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O43426 (SYNJ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Synaptojanin-1

EC=3.1.3.36
Alternative name(s):
Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 1
Gene names
Name:SYNJ1
Synonyms:KIAA0910
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1573 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inositol 5-phosphatase which has a role in clathrin-mediated endocytosis.

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.

Subunit structure

Interacts with ASH/GRB2. Interacts with PACSIN1, PACSIN2 and PACSIN3 By similarity. Binds AMPH, SH3GL1, SH3GL2 and SH3GL3. Interacts with MYO1E (via SH3 domain). Ref.6 Ref.7

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Concentrated at clathrin-coated endocytic intermediates in nerve terminals. Isoform 1 is more enriched than isoform 2 in developing brain as well as non-neuronal cells. Isoform 2 is very abundant in nerve terminals.

Domain

Binds to EPS15 (a clathrin coat-associated protein) via a C-terminal domain containing three Asn-Pro-Phe (NPF) repeats By similarity.

The C-terminal proline-rich region mediates binding to a variety of SH3 domain-containing proteins including AMPH, SH3GL1, SH3GL2, SH3GL3 and GRB2.

Sequence similarities

Belongs to the synaptojanin family.

In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.

Contains 1 RRM (RNA recognition motif) domain.

Contains 1 SAC domain.

Sequence caution

The sequence BAA74933.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43426-1)

Also known as: Synaptojanin-170;

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: O43426-2)

Also known as: Synaptojanin-145;

The sequence of this isoform differs from the canonical sequence as follows:
     1306-1311: VKTNGI → QEQPSG
     1312-1573: Missing.
Isoform 3 (identifier: O43426-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1144-1159: Missing.
     1306-1311: VKTNGI → QEQPSG
     1312-1573: Missing.
Isoform 4 (identifier: O43426-5)

The sequence of this isoform differs from the canonical sequence as follows:
     451-451: K → KAGK
     504-511: Missing.
     525-1573: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15731573Synaptojanin-1
PRO_0000209730

Regions

Domain119 – 442324SAC
Domain902 – 97170RRM
Repeat1396 – 139831
Repeat1406 – 140832
Repeat1417 – 141933
Region500 – 899400Catalytic Potential
Region1396 – 1419243 X 3 AA repeats of N-P-F
Compositional bias900 – 1573674Pro-rich
Compositional bias1033 – 10364Poly-Ser
Compositional bias1108 – 11136Poly-Pro
Compositional bias1126 – 11294Poly-Pro
Compositional bias1485 – 14884Poly-Glu
Compositional bias1538 – 15447Poly-Pro

Amino acid modifications

Modified residue8301Phosphoserine Ref.8 Ref.9
Modified residue12201Phosphothreonine Ref.8
Modified residue13181Phosphoserine Ref.10
Modified residue15511Phosphoserine Ref.8
Modified residue15651Phosphoserine Ref.8

Natural variations

Alternative sequence4511K → KAGK in isoform 4.
VSP_035709
Alternative sequence504 – 5118Missing in isoform 4.
VSP_035710
Alternative sequence525 – 15731049Missing in isoform 4.
VSP_035711
Alternative sequence1144 – 115916Missing in isoform 3.
VSP_041578
Alternative sequence1306 – 13116VKTNGI → QEQPSG in isoform 2 and isoform 3.
VSP_002682
Alternative sequence1312 – 1573262Missing in isoform 2 and isoform 3.
VSP_002683
Natural variant2951K → R. Ref.1
Corresponds to variant rs2254562 [ dbSNP | Ensembl ].
VAR_047308
Natural variant13661V → A.
Corresponds to variant rs9980589 [ dbSNP | Ensembl ].
VAR_047309
Natural variant15081P → L.
Corresponds to variant rs2230767 [ dbSNP | Ensembl ].
VAR_059357
Natural variant15451L → P.
Corresponds to variant rs2230767 [ dbSNP | Ensembl ].
VAR_047310
Natural variant15471P → L.
Corresponds to variant rs2230767 [ dbSNP | Ensembl ].
VAR_049603

Experimental info

Sequence conflict1093 – 110816Missing in BAA74933. Ref.1
Sequence conflict13661V → VNT in AAC51922. Ref.1

Secondary structure

............... 1573
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Synaptojanin-170) [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: D50B249B1EBFFC18

FASTA1,573173,103
        10         20         30         40         50         60 
MAFSKGFRIY HKLDPPPFSL IVETRHKEEC LMFESGAVAV LSSAEKEAIK GTYSKVLDAY 

        70         80         90        100        110        120 
GLLGVLRLNL GDTMLHYLVL VTGCMSVGKI QESEVFRVTS TEFISLRIDS SDEDRISEVR 

       130        140        150        160        170        180 
KVLNSGNFYF AWSASGISLD LSLNAHRSMQ EQTTDNRFFW NQSLHLHLKH YGVNCDDWLL 

       190        200        210        220        230        240 
RLMCGGVEIR TIYAAHKQAK ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVVYLD 

       250        260        270        280        290        300 
DSVSSFIQIR GSVPLFWEQP GLQVGSHRVR MSRGFEANAP AFDRHFRTLK NLYGKQIIVN 

       310        320        330        340        350        360 
LLGSKEGEHM LSKAFQSHLK ASEHAADIQM VNFDYHQMVK GGKAEKLHSV LKPQVQKFLD 

       370        380        390        400        410        420 
YGFFYFNGSE VQRCQSGTVR TNCLDCLDRT NSVQAFLGLE MLAKQLEALG LAEKPQLVTR 

       430        440        450        460        470        480 
FQEVFRSMWS VNGDSISKIY AGTGALEGKA KLKDGARSVT RTIQNNFFDS SKQEAIDVLL 

       490        500        510        520        530        540 
LGNTLNSDLA DKARALLTTG SLRVSEQTLQ SASSKVLKSM CENFYKYSKP KKIRVCVGTW 

       550        560        570        580        590        600 
NVNGGKQFRS IAFKNQTLTD WLLDAPKLAG IQEFQDKRSK PTDIFAIGFE EMVELNAGNI 

       610        620        630        640        650        660 
VSASTTNQKL WAVELQKTIS RDNKYVLLAS EQLVGVCLFV FIRPQHAPFI RDVAVDTVKT 

       670        680        690        700        710        720 
GMGGATGNKG AVAIRMLFHT TSLCFVCSHF AAGQSQVKER NEDFIEIARK LSFPMGRMLF 

       730        740        750        760        770        780 
SHDYVFWCGD FNYRIDLPNE EVKELIRQQN WDSLIAGDQL INQKNAGQVF RGFLEGKVTF 

       790        800        810        820        830        840 
APTYKYDLFS DDYDTSEKCR TPAWTDRVLW RRRKWPFDRS AEDLDLLNAS FQDESKILYT 

       850        860        870        880        890        900 
WTPGTLLHYG RAELKTSDHR PVVALIDIDI FEVEAEERQN IYKEVIAVQG PPDGTVLVSI 

       910        920        930        940        950        960 
KSSLPENNFF DDALIDELLQ QFASFGEVIL IRFVEDKMWV TFLEGSSALN VLSLNGKELL 

       970        980        990       1000       1010       1020 
NRTITIALKS PDWIKNLEEE MSLEKISIAL PSSTSSTLLG EDAEVAADFD MEGDVDDYSA 

      1030       1040       1050       1060       1070       1080 
EVEELLPQHL QPSSSSGLGT SPSSSPRTSP CQSPTISEGP VPSLPIRPSR APSRTPGPPS 

      1090       1100       1110       1120       1130       1140 
AQSSPIDAQP ATPLPQKDPA QPLEPKRPPP PRPVAPPTRP APPQRPPPPS GARSPAPTRK 

      1150       1160       1170       1180       1190       1200 
EFGGIGAPPS PGVARREMEA PKSPGTTRKD NIGRSQPSPQ AGLAGPGPAG YSTARPTIPP 

      1210       1220       1230       1240       1250       1260 
RAGVISAPQS HARASAGRLT PESQSKTSET SKGSTFLPEP LKPQAAFPPQ SSLPPPAQRL 

      1270       1280       1290       1300       1310       1320 
QEPLVPVAAP MPQSGPQPNL ETPPQPPPRS RSSHSLPSEA SSQPQVKTNG ISDGKRESPL 

      1330       1340       1350       1360       1370       1380 
KIDPFEDLSF NLLAVSKAQL SVQTSPVPTP DPKRLIQLPS ATQSNVLSSV SCMPTMPPIP 

      1390       1400       1410       1420       1430       1440 
ARSQSQENMR SSPNPFITGL TRTNPFSDRT AAPGNPFRAK SEESEATSWF SKEEPVTISP 

      1450       1460       1470       1480       1490       1500 
FPSLQPLGHN KSRASSSLDG FKDSFDLQGQ STLKISNPKG WVTFEEEEDF GVKGKSKSAC 

      1510       1520       1530       1540       1550       1560 
SDLLGNQPSS FSGSNLTLND DWNKGTNVSF CVLPSRRPPP PPVPLLPPGT SPPVDPFTTL 

      1570 
ASKASPTLDF TER 

« Hide

Isoform 2 (Synaptojanin-145) [UniParc].

