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Q92797 (SYMPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Symplekin
Gene names
Name:SYMPK
Synonyms:SPK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1274 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity. Ref.10 Ref.16

Subunit structure

Found in a heat-sensitive complex at least composed of several cleavage and polyadenylation specific and cleavage stimulation factors. Interacts with CPSF2, CPSF3 and CSTF2. Interacts with HSF1 in heat-stressed cells. Interacts with SSU72. Ref.7 Ref.9 Ref.10 Ref.11 Ref.16 Ref.17

Subcellular location

Cytoplasmcytoskeleton. Cell junctiontight junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Nucleusnucleoplasm. Note: Cytoplasmic face of adhesion plaques (major) and nucleoplasm (minor) (in cells with TJ). Nucleoplasm (in cells without TJ). Nuclear bodies of heat-stressed cells. Ref.5 Ref.8 Ref.9

Tissue specificity

In testis, expressed in polar epithelia and Sertoli cells but not in vascular endothelia. The protein is detected in stomach, duodenum, pancreas, liver, fetal brain, carcinomas, lens-forming cells, fibroblasts, lymphocytes, lymphoma cells, erythroleukemia cells but not in endothelium of vessels, epidermis, intercalated disks, Purkinje fiber cells of the heart and lymph node. Ref.5

Domain

The HEAT repeats have been determined based on 3D-structure analysis of the D.melanogaster ortholog and are not detected by sequence-based prediction programs.

Miscellaneous

Could be used as a differentiation marker in the differential diagnosis of tumors.

Sequence similarities

Belongs to the Symplekin family.

Contains 5 HEAT repeats.

Sequence caution

The sequence AAC50667.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH30214.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAD92261.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA71861.1 differs from that shown. Reason: Frameshift at position 67.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CPSF2Q9P2I02EBI-1051992,EBI-1043224

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q92797-1)

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: Q92797-2)

The sequence of this isoform differs from the canonical sequence as follows:
     637-672: GSLDKYEDCLIRLLSGLQEKPDQKDGIFTKVVLEAP → PRLCWRRHSSQRVPWRWSASTARMRVAPIWACPHFET
     673-1274: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12741274Symplekin
PRO_0000072385

Regions

Repeat31 – 6434HEAT 1
Repeat67 – 10135HEAT 2
Repeat104 – 14643HEAT 3
Repeat153 – 19240HEAT 4
Repeat227 – 26640HEAT 5
Region1 – 124124Interaction with HSF1
Motif345 – 36016Nuclear localization signal Potential
Compositional bias1168 – 11758Poly-Ser

Amino acid modifications

Modified residue4941Phosphoserine Ref.13
Modified residue12431Phosphoserine Ref.12 Ref.14
Modified residue12571Phosphothreonine Ref.12
Modified residue12591Phosphoserine Ref.12

Natural variations

Alternative sequence637 – 67236GSLDK…VLEAP → PRLCWRRHSSQRVPWRWSAS TARMRVAPIWACPHFET in isoform 2.
VSP_014842
Alternative sequence673 – 1274602Missing in isoform 2.
VSP_014843

Experimental info

Mutagenesis1851K → A: Abolishes stimulation of SSU72 phosphatase activity. Ref.16

Secondary structure

.............................................. 1274
Helix Strand Turn

Details...

Sequences

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

Last modified July 19, 2005. Version 2.
Checksum: D8AD9ABB0B25A688

FASTA1,274141,148
        10         20         30         40         50         60 
MASGSGDSVT RRSVASQFFT QEEGPGIDGM TTSERVVDLL NQAALITNDS KITVLKQVQE 

        70         80         90        100        110        120 
LIINKDPTLL DNFLDEIIAF QADKSIEVRK FVIGFIEEAC KRDIELLLKL IANLNMLLRD 

       130        140        150        160        170        180 
ENVNVVKKAI LTMTQLYKVA LQWMVKSRVI SELQEACWDM VSAMAGDIIL LLDSDNDGIR 

       190        200        210        220        230        240 
THAIKFVEGL IVTLSPRMAD SEIPRRQEHD ISLDRIPRDH PYIQYNVLWE EGKAALEQLL 

       250        260        270        280        290        300 
KFMVHPAISS INLTTALGSL ANIARQRPMF MSEVIQAYET LHANLPPTLA KSQVSSVRKN 

       310        320        330        340        350        360 
LKLHLLSVLK HPASLEFQAQ ITTLLVDLGT PQAEIARNMP SSKDTRKRPR DDSDSTLKKM 

       370        380        390        400        410        420 
KLEPNLGEDD EDKDLEPGPS GTSKASAQIS GQSDTDITAE FLQPLLTPDN VANLVLISMV 

       430        440        450        460        470        480 
YLPEAMPASF QAIYTPVESA GTEAQIKHLA RLMATQMTAA GLGPGVEQTK QCKEEPKEEK 

       490        500        510        520        530        540 
VVKTESVLIK RRLSAQGQAI SVVGSLSSMS PLEEEAPQAK RRPEPIIPVT QPRLAGAGGR 

       550        560        570        580        590        600 
KKIFRLSDVL KPLTDAQVEA MKLGAVKRIL RAEKAVACSG AAQVRIKILA SLVTQFNSGL 

       610        620        630        640        650        660 
KAEVLSFILE DVRARLDLAF AWLYQEYNAY LAAGASGSLD KYEDCLIRLL SGLQEKPDQK 

       670        680        690        700        710        720 
DGIFTKVVLE APLITESALE VVRKYCEDES RTYLGMSTLR DLIFKRPSRQ FQYLHVLLDL 

       730        740        750        760        770        780 
SSHEKDKVRS QALLFIKRMY EKEQLREYVE KFALNYLQLL VHPNPPSVLF GADKDTEVAA 

       790        800        810        820        830        840 
PWTEETVKQC LYLYLALLPQ NHKLIHELAA VYTEAIADIK RTVLRVIEQP IRGMGMNSPE 

       850        860        870        880        890        900 
LLLLVENCPK GAETLVTRCL HSLTDKVPPS PELVKRVRDL YHKRLPDVRF LIPVLNGLEK 

       910        920        930        940        950        960 
KEVIQALPKL IKLNPIVVKE VFNRLLGTQH GEGNSALSPL NPGELLIALH NIDSVKCDMK 

       970        980        990       1000       1010       1020 
SIIKATNLCF AERNVYTSEV LAVVMQQLME QSPLPMLLMR TVIQSLTMYP RLGGFVMNIL 

      1030       1040       1050       1060       1070       1080 
SRLIMKQVWK YPKVWEGFIK CCQRTKPQSF QVILQLPPQQ LGAVFDKCPE LREPLLAHVR 

      1090       1100       1110       1120       1130       1140 
SFTPHQQAHI PNSIMTILEA SGKQEPEAKE APAGPLEEDD LEPLTLAPAP APRPPQDLIG 

      1150       1160       1170       1180       1190       1200 
LRLAQEKALK RQLEEEQKLK PGGVGAPSSS SPSPSPSARP GPPPSEEAMD FREEGPECET 

      1210       1220       1230       1240       1250       1260 
PGIFISMDDD SGLTEAALLD SSLEGPLPKE TAAGGLTLKE ERSPQTLAPV GEDAMKTPSP 

      1270 
AAEDAREPEA KGNS 

« Hide

Isoform 2 [UniParc].

Checksum: E5939FC7FFDAA3AA
Show »

FASTA67374,523

References

« Hide 'large scale' references
[1]"Six transcripts map within 200 kilobases of the myotonic dystrophy expanded repeat."
Alwazzan M., Hamshere M.G., Lennon G.G., Brook J.D.
Mamm. Genome 9:485-487(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Chromosomal localization to 19q13.3, partial genomic structure and 5' cDNA sequence of the human symplekin gene."
Ueki K., Ramaswamy S., Billings S.J., Mohrenweiser H.W., Louis D.N.
Somat. Cell Mol. Genet. 23:229-231(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-155 (ISOFORM 1).
[4]"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] OF 17-1274 (ISOFORM 1).
Tissue: Kidney and Lung.
[5]"Symplekin, a novel type of tight junction plaque protein."
Keon B.H., Schaefer S., Kuhn C., Grund C., Franke W.W.
J. Cell Biol. 134:1003-1018(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-1274 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Colon carcinoma.
[6]"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 426-533 (ISOFORM 1).
[7]"Complex protein interactions within the human polyadenylation machinery identify a novel component."
Takagaki Y., Manley J.L.
Mol. Cell. Biol. 20:1515-1525(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSTF2.
[8]"Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes."
Hofmann I., Schnoelzer M., Kaufmann I., Franke W.W.
Mol. Biol. Cell 13:1665-1676(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin."
Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D.
J. Biol. Chem. 279:10551-10555(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSF1, SUBCELLULAR LOCATION.
[10]"Symplekin and multiple other polyadenylation factors participate in 3'-end maturation of histone mRNAs."
Kolev N.G., Steitz J.A.
Genes Dev. 19:2583-2592(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A HEAT-SENSITIVE COMPLEX.
[11]"Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation."
Kolev N.G., Yario T.A., Benson E., Steitz J.A.
EMBO Rep. 9:1013-1018(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CPSF2 AND CPSF3.
[12]"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-1243; THR-1257 AND SER-1259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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-1243, 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]"Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex."
Xiang K., Nagaike T., Xiang S., Kilic T., Beh M.M., Manley J.L., Tong L.
Nature 467:729-733(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-395 IN COMPLEX WITH SSU72, FUNCTION, MUTAGENESIS OF LYS-185, INTERACTION WITH SSU72.
[17]"An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72."
Xiang K., Manley J.L., Tong L.
Genes Dev. 26:2265-2270(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-360 IN COMPLEX WITH SSU72, INTERACTION WITH SSU72.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10931 mRNA. Translation: CAA71861.1. Frameshift.
AB209024 mRNA. Translation: BAD92261.1. Different initiation.
U88726 mRNA. Translation: AAB58578.1.
BC006536 mRNA. Translation: AAH06536.2.
BC006567 mRNA. Translation: AAH06567.2.
BC030214 mRNA. Translation: AAH30214.1. Sequence problems.
U49240 mRNA. Translation: AAC50667.1. Different initiation.
DB328640 mRNA. No translation available.
RefSeqNP_004810.2. NM_004819.2.
XP_005259343.1. XM_005259286.1.
UniGeneHs.515475.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O2QX-ray2.40A/D30-360[»]
3O2SX-ray2.50A30-360[»]
3O2TX-ray1.40A30-395[»]
3ODRX-ray2.20A1-395[»]
3ODSX-ray1.90A1-395[»]
4H3HX-ray2.20A/D30-360[»]
4H3KX-ray2.00A/D30-360[»]
ProteinModelPortalQ92797.
SMRQ92797. Positions 30-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113833. 13 interactions.
DIPDIP-42506N.
IntActQ92797. 5 interactions.
MINTMINT-1537611.
STRING9606.ENSP00000245934.

PTM databases

PhosphoSiteQ92797.

Polymorphism databases

DMDM71153180.

Proteomic databases

PaxDbQ92797.
PRIDEQ92797.

Protocols and materials databases

DNASU8189.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245934; ENSP00000245934; ENSG00000125755. [Q92797-1]
GeneID8189.
KEGGhsa:8189.
UCSCuc002pdn.3. human. [Q92797-1]
uc002pdq.2. human. [Q92797-2]

Organism-specific databases

CTD8189.
GeneCardsGC19M046318.
H-InvDBHIX0015243.
HGNCHGNC:22935. SYMPK.
HPAHPA041756.
HPA055661.
MIM602388. gene.
neXtProtNX_Q92797.
PharmGKBPA134896920.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273943.
HOGENOMHOG000046745.
HOVERGENHBG062441.
InParanoidQ92797.
KOK06100.
OMAEACKRDN.
OrthoDBEOG7RZ5PC.
PhylomeDBQ92797.
TreeFamTF312860.

Gene expression databases

ArrayExpressQ92797.
BgeeQ92797.
CleanExHS_SYMPK.
GenevestigatorQ92797.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021850. Symplekin.
IPR022075. Symplekin_C.
[Graphical view]
PANTHERPTHR15245:SF7. PTHR15245:SF7. 1 hit.
PfamPF12295. Symplekin_C. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSSYMPK. human.
EvolutionaryTraceQ92797.
GeneWikiSYMPK.
GenomeRNAi8189.
NextBio30878.
PROQ92797.
SOURCESearch...

Entry information

Entry nameSYMPK_HUMAN
AccessionPrimary (citable) accession number: Q92797
Secondary accession number(s): O00521 expand/collapse secondary AC list , O00689, O00733, Q59GT5, Q8N2U5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 126 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 chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM