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Q9UMZ2

- SYNRG_HUMAN

UniProt

Q9UMZ2 - SYNRG_HUMAN

Protein

Synergin gamma

Gene

SYNRG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. intracellular protein transport Source: ProtInc

    Keywords - Biological processi

    Endocytosis, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synergin gamma
    Alternative name(s):
    AP1 subunit gamma-binding protein 1
    Gamma-synergin
    Gene namesi
    Name:SYNRG
    Synonyms:AP1GBP1, SYNG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:557. SYNRG.

    Subcellular locationi

    Cytoplasm By similarity. Golgi apparatustrans-Golgi network membrane By similarity; Peripheral membrane protein By similarity
    Note: Associates with membranes via the adapter protein complex AP-1. Colocalizes with AP1G1 By similarity.By similarity

    GO - Cellular componenti

    1. AP-1 adaptor complex Source: ProtInc
    2. cytoplasm Source: ProtInc
    3. Golgi apparatus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24847.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13141314Synergin gammaPRO_0000072387Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei473 – 4731Phosphoserine3 Publications
    Modified residuei513 – 5131N6-acetyllysine1 Publication
    Modified residuei580 – 5801PhosphoserineBy similarity
    Modified residuei720 – 7201Phosphoserine1 Publication
    Modified residuei744 – 7441N6-acetyllysine1 Publication
    Modified residuei752 – 7521Phosphoserine6 Publications
    Modified residuei852 – 8521Phosphoserine1 Publication
    Modified residuei855 – 8551Phosphoserine1 Publication
    Modified residuei909 – 9091Phosphoserine1 Publication
    Modified residuei919 – 9191Phosphoserine1 Publication
    Modified residuei935 – 9351Phosphoserine1 Publication
    Modified residuei1075 – 10751Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UMZ2.
    PaxDbiQ9UMZ2.
    PRIDEiQ9UMZ2.

    PTM databases

    PhosphoSiteiQ9UMZ2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UMZ2.
    BgeeiQ9UMZ2.
    CleanExiHS_AP1GBP1.
    GenevestigatoriQ9UMZ2.

    Organism-specific databases

    HPAiHPA023554.
    HPA023555.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi116432. 7 interactions.
    MINTiMINT-126209.
    STRINGi9606.ENSP00000005279.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UMZ2.
    SMRiQ9UMZ2. Positions 290-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini295 – 38894EHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni518 – 786269Interaction with A1P1G1 and A1P1G2Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili115 – 15541Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi457 – 4615DFXDF motif 1
    Motifi690 – 6945DFXDF motif 2
    Motifi775 – 7795DFXDF motif 3

    Domaini

    The DFXDF motifs mediate the interaction with gamma-appendage subunits AP1G1 and AP1G2.1 Publication

    Sequence similaritiesi

    Contains 1 EH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG136044.
    HOGENOMiHOG000293152.
    HOVERGENiHBG055053.
    OMAiDLDMFSS.
    OrthoDBiEOG7GXP9S.
    PhylomeDBiQ9UMZ2.
    TreeFamiTF316700.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR000261. EPS15_homology.
    [Graphical view]
    PROSITEiPS50031. EH. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UMZ2-1) [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

    MALRPGAGSG GGGAAGAGAG SAGGGGFMFP VAGGIRPPQA GLMPMQQQGF     50
    PMVSVMQPNM QGIMGMNYSS QMSQGPIAMQ AGIPMGPMPA AGMPYLGQAP 100
    FLGMRPPGPQ YTPDMQKQFA EEQQKRFEQQ QKLLEEERKR RQFEEQKQKL 150
    RLLSSVKPKT GEKSRDDALE AIKGNLDGFS RDAKMHPTPA SHPKKPGPSL 200
    EEKFLVSCDI STSGQEQIKL NTSEVGHKAL GPGSSKKYPS LMASNGVAVD 250
    GCVSGTTTAE AENTSDQNLS IEESGVGVFP SQDPAQPRMP PWIYNESLVP 300
    DAYKKILETT MTPTGIDTAK LYPILMSSGL PRETLGQIWA LANRTTPGKL 350
    TKEELYTVLA MIAVTQRGVP AMSPDALNQF PAAPIPTLSG FSMTLPTPVS 400
    QPTVIPSGPA GSMPLSLGQP VMGINLVGPV GGAAAQASSG FIPTYPANQV 450
    VKPEEDDFQD FQDASKSGSL DDSFSDFQEL PASSKTSNSQ HGNSAPSLLM 500
    PLPGTKALPS MDKYAVFKGI AADKSSENTV PPGDPGDKYS AFRELEQTAE 550
    NKPLGESFAE FRSAGTDDGF TDFKTADSVS PLEPPTKDKT FPPSFPSGTI 600
    QQKQQTQVKN PLNLADLDMF SSVNCSSEKP LSFSAVFSTS KSVSTPQSTG 650
    SAATMTALAA TKTSSLADDF GEFSLFGEYS GLAPVGEQDD FADFMAFSNS 700
    SISSEQKPDD KYDALKEEAS PVPLTSNVGS TVKGGQNSTA ASTKYDVFRQ 750
    LSLEGSGLGV EDLKDNTPSG KSDDDFADFH SSKFSSINSD KSLGEKAVAF 800
    RHTKEDSASV KSLDLPSIGG SSVGKEDSED ALSVQFDMKL ADVGGDLKHV 850
    MSDSSLDLPT VSGQHPPAAD IEDLKYAAFG SYSSNFAVST LTSYDWSDRD 900
    DATQGRKLSP FVLSAGSGSP SATSILQKKE TSFGSSENIT MTSLSKVTTF 950
    VSEDALPETT FPALASFKDT IPQTSEQKEY ENRDYKDFTK QDLPTAERSQ 1000
    EATCPSPASS GASQETPNEC SDDFGEFQSE KPKISKFDFL VATSQSKMKS 1050
    SEEMIKSELA TFDLSVQGSH KRSLSLGDKE ISRSSPSPAL EQPFRDRSNT 1100
    LNEKPALPVI RDKYKDLTGE VEENERYAYE WQRCLGSALN VIKKANDTLN 1150
    GISSSSVCTE VIQSAQGMEY LLGVVEVYRV TKRVELGIKA TAVCSEKLQQ 1200
    LLKDIDKVWN NLIGFMSLAT LTPDENSLDF SSCMLRPGIK NAQELACGVC 1250
    LLNVDSRSRK EEKPAEEHPK KAFNSETDSF KLAYGGHQYH ASCANFWINC 1300
    VEPKPPGLVL PDLL 1314
    Length:1,314
    Mass (Da):140,654
    Last modified:April 3, 2007 - v2
    Checksum:i70C105203EF0BBBF
    GO
    Isoform 2 (identifier: Q9UMZ2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-275: Missing.

    Show »
    Length:1,236
    Mass (Da):132,654
    Checksum:iD22A62B08D8E0B01
    GO
    Isoform 3 (identifier: Q9UMZ2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-275: Missing.
         1260-1271: Missing.

    Show »
    Length:1,224
    Mass (Da):131,222
    Checksum:i3D54B7286CED8226
    GO
    Isoform 4 (identifier: Q9UMZ2-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1260-1271: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,302
    Mass (Da):139,223
    Checksum:i35E8013E37F73B80
    GO
    Isoform 5 (identifier: Q9UMZ2-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-275: Missing.
         366-448: Missing.
         870-914: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,108
    Mass (Da):119,509
    Checksum:iF31FEC0F4F4515FC
    GO
    Isoform 6 (identifier: Q9UMZ2-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-275: Missing.
         1222-1222: T → TCCWEKMTVITKHLSPYHELLEEK

    Note: Gene prediction based on EST data.