Checksum: 26F2B693F03D2617
Show »

FASTA1,311144,859
Isoform 3 [UniParc].

Checksum: F082833051AB7F69
Show »

FASTA1,295143,254
Isoform 4 [UniParc].

Checksum: 9B1ECB57B0D071C9
Show »

FASTA51958,068

References

« Hide 'large scale' references
[1]"Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15."
Haffner C., Takei K., Chen H., Ringstad N., Hudson A., Butler M.H., Salcini A.E., Di Fiore P.P., De Camilli P.
FEBS Lett. 419:175-180(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-295.
Tissue: Cerebellum.
[2]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 4).
Tissue: Placenta.
[6]"The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity."
Cestra G., Castagnoli L., Dente L., Minenkova O., Petrelli A., Migone N., Hoffmueller U., Schneider-Mergener J., Cesareni G.
J. Biol. Chem. 274:32001-32007(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AMPH; SH3GL1; SH3GL2 AND SH3GL3.
[7]"Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis."
Krendel M., Osterweil E.K., Mooseker M.S.
FEBS Lett. 581:644-650(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO1E.
[8]"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-830; THR-1220; SER-1551 AND SER-1565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-830, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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-1318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Solution structure of RNA binding domain in synaptojanin 1."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 894-971.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF009039 mRNA. Translation: AAC51921.1.
AF009040 mRNA. Translation: AAC51922.1.
AB020717 mRNA. Translation: BAA74933.2. Different initiation.
AP000275 Genomic DNA. No translation available.
AP000276 Genomic DNA. No translation available.
AP000277 Genomic DNA. No translation available.
AP000278 Genomic DNA. No translation available.
AP000279 Genomic DNA. No translation available.
BC098395 mRNA. Translation: AAH98395.1.
RefSeqNP_001153774.1. NM_001160302.1.
NP_001153778.1. NM_001160306.1.
NP_003886.3. NM_003895.3.
NP_982271.2. NM_203446.2.
UniGeneHs.473632.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W80X-ray1.90P1477-1488[»]
Q1458-1469[»]
2DNRNMR-A894-971[»]
2VJ0X-ray1.60P1477-1488[»]
ProteinModelPortalO43426.
SMRO43426. Positions 44-444, 527-870, 895-971.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114388. 13 interactions.
IntActO43426. 6 interactions.
MINTMINT-109209.
STRING9606.ENSP00000322234.

PTM databases

PhosphoSiteO43426.

Proteomic databases

PaxDbO43426.
PRIDEO43426.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322229; ENSP00000322234; ENSG00000159082. [O43426-1]
ENST00000357345; ENSP00000349903; ENSG00000159082. [O43426-4]
GeneID8867.
KEGGhsa:8867.
UCSCuc002yqf.2. human. [O43426-4]

Organism-specific databases

CTD8867.
GeneCardsGC21M033997.
HGNCHGNC:11503. SYNJ1.
HPAHPA011916.
MIM604297. gene.
neXtProtNX_O43426.
PharmGKBPA36285.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5411.
HOGENOMHOG000007937.
HOVERGENHBG079225.
InParanoidO43426.
KOK01099.
PhylomeDBO43426.

Enzyme and pathway databases

BioCycMetaCyc:HS08354-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO43426.
BgeeO43426.
CleanExHS_SYNJ1.
GenevestigatorO43426.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
3.60.10.10. 1 hit.
InterProIPR015047. DUF1866.
IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR002013. Syja_N.
[Graphical view]
PfamPF08952. DUF1866. 1 hit.
PF03372. Exo_endo_phos. 1 hit.
PF02383. Syja_N. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 2 hits.
PROSITEPS50102. RRM. 1 hit.
PS50275. SAC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43426.
GenomeRNAi8867.
NextBio33289.
PROO43426.
SOURCESearch...

Entry information

Entry nameSYNJ1_HUMAN
AccessionPrimary (citable) accession number: O43426
Secondary accession number(s): O43425, O94984, Q4KMR1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 142 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 21

Human chromosome 21: entries, gene names and cross-references to MIM