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Q9UMZ2

- SYNRG_HUMAN

UniProt

Q9UMZ2 - SYNRG_HUMAN

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Protein

Synergin gamma

Gene

SYNRG

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UMZ2.
CleanExiHS_AP1GBP1.
ExpressionAtlasiQ9UMZ2. differential.
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. 10 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.
GeneTreeiENSGT00390000010789.
HOGENOMiHOG000293152.
HOVERGENiHBG055053.
InParanoidiQ9UMZ2.
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

        10         20         30         40         50
MALRPGAGSG GGGAAGAGAG SAGGGGFMFP VAGGIRPPQA GLMPMQQQGF
60 70 80 90 100
PMVSVMQPNM QGIMGMNYSS QMSQGPIAMQ AGIPMGPMPA AGMPYLGQAP
110 120 130 140 150
FLGMRPPGPQ YTPDMQKQFA EEQQKRFEQQ QKLLEEERKR RQFEEQKQKL
160 170 180 190 200
RLLSSVKPKT GEKSRDDALE AIKGNLDGFS RDAKMHPTPA SHPKKPGPSL
210 220 230 240 250
EEKFLVSCDI STSGQEQIKL NTSEVGHKAL GPGSSKKYPS LMASNGVAVD
260 270 280 290 300
GCVSGTTTAE AENTSDQNLS IEESGVGVFP SQDPAQPRMP PWIYNESLVP
310 320 330 340 350
DAYKKILETT MTPTGIDTAK LYPILMSSGL PRETLGQIWA LANRTTPGKL
360 370 380 390 400
TKEELYTVLA MIAVTQRGVP AMSPDALNQF PAAPIPTLSG FSMTLPTPVS
410 420 430 440 450
QPTVIPSGPA GSMPLSLGQP VMGINLVGPV GGAAAQASSG FIPTYPANQV
460 470 480 490 500
VKPEEDDFQD FQDASKSGSL DDSFSDFQEL PASSKTSNSQ HGNSAPSLLM
510 520 530 540 550
PLPGTKALPS MDKYAVFKGI AADKSSENTV PPGDPGDKYS AFRELEQTAE
560 570 580 590 600
NKPLGESFAE FRSAGTDDGF TDFKTADSVS PLEPPTKDKT FPPSFPSGTI
610 620 630 640 650
QQKQQTQVKN PLNLADLDMF SSVNCSSEKP LSFSAVFSTS KSVSTPQSTG
660 670 680 690 700
SAATMTALAA TKTSSLADDF GEFSLFGEYS GLAPVGEQDD FADFMAFSNS
710 720 730 740 750
SISSEQKPDD KYDALKEEAS PVPLTSNVGS TVKGGQNSTA ASTKYDVFRQ
760 770 780 790 800
LSLEGSGLGV EDLKDNTPSG KSDDDFADFH SSKFSSINSD KSLGEKAVAF
810 820 830 840 850
RHTKEDSASV KSLDLPSIGG SSVGKEDSED ALSVQFDMKL ADVGGDLKHV
860 870 880 890 900
MSDSSLDLPT VSGQHPPAAD IEDLKYAAFG SYSSNFAVST LTSYDWSDRD
910 920 930 940 950
DATQGRKLSP FVLSAGSGSP SATSILQKKE TSFGSSENIT MTSLSKVTTF
960 970 980 990 1000
VSEDALPETT FPALASFKDT IPQTSEQKEY ENRDYKDFTK QDLPTAERSQ
1010 1020 1030 1040 1050
EATCPSPASS GASQETPNEC SDDFGEFQSE KPKISKFDFL VATSQSKMKS
1060 1070 1080 1090 1100
SEEMIKSELA TFDLSVQGSH KRSLSLGDKE ISRSSPSPAL EQPFRDRSNT
1110 1120 1130 1140 1150
LNEKPALPVI RDKYKDLTGE VEENERYAYE WQRCLGSALN VIKKANDTLN
1160 1170 1180 1190 1200
GISSSSVCTE VIQSAQGMEY LLGVVEVYRV TKRVELGIKA TAVCSEKLQQ
1210 1220 1230 1240 1250
LLKDIDKVWN NLIGFMSLAT LTPDENSLDF SSCMLRPGIK NAQELACGVC
1260 1270 1280 1290 1300
LLNVDSRSRK EEKPAEEHPK KAFNSETDSF KLAYGGHQYH ASCANFWINC
1310
VEPKPPGLVL PDLL
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

EnsembliENST00000612223; ENSP00000483453; ENSG00000275066. [Q9UMZ2-1]
ENST00000614941; ENSP00000481151; ENSG00000275066. [Q9UMZ2-6]
ENST00000616179; ENSP00000482962; ENSG00000275066. [Q9UMZ2-9]
ENST00000619541; ENSP00000477885; ENSG00000275066. [Q9UMZ2-8]
ENST00000621136; ENSP00000484529; ENSG00000275066. [Q9UMZ2-4]
ENST00000622045; ENSP00000483063; ENSG00000275066. [Q9UMZ2-7]
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. 10 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

Ensembli ENST00000612223 ; ENSP00000483453 ; ENSG00000275066 . [Q9UMZ2-1 ]
ENST00000614941 ; ENSP00000481151 ; ENSG00000275066 . [Q9UMZ2-6 ]
ENST00000616179 ; ENSP00000482962 ; ENSG00000275066 . [Q9UMZ2-9 ]
ENST00000619541 ; ENSP00000477885 ; ENSG00000275066 . [Q9UMZ2-8 ]
ENST00000621136 ; ENSP00000484529 ; ENSG00000275066 . [Q9UMZ2-4 ]
ENST00000622045 ; ENSP00000483063 ; ENSG00000275066 . [Q9UMZ2-7 ]
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.
GeneTreei ENSGT00390000010789.
HOGENOMi HOG000293152.
HOVERGENi HBG055053.
InParanoidi Q9UMZ2.
OMAi DLDMFSS.
OrthoDBi EOG7GXP9S.
PhylomeDBi Q9UMZ2.
TreeFami TF316700.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9UMZ2.
CleanExi HS_AP1GBP1.
ExpressionAtlasi Q9UMZ2. differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 116 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