
| GeneID | 11276. |
| KEGG | hsa:11276. |
| UCSC | uc002hoa.1. human. uc002hoc.1. human. uc002hod.1. human. |
Organism-specific databases | |
| CTD | 11276. |
| GeneCards | GC17M032952. |
| H-InvDB | HIX0013748. |
| HGNC | HGNC:557. SYNRG. |
| HPA | HPA023554. HPA023555. |
| MIM | 607291. gene. |
| PharmGKB | PA24847. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q9UMZ2. |
| HOVERGEN | Q9UMZ2. |
Gene expression databases | |
| ArrayExpress | Q9UMZ2. |
| Bgee | Q9UMZ2. |
| CleanEx | HS_AP1GBP1. |
| Genevestigator | Q9UMZ2. |
| GermOnline | ENSG00000006114. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR011992. EF-Hand_type. IPR000261. EPS15_homology. [Graphical view] |
| Gene3D | G3DSA:1.10.238.10. EF-Hand_type. 1 hit. |
| PROSITE | PS50031. EH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 42921. |
| SOURCE | Search... |
Entry information
| Entry name | SYNRG_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9UMZ2 Secondary accession number(s): B7ZKZ3 Q6ZT17 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