    Show »
    Length:1,259
    Mass (Da):135,454
    Checksum:i00E53A7CC4AC2FC5
    GO
    Isoform 7 (identifier: Q9UMZ2-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         40-40: Missing.
         198-275: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,235
    Mass (Da):132,582
    Checksum:iC243DC3D72946E67
    GO
    Isoform 8 (identifier: Q9UMZ2-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-275: Missing.
         870-914: Missing.
         1260-1271: Missing.

    Show »
    Length:1,179
    Mass (Da):126,214
    Checksum:iBAEC72332586ED58
    GO

    Sequence cautioni

    The sequence AK126988 differs from that shown. Reason: Intron retention.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131S → P in AK126988. (PubMed:14702039)Curated
    Sequence conflicti349 – 3491K → R in AK126988. (PubMed:14702039)Curated
    Sequence conflicti1123 – 11231E → K in AAD49732. (PubMed:10477754)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401A → G.
    Corresponds to variant rs12944821 [ dbSNP | Ensembl ].
    VAR_051395
    Natural varianti222 – 2221T → A.
    Corresponds to variant rs12602536 [ dbSNP | Ensembl ].
    VAR_051396

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei40 – 401Missing in isoform 7. 1 PublicationVSP_054732
    Alternative sequencei198 – 27578Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_023015Add
    BLAST
    Alternative sequencei366 – 44883Missing in isoform 5. 1 PublicationVSP_043281Add
    BLAST
    Alternative sequencei870 – 91445Missing in isoform 5 and isoform 8. 1 PublicationVSP_043282Add
    BLAST
    Alternative sequencei1222 – 12221T → TCCWEKMTVITKHLSPYHEL LEEK in isoform 6. CuratedVSP_054733
    Alternative sequencei1260 – 127112Missing in isoform 3, isoform 4 and isoform 8. 1 PublicationVSP_023016Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169548 mRNA. Translation: AAD49732.1.
    AC004099 Genomic DNA. No translation available.
    AC091199 Genomic DNA. No translation available.
    BC090930 mRNA. Translation: AAH90930.1.
    BC117313 mRNA. Translation: AAI17314.1.
    BC143476 mRNA. Translation: AAI43477.1.
    BC143478 mRNA. Translation: AAI43479.1.
    AK126988 mRNA. No translation available.
    CCDSiCCDS11321.1. [Q9UMZ2-1]
    CCDS11322.2. [Q9UMZ2-4]
    CCDS54113.1. [Q9UMZ2-6]
    CCDS54114.1. [Q9UMZ2-7]
    CCDS59284.1. [Q9UMZ2-8]
    CCDS59285.1. [Q9UMZ2-9]
    RefSeqiNP_001157016.1. NM_001163544.2. [Q9UMZ2-3]
    NP_001157017.1. NM_001163545.2. [Q9UMZ2-8]
    NP_001157018.1. NM_001163546.2. [Q9UMZ2-9]
    NP_001157019.1. NM_001163547.2. [Q9UMZ2-6]
    NP_009178.3. NM_007247.5. [Q9UMZ2-1]
    NP_542117.3. NM_080550.4. [Q9UMZ2-4]
    NP_942583.1. NM_198882.2. [Q9UMZ2-7]
    XP_005257045.1. XM_005256988.2. [Q9UMZ2-5]
    XP_006725371.1. XM_006725308.1. [Q9UMZ2-5]
    UniGeneiHs.594647.

    Genome annotation databases

    GeneIDi11276.
    KEGGihsa:11276.
    UCSCiuc002hoa.3. human. [Q9UMZ2-1]
    uc002hob.3. human. [Q9UMZ2-5]
    uc002hoc.3. human. [Q9UMZ2-3]
    uc002hod.3. human. [Q9UMZ2-4]
    uc010wdg.2. human. [Q9UMZ2-6]

    Polymorphism databases

    DMDMi143811464.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169548 mRNA. Translation: AAD49732.1 .
    AC004099 Genomic DNA. No translation available.
    AC091199 Genomic DNA. No translation available.
    BC090930 mRNA. Translation: AAH90930.1 .
    BC117313 mRNA. Translation: AAI17314.1 .
    BC143476 mRNA. Translation: AAI43477.1 .
    BC143478 mRNA. Translation: AAI43479.1 .
    AK126988 mRNA. No translation available.
    CCDSi CCDS11321.1. [Q9UMZ2-1 ]
    CCDS11322.2. [Q9UMZ2-4 ]
    CCDS54113.1. [Q9UMZ2-6 ]
    CCDS54114.1. [Q9UMZ2-7 ]
    CCDS59284.1. [Q9UMZ2-8 ]
    CCDS59285.1. [Q9UMZ2-9 ]
    RefSeqi NP_001157016.1. NM_001163544.2. [Q9UMZ2-3 ]
    NP_001157017.1. NM_001163545.2. [Q9UMZ2-8 ]
    NP_001157018.1. NM_001163546.2. [Q9UMZ2-9 ]
    NP_001157019.1. NM_001163547.2. [Q9UMZ2-6 ]
    NP_009178.3. NM_007247.5. [Q9UMZ2-1 ]
    NP_542117.3. NM_080550.4. [Q9UMZ2-4 ]
    NP_942583.1. NM_198882.2. [Q9UMZ2-7 ]
    XP_005257045.1. XM_005256988.2. [Q9UMZ2-5 ]
    XP_006725371.1. XM_006725308.1. [Q9UMZ2-5 ]
    UniGenei Hs.594647.

    3D structure databases

    ProteinModelPortali Q9UMZ2.
    SMRi Q9UMZ2. Positions 290-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116432. 7 interactions.
    MINTi MINT-126209.
    STRINGi 9606.ENSP00000005279.

    PTM databases

    PhosphoSitei Q9UMZ2.

    Polymorphism databases

    DMDMi 143811464.

    Proteomic databases

    MaxQBi Q9UMZ2.
    PaxDbi Q9UMZ2.
    PRIDEi Q9UMZ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 11276.
    KEGGi hsa:11276.
    UCSCi uc002hoa.3. human. [Q9UMZ2-1 ]
    uc002hob.3. human. [Q9UMZ2-5 ]
    uc002hoc.3. human. [Q9UMZ2-3 ]
    uc002hod.3. human. [Q9UMZ2-4 ]
    uc010wdg.2. human. [Q9UMZ2-6 ]

    Organism-specific databases

    CTDi 11276.
    GeneCardsi GC17M035874.
    HGNCi HGNC:557. SYNRG.
    HPAi HPA023554.
    HPA023555.
    MIMi 607291. gene.
    neXtProti NX_Q9UMZ2.
    PharmGKBi PA24847.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG136044.
    HOGENOMi HOG000293152.
    HOVERGENi HBG055053.
    OMAi DLDMFSS.
    OrthoDBi EOG7GXP9S.
    PhylomeDBi Q9UMZ2.
    TreeFami TF316700.

    Miscellaneous databases

    GeneWikii Synergin_gamma.
    GenomeRNAii 11276.
    NextBioi 42921.
    PROi Q9UMZ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UMZ2.
    Bgeei Q9UMZ2.
    CleanExi HS_AP1GBP1.
    Genevestigatori Q9UMZ2.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR000261. EPS15_homology.
    [Graphical view ]
    PROSITEi PS50031. EH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORMS 2; 3; 5 AND 7).
      Tissue: Brain and Lymph.
    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] OF 27-493 (ISOFORM 1).
      Tissue: Brain.
    5. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2.
    6. Cited for: DOMAIN, INTERACTION WITH AP1G1.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-752; SER-909; SER-919; SER-935 AND SER-1075, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-752; SER-852 AND SER-855, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-513 AND LYS-744, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; SER-752 AND SER-1075, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-752 AND SER-1075, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYNRG_HUMAN
    AccessioniPrimary (citable) accession number: Q9UMZ2
    Secondary accession number(s): A8MWU4
    , B7ZKZ2, B7ZKZ3, Q17RI2, Q5BKU5, Q6ZT17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3