Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Striated muscle preferentially expressed protein kinase

Gene

SPEG

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

Functioni

Isoform 3 may have a role in regulating the growth and differentiation of arterial smooth muscle cells.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1630ATPPROSITE-ProRule annotation1
Active sitei1719Proton acceptorBy similarity1
Binding sitei2995ATPPROSITE-ProRule annotation1
Active sitei3085Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1607 – 1615ATPPROSITE-ProRule annotation9
Nucleotide bindingi2972 – 2980ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • muscle cell differentiation Source: Ensembl
  • muscle organ development Source: ProtInc
  • negative regulation of cell proliferation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01059-MONOMER.
SignaLinkiQ15772.

Names & Taxonomyi

Protein namesi
Recommended name:
Striated muscle preferentially expressed protein kinase (EC:2.7.11.1)
Alternative name(s):
Aortic preferentially expressed protein 1
Short name:
APEG-1
Gene namesi
Name:SPEG
Synonyms:APEG1, KIAA1297
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:16901. SPEG.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Myopathy, centronuclear, 5 (CNM5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of centronuclear myopathy, a congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. CNM5 features include severe neonatal hypotonia with respiratory insufficiency, difficulty feeding, and delayed motor development. Some patients die in infancy, and some develop dilated cardiomyopathy.
See also OMIM:615959
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0718082757G → V in CNM5. 1 PublicationCorresponds to variant rs587777676dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10290.
MalaCardsiSPEG.
MIMi615959. phenotype.
OpenTargetsiENSG00000072195.
Orphaneti169186. Autosomal recessive centronuclear myopathy.
PharmGKBiPA142672598.

Polymorphism and mutation databases

BioMutaiSPEG.
DMDMi218512143.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000726661 – 3267Striated muscle preferentially expressed protein kinaseAdd BLAST3267

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei139PhosphoserineBy similarity1
Modified residuei364PhosphoserineBy similarity1
Modified residuei371PhosphoserineBy similarity1
Modified residuei375PhosphothreonineBy similarity1
Modified residuei378PhosphoserineBy similarity1
Modified residuei381PhosphoserineBy similarity1
Modified residuei419PhosphoserineBy similarity1
Modified residuei449PhosphothreonineBy similarity1
Modified residuei453PhosphoserineBy similarity1
Modified residuei488PhosphoserineCombined sources1
Modified residuei506PhosphoserineBy similarity1
Modified residuei526PhosphoserineBy similarity1
Modified residuei549PhosphoserineBy similarity1
Disulfide bondi989 ↔ 1041PROSITE-ProRule annotation
Modified residuei1128PhosphoserineBy similarity1
Modified residuei1172PhosphoserineBy similarity1
Modified residuei1988PhosphoserineBy similarity1
Modified residuei2014PhosphoserineBy similarity1
Modified residuei2015PhosphoserineBy similarity1
Modified residuei2037PhosphoserineBy similarity1
Modified residuei2055Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei2055Omega-N-methylarginine; alternateBy similarity1
Modified residuei2109PhosphoserineBy similarity1
Modified residuei2130PhosphoserineBy similarity1
Modified residuei2139Omega-N-methylarginineBy similarity1
Modified residuei2177PhosphoserineBy similarity1
Modified residuei2376PhosphoserineBy similarity1
Modified residuei2380PhosphothreonineBy similarity1
Modified residuei2410PhosphoserineBy similarity1
Modified residuei2414PhosphoserineBy similarity1
Modified residuei2438PhosphoserineBy similarity1
Modified residuei2439PhosphoserineBy similarity1
Modified residuei2444PhosphoserineBy similarity1
Modified residuei2448PhosphoserineBy similarity1
Modified residuei2521PhosphoserineBy similarity1
Modified residuei2524PhosphoserineBy similarity1
Modified residuei2559PhosphoserineBy similarity1
Disulfide bondi2605 ↔ 2657PROSITE-ProRule annotation
Modified residuei2771PhosphothreonineBy similarity1
Modified residuei2774PhosphoserineBy similarity1
Modified residuei2949PhosphoserineBy similarity1

Post-translational modificationi

May be autophosphorylated.

