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Q9UMZ2 (SYNRG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synergin gamma
Alternative name(s):
AP1 subunit gamma-binding protein 1
Gamma-synergin
Gene names
Name:SYNRG
Synonyms:AP1GBP1, SYNG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1314 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity. Golgi apparatustrans-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.6

Sequence similarities

Contains 1 EH domain.

Sequence caution

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

Ontologies

Alternative products

This entry describes 8 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.
Isoform 4 (identifier: Q9UMZ2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1260-1271: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9UMZ2-6)

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.
Isoform 6 (identifier: Q9UMZ2-7)

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.
Isoform 7 (identifier: Q9UMZ2-8)

The sequence of this isoform differs from the canonical sequence as follows:
     40-40: Missing.
     198-275: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: Q9UMZ2-9)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13141314Synergin gamma
PRO_0000072387

Regions

Domain295 – 38894EH
Region518 – 786269Interaction with A1P1G1 and A1P1G2
Coiled coil115 – 15541 Potential
Motif457 – 4615DFXDF motif 1
Motif690 – 6945DFXDF motif 2
Motif775 – 7795DFXDF motif 3

Amino acid modifications

Modified residue4731Phosphoserine Ref.9 Ref.12 Ref.16
Modified residue5131N6-acetyllysine Ref.13
Modified residue5801Phosphoserine By similarity
Modified residue7201Phosphoserine Ref.14
Modified residue7441N6-acetyllysine Ref.13
Modified residue7521Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.16
Modified residue8521Phosphoserine Ref.12
Modified residue8551Phosphoserine Ref.12
Modified residue9091Phosphoserine Ref.9
Modified residue9191Phosphoserine Ref.9
Modified residue9351Phosphoserine Ref.9
Modified residue10751Phosphoserine Ref.9 Ref.14 Ref.16

Natural variations

Alternative sequence401Missing in isoform 7.
VSP_054732
Alternative sequence198 – 27578Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_023015
Alternative sequence366 – 44883Missing in isoform 5.
VSP_043281
Alternative sequence870 – 91445Missing in isoform 5 and isoform 8.
VSP_043282
Alternative sequence12221T → TCCWEKMTVITKHLSPYHEL LEEK in isoform 6.
VSP_054733
Alternative sequence1260 – 127112Missing in isoform 3, isoform 4 and isoform 8.
VSP_023016
Natural variant401A → G.
Corresponds to variant rs12944821 [ dbSNP | Ensembl ].
VAR_051395
Natural variant2221T → A.
Corresponds to variant rs12602536 [ dbSNP | Ensembl ].
VAR_051396

Experimental info

Sequence conflict2131S → P in AK126988. Ref.4
Sequence conflict3491K → R in AK126988. Ref.4
Sequence conflict11231E → K in AAD49732. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 70C105203EF0BBBF

FASTA1,314140,654
        10         20         30         40         50         60 
MALRPGAGSG GGGAAGAGAG SAGGGGFMFP VAGGIRPPQA GLMPMQQQGF PMVSVMQPNM 

        70         80         90        100        110        120 
QGIMGMNYSS QMSQGPIAMQ AGIPMGPMPA AGMPYLGQAP FLGMRPPGPQ YTPDMQKQFA 

       130        140        150        160        170        180 
EEQQKRFEQQ QKLLEEERKR RQFEEQKQKL RLLSSVKPKT GEKSRDDALE AIKGNLDGFS 

       190        200        210        220        230        240 
RDAKMHPTPA SHPKKPGPSL EEKFLVSCDI STSGQEQIKL NTSEVGHKAL GPGSSKKYPS 

       250        260        270        280        290        300 
LMASNGVAVD GCVSGTTTAE AENTSDQNLS IEESGVGVFP SQDPAQPRMP PWIYNESLVP 

       310        320        330        340        350        360 
DAYKKILETT MTPTGIDTAK LYPILMSSGL PRETLGQIWA LANRTTPGKL TKEELYTVLA 

       370        380        390        400        410        420 
MIAVTQRGVP AMSPDALNQF PAAPIPTLSG FSMTLPTPVS QPTVIPSGPA GSMPLSLGQP 

       430        440        450        460        470        480 
VMGINLVGPV GGAAAQASSG FIPTYPANQV VKPEEDDFQD FQDASKSGSL DDSFSDFQEL 

       490        500        510        520        530        540 
PASSKTSNSQ HGNSAPSLLM PLPGTKALPS MDKYAVFKGI AADKSSENTV PPGDPGDKYS 

       550        560        570        580        590        600 
AFRELEQTAE NKPLGESFAE FRSAGTDDGF TDFKTADSVS PLEPPTKDKT FPPSFPSGTI 

       610        620        630        640        650        660 
QQKQQTQVKN PLNLADLDMF SSVNCSSEKP LSFSAVFSTS KSVSTPQSTG SAATMTALAA 

       670        680        690        700        710        720 
TKTSSLADDF GEFSLFGEYS GLAPVGEQDD FADFMAFSNS SISSEQKPDD KYDALKEEAS 

       730        740        750        760        770        780 
PVPLTSNVGS TVKGGQNSTA ASTKYDVFRQ LSLEGSGLGV EDLKDNTPSG KSDDDFADFH 

       790        800        810        820        830        840 
SSKFSSINSD KSLGEKAVAF RHTKEDSASV KSLDLPSIGG SSVGKEDSED ALSVQFDMKL 

       850        860        870        880        890        900 
ADVGGDLKHV MSDSSLDLPT VSGQHPPAAD IEDLKYAAFG SYSSNFAVST LTSYDWSDRD 

       910        920        930        940        950        960 
DATQGRKLSP FVLSAGSGSP SATSILQKKE TSFGSSENIT MTSLSKVTTF VSEDALPETT 

       970        980        990       1000       1010       1020 
FPALASFKDT IPQTSEQKEY ENRDYKDFTK QDLPTAERSQ EATCPSPASS GASQETPNEC 

      1030       1040       1050       1060       1070       1080 
SDDFGEFQSE KPKISKFDFL VATSQSKMKS SEEMIKSELA TFDLSVQGSH KRSLSLGDKE 

      1090       1100       1110       1120       1130       1140 
ISRSSPSPAL EQPFRDRSNT LNEKPALPVI RDKYKDLTGE VEENERYAYE WQRCLGSALN 

      1150       1160       1170       1180       1190       1200 
VIKKANDTLN GISSSSVCTE VIQSAQGMEY LLGVVEVYRV TKRVELGIKA TAVCSEKLQQ 

      1210       1220       1230       1240       1250       1260 
LLKDIDKVWN NLIGFMSLAT LTPDENSLDF SSCMLRPGIK NAQELACGVC LLNVDSRSRK 

      1270       1280       1290       1300       1310 
EEKPAEEHPK KAFNSETDSF KLAYGGHQYH ASCANFWINC VEPKPPGLVL PDLL 

« Hide

Isoform 2 [UniParc].

Checksum: D22A62B08D8E0B01
Show »

FASTA1,236132,654
Isoform 3 [UniParc].

Checksum: 3D54B7286CED8226
Show »

FASTA1,224131,222
Isoform 4 [UniParc].

Checksum: 35E8013E37F73B80
Show »

FASTA1,302139,223
Isoform 5 [UniParc].

Checksum: F31FEC0F4F4515FC
Show »

FASTA1,108119,509
Isoform 6 [UniParc].

Checksum: 00E53A7CC4AC2FC5
Show »

FASTA1,259135,454
Isoform 7 [UniParc].

Checksum: C243DC3D72946E67
Show »

FASTA1,235132,582
Isoform 8 [UniParc].

Checksum: BAEC72332586ED58
Show »

FASTA1,179126,214

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] [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. expand/collapse author list , 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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
Cited for: DOMAIN, INTERACTION WITH AP1G1.
[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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11321.1. [Q9UMZ2-1]
CCDS11322.2. [Q9UMZ2-4]
CCDS54113.1. [Q9UMZ2-6]
RefSeqNP_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]
UniGeneHs.594647.

3D structure databases

ProteinModelPortalQ9UMZ2.
SMRQ9UMZ2. Positions 290-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116432. 7 interactions.
MINTMINT-126209.
STRING9606.ENSP00000005279.

PTM databases

PhosphoSiteQ9UMZ2.

Polymorphism databases

DMDM143811464.

Proteomic databases

MaxQBQ9UMZ2.
PaxDbQ9UMZ2.
PRIDEQ9UMZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339208; ENSP00000343610; ENSG00000006114. [Q9UMZ2-1]
ENST00000345615; ENSP00000315722; ENSG00000006114. [Q9UMZ2-4]
ENST00000346661; ENSP00000005279; ENSG00000006114. [Q9UMZ2-5]
ENST00000394378; ENSP00000377903; ENSG00000006114.
ENST00000585472; ENSP00000466741; ENSG00000006114.
ENST00000591288; ENSP00000468371; ENSG00000006114. [Q9UMZ2-6]
GeneID11276.
KEGGhsa:11276.
UCSCuc002hoa.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

CTD11276.
GeneCardsGC17M035874.
HGNCHGNC:557. SYNRG.
HPAHPA023554.
HPA023555.
MIM607291. gene.
neXtProtNX_Q9UMZ2.
PharmGKBPA24847.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136044.
HOGENOMHOG000293152.
HOVERGENHBG055053.
OMADLDMFSS.
OrthoDBEOG7GXP9S.
PhylomeDBQ9UMZ2.
TreeFamTF316700.

Gene expression databases

ArrayExpressQ9UMZ2.
BgeeQ9UMZ2.
CleanExHS_AP1GBP1.
GenevestigatorQ9UMZ2.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR000261. EPS15_homology.
[Graphical view]
PROSITEPS50031. EH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSynergin_gamma.
GenomeRNAi11276.
NextBio42921.
PROQ9UMZ2.
SOURCESearch...

Entry information

Entry nameSYNRG_HUMAN
AccessionPrimary (citable) accession number: Q9UMZ2
Secondary accession number(s): A8MWU4 expand/collapse secondary AC list , B7ZKZ2, B7ZKZ3, Q17RI2, Q5BKU5, Q6ZT17
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM