Q92797 (SYMPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Symplekin

Gene names

Name:	SYMPK
Synonyms:	SPK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1274 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cell junction › tight junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Nucleus › nucleoplasm. 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.

Ontologies

Keywords
Biological process	Cell adhesion mRNA processing
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus Tight junction
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW mRNA polyadenylation Inferred from mutant phenotype Ref.16. Source: UniProtKB positive regulation of protein dephosphorylation Inferred from direct assay Ref.16. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from direct assay Ref.5. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1274

1274

Symplekin

PRO_0000072385

Regions

Repeat

31 – 64

34

HEAT 1

Repeat

67 – 101

35

HEAT 2

Repeat

104 – 146

43

HEAT 3

Repeat

153 – 192

40

HEAT 4

Repeat

227 – 266

40

HEAT 5

Region

1 – 124

124

Interaction with HSF1

Motif

345 – 360

16

Nuclear localization signal Potential

Compositional bias

1168 – 1175

8

Poly-Ser

Amino acid modifications

Modified residue

494

1

Phosphoserine Ref.13

Modified residue

1243

1

Phosphoserine Ref.12 Ref.14

Modified residue

1257

1

Phosphothreonine Ref.12

Modified residue

1259

1

Phosphoserine Ref.12

Natural variations

Alternative sequence

637 – 672

36

GSLDK…VLEAP → PRLCWRRHSSQRVPWRWSAS TARMRVAPIWACPHFET in isoform 2.

VSP_014842

Alternative sequence

673 – 1274

602

Missing in isoform 2.

VSP_014843

Experimental info

Mutagenesis

185

1

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

Secondary structure

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1274

Helix Strand Turn

Details...

Helix

32 – 45

14

Helix

50 – 63

14

Helix

67 – 73

7

Helix

74 – 78

5

Helix

79 – 82

4

Helix

86 – 102

17

Helix

104 – 106

3

Helix

107 – 118

12

Helix

123 – 146

24

Helix

152 – 170

19

Helix

171 – 173

3

Helix

177 – 193

17

Helix

205 – 207

3

Helix

213 – 215

3

Beta strand

221 – 223

3

Helix

225 – 242

18

Helix

250 – 266

17

Helix

268 – 270

3

Helix

271 – 283

13

Helix

287 – 289

3

Helix

291 – 293

3

Helix

294 – 309

16

Helix

312 – 317

6

Helix

318 – 327

10

Helix

332 – 337

6

Helix

342 – 345

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: D8AD9ABB0B25A688	FASTA	1,274	141,148
	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
	Isoform 2 [UniParc]. Checksum: E5939FC7FFDAA3AA	FASTA	673	74,523
	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 LAAGASPRLC WRRHSSQRVP WRWSASTARM 670 RVAPIWACPH FET

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

IPI

IPI00023344.
IPI00413614.
IPI00556574.

RefSeq

NP_004810.2. NM_004819.2.

UniGene

Hs.515475.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3O2Q	X-ray	2.40	A/D	30-360	[»]
3O2S	X-ray	2.50	A	30-360	[»]
3O2T	X-ray	1.40	A	30-395	[»]
3ODR	X-ray	2.20	A	1-395	[»]
3ODS	X-ray	1.90	A	1-395	[»]
4H3H	X-ray	2.20	A/D	30-360	[»]
4H3K	X-ray	2.00	A/D	30-360	[»]

ProteinModelPortal

Q92797.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42506N.

MINT

MINT-1537611.

STRING

9606.ENSP00000245934.

PTM databases

PhosphoSite

Q92797.

Polymorphism databases

DMDM

71153180.

Proteomic databases

PaxDb

Q92797.

PRIDE

Q92797.

Protocols and materials databases

DNASU

8189.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000245934; ENSP00000245934; ENSG00000125755.

GeneID

8189.

KEGG

hsa:8189.

UCSC

uc002pdn.3. human.
uc002pdq.2. human.

Organism-specific databases

CTD

8189.

GeneCards

GC19M046318.

H-InvDB

HIX0015243.

HGNC

HGNC:22935. SYMPK.

HPA

HPA041756.

MIM

602388. gene.

neXtProt

NX_Q92797.

PharmGKB

PA134896920.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG273943.

HOGENOM

HOG000046745.

HOVERGEN

HBG062441.

InParanoid

Q92797.

KO

K06100.

OMA

EACKRDN.

OrthoDB

EOG4C2H8Q.

Gene expression databases

Bgee

Q92797.

CleanEx

HS_SYMPK.

Genevestigator

Q92797.

GermOnline

ENSG00000125755. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 3 hits.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021850. DUF3453.
IPR022075. Symplekin_C.
[Graphical view]

Pfam

PF11935. DUF3453. 1 hit.
PF12295. Symplekin_C. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50077. HEAT_REPEAT. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SYMPK. human.

EvolutionaryTrace

Q92797.

GenomeRNAi

8189.

NextBio

30878.

SOURCE

Search...

Entry information

Entry name

SYMPK_HUMAN

Accession

Primary (citable) accession number: Q92797
Secondary accession number(s): O00521 , O00689, O00733, Q59GT5, Q8N2U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.