Keywords - PTMi

Disulfide bond, Methylation, Phosphoprotein

Proteomic databases

EPDiQ15772.
MaxQBiQ15772.
PaxDbiQ15772.
PeptideAtlasiQ15772.
PRIDEiQ15772.

PTM databases

iPTMnetiQ15772.
PhosphoSitePlusiQ15772.

Expressioni

Tissue specificityi

Isoform 1 is preferentially expressed in striated muscle. Non-kinase form such as isoform 3 is predominantly expressed in the aorta. Isoform 3 appears to be expressed only in highly differentiated ASMC in normal vessel walls and down-regulated in dedifferentiated ASMC in vivo. In response to vascular injuries ASMC dedifferentiate and change from a quiescent and contractile phenotype to a proliferative and synthetic phenotype. This proliferation of vascular smooth muscle cells is one of the most prominent features of atherosclerosis.2 Publications

Inductioni

Isoform 3 is quickly down-regulated in response to vascular injury, when ASMC cells change from a quiescent to a proliferative phenotype.1 Publication

Gene expression databases

BgeeiENSG00000072195.
CleanExiHS_SPEG.
ExpressionAtlasiQ15772. baseline and differential.
GenevisibleiQ15772. HS.

Organism-specific databases

HPAiHPA018904.

Interactioni

Subunit structurei

Interacts with MTM1. Isoform 3 is found as a monomer or homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRMT1Q998733EBI-1384196,EBI-78738

Protein-protein interaction databases

BioGridi115579. 5 interactors.
IntActiQ15772. 4 interactors.
STRINGi9606.ENSP00000311684.

Structurei

Secondary structure

13267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi867 – 873Combined sources7
Beta strandi878 – 881Combined sources4
Beta strandi886 – 896Combined sources11
Beta strandi899 – 904Combined sources6
Beta strandi915 – 919Combined sources5
Helixi921 – 923Combined sources3
Beta strandi924 – 931Combined sources8
Helixi934 – 936Combined sources3
Beta strandi938 – 946Combined sources9
Beta strandi949 – 960Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U2HX-ray0.96A864-960[»]
ProteinModelPortaliQ15772.
SMRiQ15772.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 124Ig-like 1Add BLAST82
Domaini722 – 810Ig-like 2Add BLAST89
Domaini869 – 958Ig-like 3Add BLAST90
Domaini963 – 1057Ig-like 4Add BLAST95
Domaini1064 – 1152Ig-like 5Add BLAST89
Domaini1188 – 1278Ig-like 6Add BLAST91
Domaini1285 – 1382Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST98
Domaini1384 – 1480Ig-like 7Add BLAST97
Domaini1485 – 1573Ig-like 8Add BLAST89
Domaini1601 – 1854Protein kinase 1PROSITE-ProRule annotationAdd BLAST254
Domaini2583 – 2673Ig-like 9Add BLAST91
Domaini2680 – 2774Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini2966 – 3218Protein kinase 2PROSITE-ProRule annotationAdd BLAST253

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi284 – 345Pro-richAdd BLAST62
Compositional biasi525 – 634Pro-richAdd BLAST110
Compositional biasi1919 – 1924Poly-Ser6
Compositional biasi1925 – 1931Poly-Glu7
Compositional biasi2175 – 2316Pro-richAdd BLAST142
Compositional biasi2339 – 2503Arg-richAdd BLAST165
Compositional biasi2786 – 2965Pro-richAdd BLAST180

Sequence similaritiesi

Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 2 protein kinase domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
KOG0613. Eukaryota.
ENOG410XQFD. LUCA.
GeneTreeiENSGT00760000118877.
HOVERGENiHBG083339.
InParanoidiQ15772.
KOiK08809.
OMAiQYRDVHR.
OrthoDBiEOG091G002S.
PhylomeDBiQ15772.
TreeFamiTF331962.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015726. Ser/Thr_kin_striated_muscle-sp.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR10489:SF728. PTHR10489:SF728. 6 hits.
PfamiPF07679. I-set. 9 hits.
PF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 8 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 4 (identifier: Q15772-5) [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
MQKARGTRGE DAGTRAPPSP GVPPKRAKVG AGGGAPVAVA GAPVFLRPLK
60 70 80 90 100
NAAVCAGSDV RLRVVVSGTP QPSLRWFRDG QLLPAPAPEP SCLWLRRCGA
110 120 130 140 150
QDAGVYSCMA QNERGRASCE AVLTVLEVGD SETAEDDISD VQGTQRLELR
160 170 180 190 200
DDGAFSTPTG GSDTLVGTSL DTPPTSVTGT SEEQVSWWGS GQTVLEQEAG
210 220 230 240 250
SGGGTRRLPG SPRQAQATGA GPRHLGVEPL VRASRANLVG ASWGSEDSLS
260 270 280 290 300
VASDLYGSAF SLYRGRALSI HVSVPQSGLR REEPDLQPQL ASEAPRRPAQ
310 320 330 340 350
PPPSKSALLP PPSPRVGKRS PPGPPAQPAA TPTSPHRRTQ EPVLPEDTTT
360 370 380 390 400
EEKRGKKSKS SGPSLAGTAE SRPQTPLSEA SGRLSALGRS PRLVRAGSRI
410 420 430 440 450
LDKLQFFEER RRSLERSDSP PAPLRPWVPL RKARSLEQPK SERGAPWGTP
460 470 480 490 500
GASQEELRAP GSVAERRRLF QQKAASLDER TRQRSPASDL ELRFAQELGR
510 520 530 540 550
IRRSTSREEL VRSHESLRAT LQRAPSPREP GEPPLFSRPS TPKTSRAVSP
560 570 580 590 600
AAAQPPSPSS AEKPGDEPGR PRSRGPAGRT EPGEGPQQEV RRRDQFPLTR
610 620 630 640 650
SRAIQECRSP VPPPAADPPE ARTKAPPGRK REPPAQAVRF LPWATPGLEG
660 670 680 690 700
AAVPQTLEKN RAGPEAEKRL RRGPEEDGPW GPWDRRGARS QGKGRRARPT
710 720 730 740 750
SPELESSDDS YVSAGEEPLE APVFEIPLQN VVVAPGADVL LKCIITANPP
760 770 780 790 800
PQVSWHKDGS ALRSEGRLLL RAEGERHTLL LREARAADAG SYMATATNEL
810 820 830 840 850
GQATCAASLT VRPGGSTSPF SSPITSDEEY LSPPEEFPEP GETWPRTPTM
860 870 880 890 900
KPSPSQNRRS SDTGSKAPPT FKVSLMDQSV REGQDVIMSI RVQGEPKPVV
910 920 930 940 950
SWLRNRQPVR PDQRRFAEEA EGGLCRLRIL AAERGDAGFY TCKAVNEYGA
960 970 980 990 1000
RQCEARLEVR AHPESRSLAV LAPLQDVDVG AGEMALFECL VAGPTDVEVD
1010 1020 1030 1040 1050
WLCRGRLLQP ALLKCKMHFD GRKCKLLLTS VHEDDSGVYT CKLSTAKDEL
1060 1070 1080 1090 1100
TCSARLTVRP SLAPLFTRLL EDVEVLEGRA ARFDCKISGT PPPVVTWTHF
1110 1120 1130 1140 1150
GCPMEESENL RLRQDGGLHS LHIAHVGSED EGLYAVSAVN THGQAHCSAQ
1160 1170 1180 1190 1200
LYVEEPRTAA SGPSSKLEKM PSIPEEPEQG ELERLSIPDF LRPLQDLEVG
1210 1220 1230 1240 1250
LAKEAMLECQ VTGLPYPTIS WFHNGHRIQS SDDRRMTQYR DVHRLVFPAV
1260 1270 1280 1290 1300
GPQHAGVYKS VIANKLGKAA CYAHLYVTDV VPGPPDGAPQ VVAVTGRMVT
1310 1320 1330 1340 1350
LTWNPPRSLD MAIDPDSLTY TVQHQVLGSD QWTALVTGLR EPGWAATGLR
1360 1370 1380 1390 1400
KGVQHIFRVL STTVKSSSKP SPPSEPVQLL EHGPTLEEAP AMLDKPDIVY
1410 1420 1430 1440 1450
VVEGQPASVT VTFNHVEAQV VWRSCRGALL EARAGVYELS QPDDDQYCLR
1460 1470 1480 1490 1500
ICRVSRRDMG ALTCTARNRH GTQTCSVTLE LAEAPRFESI MEDVEVGAGE
1510 1520 1530 1540 1550
TARFAVVVEG KPLPDIMWYK DEVLLTESSH VSFVYEENEC SLVVLSTGAQ
1560 1570 1580 1590 1600
DGGVYTCTAQ NLAGEVSCKA ELAVHSAQTA MEVEGVGEDE DHRGRRLSDF
1610 1620 1630 1640 1650
YDIHQEIGRG AFSYLRRIVE RSSGLEFAAK FIPSQAKPKA SARREARLLA
1660 1670 1680 1690 1700
RLQHDCVLYF HEAFERRRGL VIVTELCTEE LLERIARKPT VCESEIRAYM
1710 1720 1730 1740 1750
RQVLEGIHYL HQSHVLHLDV KPENLLVWDG AAGEQQVRIC DFGNAQELTP
1760 1770 1780 1790 1800
GEPQYCQYGT PEFVAPEIVN QSPVSGVTDI WPVGVVAFLC LTGISPFVGE
1810 1820 1830 1840 1850
NDRTTLMNIR NYNVAFEETT FLSLSREARG FLIKVLVQDR LRPTAEETLE
1860 1870 1880 1890 1900
HPWFKTQAKG AEVSTDHLKL FLSRRRWQRS QISYKCHLVL RPIPELLRAP
1910 1920 1930 1940 1950
PERVWVTMPR RPPPSGGLSS SSDSEEEELE ELPSVPRPLQ PEFSGSRVSL
1960 1970 1980 1990 2000
TDIPTEDEAL GTPETGAATP MDWQEQGRAP SQDQEAPSPE ALPSPGQEPA
2010 2020 2030 2040 2050
AGASPRRGEL RRGSSAESAL PRAGPRELGR GLHKAASVEL PQRRSPSPGA
2060 2070 2080 2090 2100
TRLARGGLGE GEYAQRLQAL RQRLLRGGPE DGKVSGLRGP LLESLGGRAR
2110 2120 2130 2140 2150
DPRMARAASS EAAPHHQPPL ENRGLQKSSS FSQGEAEPRG RHRRAGAPLE
2160 2170 2180 2190 2200
IPVARLGARR LQESPSLSAL SEAQPSSPAR PSAPKPSTPK SAEPSATTPS
2210 2220 2230 2240 2250
DAPQPPAPQP AQDKAPEPRP EPVRASKPAP PPQALQTLAL PLTPYAQIIQ
2260 2270 2280 2290 2300
SLQLSGHAQG PSQGPAAPPS EPKPHAAVFA RVASPPPGAP EKRVPSAGGP
2310 2320 2330 2340 2350
PVLAEKARVP TVPPRPGSSL SSSIENLESE AVFEAKFKRS RESPLSLGLR
2360 2370 2380 2390 2400
LLSRSRSEER GPFRGAEEED GIYRPSPAGT PLELVRRPER SRSVQDLRAV
2410 2420 2430 2440 2450
GEPGLVRRLS LSLSQRLRRT PPAQRHPAWE ARGGDGESSE GGSSARGSPV
2460 2470 2480 2490 2500
LAMRRRLSFT LERLSSRLQR SGSSEDSGGA SGRSTPLFGR LRRATSEGES
2510 2520 2530 2540 2550
LRRLGLPHNQ LAAQAGATTP SAESLGSEAS ATSGSSAPGE SRSRLRWGFS
2560 2570 2580 2590 2600
RPRKDKGLSP PNLSASVQEE LGHQYVRSES DFPPVFHIKL KDQVLLEGEA
2610 2620 2630 2640 2650
ATLLCLPAAC PAPHISWMKD KKSLRSEPSV IIVSCKDGRQ LLSIPRAGKR
2660 2670 2680 2690 2700
HAGLYECSAT NVLGSITSSC TVAVARVPGK LAPPEVPQTY QDTALVLWKP
2710 2720 2730 2740 2750
GDSRAPCTYT LERRVDGESV WHPVSSGIPD CYYNVTHLPV GVTVRFRVAC
2760 2770 2780 2790 2800
ANRAGQGPFS NSSEKVFVRG TQDSSAVPSA AHQEAPVTSR PARARPPDSP
2810 2820 2830 2840 2850
TSLAPPLAPA APTPPSVTVS PSSPPTPPSQ ALSSLKAVGP PPQTPPRRHR
2860 2870 2880 2890 2900
GLQAARPAEP TLPSTHVTPS EPKPFVLDTG TPIPASTPQG VKPVSSSTPV
2910 2920 2930 2940 2950
YVVTSFVSAP PAPEPPAPEP PPEPTKVTVQ SLSPAKEVVS SPGSSPRSSP
2960 2970 2980 2990 3000
RPEGTTLRQG PPQKPYTFLE EKARGRFGVV RACRENATGR TFVAKIVPYA
3010 3020 3030 3040 3050
AEGKRRVLQE YEVLRTLHHE RIMSLHEAYI TPRYLVLIAE SCGNRELLCG
3060 3070 3080 3090 3100
LSDRFRYSED DVATYMVQLL QGLDYLHGHH VLHLDIKPDN LLLAPDNALK
3110 3120 3130 3140 3150
IVDFGSAQPY NPQALRPLGH RTGTLEFMAP EMVKGEPIGS ATDIWGAGVL
3160 3170 3180 3190 3200
TYIMLSGRSP FYEPDPQETE ARIVGGRFDA FQLYPNTSQS ATLFLRKVLS
3210 3220 3230 3240 3250
VHPWSRPSLQ DCLAHPWLQD AYLMKLRRQT LTFTTNRLKE FLGEQRRRRA
3260
EAATRHKVLL RSYPGGP
Note: No experimental confirmation available.
Length:3,267
Mass (Da):354,289
Last modified:December 16, 2008 - v4
Checksum:iE67BEB5624144233
GO
Isoform 2 (identifier: Q15772-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-792: Missing.
     961-962: AH → GE
     963-3267: Missing.

Note: No experimental confirmation available.
Show »
Length:170
Mass (Da):18,673
Checksum:i275949922564F798
GO
Isoform 3 (identifier: Q15772-4) [UniParc]FASTAAdd to basket
Also known as: APEG1

The sequence of this isoform differs from the canonical sequence as follows:
     1-849: Missing.
     961-962: AH → GE
     963-3267: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:113
Mass (Da):12,692
Checksum:i04F367263A1397C5
GO
Isoform 1 (identifier: Q15772-1) [UniParc]FASTAAdd to basket
Also known as: SPEG

The sequence of this isoform differs from the canonical sequence as follows:
     3209-3267: LQDCLAHPWLQDAYLMKLRRQTLTFTTNRLKEFLGEQRRRRAEAATRHKVLLRSYPGGP → SCLSVCHKEIKMASS

Note: Produced by alternative splicing.
Show »
Length:3,223
Mass (Da):348,903
Checksum:iFBF1188F9F1B883A
GO

Sequence cautioni

The sequence AAY15052 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence ABD61734 differs from that shown. Reason: Frameshift at positions 31 and 35.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71Q → H in ABD61734 (PubMed:16545539).Curated1
Sequence conflicti73S → I in ABD61734 (PubMed:16545539).Curated1
Sequence conflicti2047S → G in AAT80901 (PubMed:15185077).Curated1
Sequence conflicti2047S → G in BAA92535 (PubMed:10718198).Curated1
Sequence conflicti3005R → P in AAT80901 (PubMed:15185077).Curated1
Sequence conflicti3005R → P in BAA92535 (PubMed:10718198).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041101206R → H.1 PublicationCorresponds to variant rs55821435dbSNPEnsembl.1
Natural variantiVAR_041102934R → C.1 PublicationCorresponds to variant rs34398769dbSNPEnsembl.1
Natural variantiVAR_041103966R → Q.1 PublicationCorresponds to variant rs34861443dbSNPEnsembl.1
Natural variantiVAR_0411041103P → L.1 PublicationCorresponds to variant rs56334571dbSNPEnsembl.1
Natural variantiVAR_0411051135A → V.1 PublicationCorresponds to variant rs55670811dbSNPEnsembl.1
Natural variantiVAR_0411061178E → D in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0411071234R → W.1 PublicationCorresponds to variant rs55916864dbSNPEnsembl.1
Natural variantiVAR_0411081340R → Q.1 PublicationCorresponds to variant rs34994343dbSNPEnsembl.1
Natural variantiVAR_0411091621R → C.1 PublicationCorresponds to variant rs55646900dbSNPEnsembl.1
Natural variantiVAR_0411101903R → W in an ovarian mucinous carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs762000831dbSNPEnsembl.1
Natural variantiVAR_0597692189P → L.Corresponds to variant rs10755037dbSNPEnsembl.1
Natural variantiVAR_0411112687P → T.3 PublicationsCorresponds to variant rs13026308dbSNPEnsembl.1
Natural variantiVAR_0411122742V → M in a gastric adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs566841339dbSNPEnsembl.1
Natural variantiVAR_0718082757G → V in CNM5. 1 PublicationCorresponds to variant rs587777676dbSNPEnsembl.1
Natural variantiVAR_0411133079H → R.1 PublicationCorresponds to variant rs12464085dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0182581 – 849Missing in isoform 3. 3 PublicationsAdd BLAST849
Alternative sequenceiVSP_0182591 – 792Missing in isoform 2. 1 PublicationAdd BLAST792
Alternative sequenceiVSP_018261961 – 962AH → GE in isoform 2 and isoform 3. 4 Publications2
Alternative sequenceiVSP_018262963 – 3267Missing in isoform 2 and isoform 3. 4 PublicationsAdd BLAST2305
Alternative sequenceiVSP_0360713209 – 3267LQDCL…YPGGP → SCLSVCHKEIKMASS in isoform 1. 3 PublicationsAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57099 mRNA. Translation: AAC50599.1.
AK126500 mRNA. Translation: BAC86568.1.
AK289531 mRNA. Translation: BAF82220.1.
CR542201 mRNA. Translation: CAG46998.1.
AC053503 Genomic DNA. Translation: AAY15052.1. Sequence problems.
CH471063 Genomic DNA. Translation: EAW70747.1.
BC006346 mRNA. Translation: AAH06346.1.
DQ395348 mRNA. Translation: ABD61734.1. Frameshift.
AY603755 mRNA. Translation: AAT80901.1.
AB037718 mRNA. Translation: BAA92535.1.
CCDSiCCDS42824.1. [Q15772-5]
CCDS54432.1. [Q15772-4]
RefSeqiNP_001166947.1. NM_001173476.1. [Q15772-4]
NP_005867.3. NM_005876.4. [Q15772-5]
XP_016858651.1. XM_017003162.1. [Q15772-3]
UniGeneiHs.21639.

Genome annotation databases

EnsembliENST00000312358; ENSP00000311684; ENSG00000072195. [Q15772-5]
ENST00000396686; ENSP00000379917; ENSG00000072195. [Q15772-4]
ENST00000396688; ENSP00000379919; ENSG00000072195. [Q15772-4]
ENST00000396689; ENSP00000379920; ENSG00000072195. [Q15772-4]
GeneIDi10290.
KEGGihsa:10290.
UCSCiuc002vlq.4. human. [Q15772-5]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57099 mRNA. Translation: AAC50599.1.
AK126500 mRNA. Translation: BAC86568.1.
AK289531 mRNA. Translation: BAF82220.1.
CR542201 mRNA. Translation: CAG46998.1.
AC053503 Genomic DNA. Translation: AAY15052.1. Sequence problems.
CH471063 Genomic DNA. Translation: EAW70747.1.
BC006346 mRNA. Translation: AAH06346.1.
DQ395348 mRNA. Translation: ABD61734.1. Frameshift.
AY603755 mRNA. Translation: AAT80901.1.
AB037718 mRNA. Translation: BAA92535.1.
CCDSiCCDS42824.1. [Q15772-5]
CCDS54432.1. [Q15772-4]
RefSeqiNP_001166947.1. NM_001173476.1. [Q15772-4]
NP_005867.3. NM_005876.4. [Q15772-5]
XP_016858651.1. XM_017003162.1. [Q15772-3]
UniGeneiHs.21639.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U2HX-ray0.96A864-960[»]
ProteinModelPortaliQ15772.
SMRiQ15772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115579. 5 interactors.
IntActiQ15772. 4 interactors.
STRINGi9606.ENSP00000311684.

PTM databases

iPTMnetiQ15772.
PhosphoSitePlusiQ15772.

Polymorphism and mutation databases

BioMutaiSPEG.
DMDMi218512143.

Proteomic databases

EPDiQ15772.
MaxQBiQ15772.
PaxDbiQ15772.
PeptideAtlasiQ15772.
PRIDEiQ15772.

Protocols and materials databases

DNASUi10290.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312358; ENSP00000311684; ENSG00000072195. [Q15772-5]
ENST00000396686; ENSP00000379917; ENSG00000072195. [Q15772-4]
ENST00000396688; ENSP00000379919; ENSG00000072195. [Q15772-4]
ENST00000396689; ENSP00000379920; ENSG00000072195. [Q15772-4]
GeneIDi10290.
KEGGihsa:10290.
UCSCiuc002vlq.4. human. [Q15772-5]

Organism-specific databases

CTDi10290.
DisGeNETi10290.
GeneCardsiSPEG.
H-InvDBHIX0002864.
HGNCiHGNC:16901. SPEG.
HPAiHPA018904.
MalaCardsiSPEG.
MIMi615950. gene.
615959. phenotype.
neXtProtiNX_Q15772.
OpenTargetsiENSG00000072195.
Orphaneti169186. Autosomal recessive centronuclear myopathy.
PharmGKBiPA142672598.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
KOG0613. Eukaryota.
ENOG410XQFD. LUCA.
GeneTreeiENSGT00760000118877.
HOVERGENiHBG083339.
InParanoidiQ15772.
KOiK08809.
OMAiQYRDVHR.
OrthoDBiEOG091G002S.
PhylomeDBiQ15772.
TreeFamiTF331962.

Enzyme and pathway databases

BioCyciZFISH:HS01059-MONOMER.
SignaLinkiQ15772.

Miscellaneous databases

ChiTaRSiSPEG. human.
EvolutionaryTraceiQ15772.
GeneWikiiSPEG.
GenomeRNAii10290.
PROiQ15772.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000072195.
CleanExiHS_SPEG.
ExpressionAtlasiQ15772. baseline and differential.
GenevisibleiQ15772. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015726. Ser/Thr_kin_striated_muscle-sp.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR10489:SF728. PTHR10489:SF728. 6 hits.
PfamiPF07679. I-set. 9 hits.
PF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 8 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPEG_HUMAN
AccessioniPrimary (citable) accession number: Q15772
Secondary accession number(s): A8K0G6
, A8MRU0, Q27J74, Q695L1, Q6FGA6, Q6ZQW1, Q6ZTL8, Q9P2P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 16, 2008
Last modified: November 30, 2016
This is version 159 of the entry and version 4 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

Miscellaneous

Expression is under the tight control of the locus control region (LCRs).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.