CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017151
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Abnormal spindle-like microcephaly-associated protein 
Protein Synonyms/Alias
 Abnormal spindle protein homolog; Asp homolog 
Gene Name
 ASPM 
Gene Synonyms/Alias
 MCPH5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
156SLWDTIKKKKISASTubiquitination[1]
177SNIQNVNKTFSVSQKubiquitination[1, 2, 3, 4, 5, 6, 7]
184KTFSVSQKVDRVRSPubiquitination[1, 4, 5]
274SKVSFNEKAVTETSFubiquitination[1, 4]
373LSPDSFIKDNYGLNQubiquitination[4]
445IPECQGSKSPKAIFEubiquitination[1]
466SNYYSFIKQNNPKFSubiquitination[1, 7]
485ISSHSHNKQPKRRPIubiquitination[1, 7]
514ENQTEINKPKAKRCLubiquitination[1]
530SAVGEHEKVINNQKEubiquitination[1]
536EKVINNQKEKEDFHSubiquitination[1]
538VINNQKEKEDFHSYLubiquitination[1]
554IIDPILSKSKSYKNEubiquitination[1, 4]
556DPILSKSKSYKNEVTubiquitination[1]
559LSKSKSYKNEVTPSSubiquitination[1, 7]
626NVTTPISKRISNREKubiquitination[1]
639EKLNLKKKTDLSIFRubiquitination[1]
687HPMPFAAKNMFYDERubiquitination[1, 4]
739LGIENQHKISVPRAPubiquitination[1, 4]
748SVPRAPTKEEMSLRAubiquitination[1, 7]
777CRLFTSEKMVKAIKKubiquitination[1]
804RKDRHLWKDVGERQKubiquitination[1]
915HDPCLFCKDAEFKASubiquitination[1]
920FCKDAEFKASKEILLubiquitination[3]
923DAEFKASKEILLAFSubiquitination[1]
994QNWDLSKKLRIPAISubiquitination[1]
1017DIVLQVLKSRGIELSubiquitination[1]
1081KHTKSIKKTISLLSCubiquitination[1]
1097SDDLINKKKGKRDSGubiquitination[1]
1215ELLENEKKNFHLVRSubiquitination[1]
1334RRVLAQRKLLMLKKEubiquitination[1]
1349KLEKVQNKAASLIQGubiquitination[1, 2, 4, 6, 8]
1421QQRYEMLKSSTLIIQubiquitination[4]
1444RKMQSQVKATVILQRubiquitination[3]
1505FRCFQAQKLYKRRKEubiquitination[4]
1511QKLYKRRKESILTIQubiquitination[1]
1519ESILTIQKYYKAYLKubiquitination[2, 6]
1522LTIQKYYKAYLKGKIubiquitination[1]
1537ERTNYLQKRAAAIQLubiquitination[1, 3]
1552QAAFRRLKAHNLCRQubiquitination[1, 4]
1679KKEFLSLKNATIKLQubiquitination[3]
1684SLKNATIKLQSTVKMubiquitination[4]
1690IKLQSTVKMKQTRKQubiquitination[1, 3]
1696VKMKQTRKQYLHLRAubiquitination[1]
1802RKNFLQVKKAATCLQubiquitination[1]
1803KNFLQVKKAATCLQAubiquitination[1]
1822YKVRQLIKQQSIAALubiquitination[1]
1830QQSIAALKIQSAFRGubiquitination[1, 2, 4, 6]
1843RGYNKRVKYQSVLQSubiquitination[2, 4, 6]
1862QRWYRAYKTLHDTRTubiquitination[1]
1875RTHFLKTKAAVISLQubiquitination[1]
1903REHQAALKIQSAFRMubiquitination[1]
1912QSAFRMAKAQKQFRLacetylation[9]
1915FRMAKAQKQFRLFKTacetylation[9]
1921QKQFRLFKTAALVIQubiquitination[4]
1939RAWTAGRKQCMEYIEubiquitination[1]
1959LVLQSMWKGKTLRRQubiquitination[1, 4]
1995KKWKIMKKAALLIQKubiquitination[1]
2002KAALLIQKYYRAYSIubiquitination[1, 3, 4, 10]
2019EQNHLYLKTKAAVVTubiquitination[1, 3, 4]
2021NHLYLKTKAAVVTLQubiquitination[1]
2041MKVRKRIKDCNKAAVubiquitination[1]
2045KRIKDCNKAAVTIQSubiquitination[1, 4, 7]
2053AAVTIQSKYRAYKTKubiquitination[1, 3, 4, 8, 10]
2088KITNHQHKEYLNLKKubiquitination[1]
2094HKEYLNLKKTAIKIQubiquitination[1, 3]
2099NLKKTAIKIQSVYRGubiquitination[1]
2124HRAATFIKAMFKMHQubiquitination[1, 3, 4]
2157CRAYYQGKMQREKYLubiquitination[1, 3, 4]
2162QGKMQREKYLTILKAubiquitination[1]
2168EKYLTILKAVKVLQAubiquitination[1, 4]
2171LTILKAVKVLQASFRubiquitination[1, 4]
2188RVRRTLRKMQTAATLubiquitination[1, 7]
2227QQRYWAMKERNIQFQubiquitination[1]
2260KKARRHLKMMHIAATmethylation[11]
2287RRFLSLKKTAILIQRubiquitination[1]
2303YRAHLCTKHHLQFLQubiquitination[4]
2358HMRYQALKQASVVIQubiquitination[1, 3, 4, 7, 10]
2405MKTRRHLKSMHSSATubiquitination[1, 4]
2432RRFISLKKATIFVQRubiquitination[1]
2459YQFLHLRKAAITIQSubiquitination[7]
2581QKLQWATKIIQEKYRubiquitination[4]
2586ATKIIQEKYRANKKKubiquitination[1]
2595RANKKKQKVFQHNELubiquitination[1]
2603VFQHNELKKETCVQAubiquitination[1, 4]
2604FQHNELKKETCVQAGubiquitination[1]
2618GFQDMNIKKQIQEQHubiquitination[1, 4, 7]
2619FQDMNIKKQIQEQHQubiquitination[1, 4, 7]
2733VRVKTERKNFLAVQKubiquitination[1]
2740KNFLAVQKSVRTIQAubiquitination[1, 4]
2765LKNVSEEKMAAIVNQubiquitination[1, 4, 7]
2781ALCCYRSKTQYEAVQubiquitination[1, 4]
2799VMIQEWYKASGLACSubiquitination[4]
2823RAAVTIQKAFCRMVTubiquitination[1, 4, 7, 10]
2837TRKLETQKCAALRIQubiquitination[1, 4, 7]
2877FRTWQTRKQFLLYRKubiquitination[1, 4]
2884KQFLLYRKAAVVLQNubiquitination[1]
2900YRAFLSAKHQRQVYLubiquitination[4]
2933KRKFQEIKNSTIKIQubiquitination[1]
2960CKVKAACKIQAWYRCubiquitination[1]
3010SAIIIQRKWRAILPAubiquitination[3]
3018WRAILPAKIAHEHFLubiquitination[1, 3]
3028HEHFLMIKRHRAACLubiquitination[1]
3053RQVFLRQKSAALIIQubiquitination[1]
3061SAALIIQKYIRAREAubiquitination[1, 2, 6, 10]
3135YKLYLAVKNANKQVNubiquitination[1]
3139LAVKNANKQVNSVICubiquitination[1]
3163QEKRFIQKYHSIKKIubiquitination[1]
3169QKYHSIKKIEHEGQEubiquitination[1]
3190RAASVIQKAVRHFLLubiquitination[1]
3364PGNKVADKGGSIFTKubiquitination[1]
3404DRIYSLYKLTAHKHKubiquitination[1, 2, 6]
3422ERILYKQKKNSSISIubiquitination[1]
3423RILYKQKKNSSISIPubiquitination[1]
3446TRIVSRLKPDWVLRRubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [10] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [11] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
Functional Description
 Probable role in mitotic spindle regulation and coordination of mitotic processes. May have a preferential role in regulating neurogenesis. 
Sequence Annotation
 DOMAIN 920 1056 CH 1.
 DOMAIN 1110 1224 CH 2.
 DOMAIN 1347 1378 IQ 1.
 DOMAIN 1393 1422 IQ 2.
 DOMAIN 1582 1613 IQ 3.
 DOMAIN 1632 1661 IQ 4.
 DOMAIN 1655 1684 IQ 5.
 DOMAIN 1728 1757 IQ 6.
 DOMAIN 1751 1782 IQ 7.
 DOMAIN 1801 1830 IQ 8.
 DOMAIN 1824 1853 IQ 9.
 DOMAIN 1874 1903 IQ 10.
 DOMAIN 1897 1928 IQ 11.
 DOMAIN 1947 1978 IQ 12.
 DOMAIN 1970 2001 IQ 13.
 DOMAIN 2020 2049 IQ 14.
 DOMAIN 2043 2074 IQ 15.
 DOMAIN 2093 2124 IQ 16.
 DOMAIN 2116 2147 IQ 17.
 DOMAIN 2166 2197 IQ 18.
 DOMAIN 2189 2218 IQ 19.
 DOMAIN 2239 2270 IQ 20.
 DOMAIN 2262 2293 IQ 21.
 DOMAIN 2311 2342 IQ 22.
 DOMAIN 2334 2365 IQ 23.
 DOMAIN 2384 2415 IQ 24.
 DOMAIN 2407 2438 IQ 25.
 DOMAIN 2457 2488 IQ 26.
 DOMAIN 2530 2561 IQ 27.
 DOMAIN 2624 2653 IQ 28.
 DOMAIN 2665 2696 IQ 29.
 DOMAIN 2688 2719 IQ 30.
 DOMAIN 2738 2767 IQ 31.
 DOMAIN 2859 2890 IQ 32.
 DOMAIN 2909 2938 IQ 33.
 DOMAIN 2932 2963 IQ 34.
 DOMAIN 2954 2985 IQ 35.
 DOMAIN 3029 3060 IQ 36.
 DOMAIN 3079 3110 IQ 37.
 DOMAIN 3181 3210 IQ 38.
 DOMAIN 3204 3235 IQ 39.
 MOD_RES 280 280 Phosphoserine.
 MOD_RES 283 283 Phosphoserine.
 MOD_RES 367 367 Phosphoserine.
 MOD_RES 392 392 Phosphoserine.
 MOD_RES 425 425 Phosphoserine.
 MOD_RES 1103 1103 Phosphoserine.  
Keyword
 Alternative splicing; Calmodulin-binding; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Primary microcephaly; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3477 AA 
Protein Sequence
MANRRVGRGC WEVSPTERRP PAGLRGPAAE EEASSPPVLS LSHFCRSPFL CFGDVLLGAS 60
RTLSLALDNP NEEVAEVKIS HFPAADLGFS VSQRCFVLQP KEKIVISVNW TPLKEGRVRE 120
IMTFLVNDVL KHQAILLGNA EEQKKKKRSL WDTIKKKKIS ASTSHNRRVS NIQNVNKTFS 180
VSQKVDRVRS PLQACENLAM NEGGPPTENN SLILEENKIP ISPISPAFNE CHGATCLPLS 240
VRRSTTYSSL HASENRELLN VHSANVSKVS FNEKAVTETS FNSVNVNGQR GENSKLSLTP 300
NCSSTLNITQ SQIHFLSPDS FVNNSHGANN ELELVTCLSS DMFMKDNSQP VHLESTIAHE 360
IYQKILSPDS FIKDNYGLNQ DLESESVNPI LSPNQFLKDN MAYMCTSQQT CKVPLSNENS 420
QVPQSPEDWR KSEVSPRIPE CQGSKSPKAI FEELVEMKSN YYSFIKQNNP KFSAVQDISS 480
HSHNKQPKRR PILSATVTKR KATCTRENQT EINKPKAKRC LNSAVGEHEK VINNQKEKED 540
FHSYLPIIDP ILSKSKSYKN EVTPSSTTAS VARKRKSDGS MEDANVRVAI TEHTEVREIK 600
RIHFSPSEPK TSAVKKTKNV TTPISKRISN REKLNLKKKT DLSIFRTPIS KTNKRTKPII 660
AVAQSSLTFI KPLKTDIPRH PMPFAAKNMF YDERWKEKQE QGFTWWLNFI LTPDDFTVKT 720
NISEVNAATL LLGIENQHKI SVPRAPTKEE MSLRAYTARC RLNRLRRAAC RLFTSEKMVK 780
AIKKLEIEIE ARRLIVRKDR HLWKDVGERQ KVLNWLLSYN PLWLRIGLET TYGELISLED 840
NSDVTGLAMF ILNRLLWNPD IAAEYRHPTV PHLYRDGHEE ALSKFTLKKL LLLVCFLDYA 900
KISRLIDHDP CLFCKDAEFK ASKEILLAFS RDFLSGEGDL SRHLGLLGLP VNHVQTPFDE 960
FDFAVTNLAV DLQCGVRLVR TMELLTQNWD LSKKLRIPAI SRLQKMHNVD IVLQVLKSRG 1020
IELSDEHGNT ILSKDIVDRH REKTLRLLWK IAFAFQVDIS LNLDQLKEEI AFLKHTKSIK 1080
KTISLLSCHS DDLINKKKGK RDSGSFEQYS ENIKLLMDWV NAVCAFYNKK VENFTVSFSD 1140
GRVLCYLIHH YHPCYVPFDA ICQRTTQTVE CTQTGSVVLN SSSESDDSSL DMSLKAFDHE 1200
NTSELYKELL ENEKKNFHLV RSAVRDLGGI PAMINHSDMS NTIPDEKVVI TYLSFLCARL 1260
LDLRKEIRAA RLIQTTWRKY KLKTDLKRHQ EREKAARIIQ LAVINFLAKQ RLRKRVNAAL 1320
VIQKYWRRVL AQRKLLMLKK EKLEKVQNKA ASLIQGYWRR YSTRQRFLKL KYYSIILQSR 1380
IRMIIAVTSY KRYLWATVTI QRHWRAYLRR KQDQQRYEML KSSTLIIQSM FRKWKQRKMQ 1440
SQVKATVILQ RAFREWHLRK QAKEENSAII IQSWYRMHKE LRKYIYIRSC VVIIQKRFRC 1500
FQAQKLYKRR KESILTIQKY YKAYLKGKIE RTNYLQKRAA AIQLQAAFRR LKAHNLCRQI 1560
RAACVIQSYW RMRQDRVRFL NLKKTIIKFQ AHVRKHQQRQ KYKKMKKAAV IIQTHFRAYI 1620
FAMKVLASYQ KTRSAVIVLQ SAYRGMQARK MYIHILTSVI KIQSYYRAYV SKKEFLSLKN 1680
ATIKLQSTVK MKQTRKQYLH LRAAALFIQQ CYRSKKIAAQ KREEYMQMRE SCIKLQAFVR 1740
GYLVRKQMRL QRKAVISLQS YFRMRKARQY YLKMYKAIIV IQNYYHAYKA QVNQRKNFLQ 1800
VKKAATCLQA AYRGYKVRQL IKQQSIAALK IQSAFRGYNK RVKYQSVLQS IIKIQRWYRA 1860
YKTLHDTRTH FLKTKAAVIS LQSAYRGWKV RKQIRREHQA ALKIQSAFRM AKAQKQFRLF 1920
KTAALVIQQN FRAWTAGRKQ CMEYIELRHA VLVLQSMWKG KTLRRQLQRQ HKCAIIIQSY 1980
YRMHVQQKKW KIMKKAALLI QKYYRAYSIG REQNHLYLKT KAAVVTLQSA YRGMKVRKRI 2040
KDCNKAAVTI QSKYRAYKTK KKYATYRASA IIIQRWYRGI KITNHQHKEY LNLKKTAIKI 2100
QSVYRGIRVR RHIQHMHRAA TFIKAMFKMH QSRISYHTMR KAAIVIQVRC RAYYQGKMQR 2160
EKYLTILKAV KVLQASFRGV RVRRTLRKMQ TAATLIQSNY RRYRQQTYFN KLKKITKTVQ 2220
QRYWAMKERN IQFQRYNKLR HSVIYIQAIF RGKKARRHLK MMHIAATLIQ RRFRTLMMRR 2280
RFLSLKKTAI LIQRKYRAHL CTKHHLQFLQ VQNAVIKIQS SYRRWMIRKR MREMHRAATF 2340
IQSTFRMHRL HMRYQALKQA SVVIQQQYQA NRAAKLQRQH YLRQRHSAVI LQAAFRGMKT 2400
RRHLKSMHSS ATLIQSRFRS LLVRRRFISL KKATIFVQRK YRATICAKHK LYQFLHLRKA 2460
AITIQSSYRR LMVKKKLQEM QRAAVLIQAT FRMYRTYITF QTWKHASILI QQHYRTYRAA 2520
KLQRENYIRQ WHSAVVIQAA YKGMKARQLL REKHKASIVI QSTYRMYRQY CFYQKLQWAT 2580
KIIQEKYRAN KKKQKVFQHN ELKKETCVQA GFQDMNIKKQ IQEQHQAAII IQKHCKAFKI 2640
RKHYLHLRAT VVSIQRRYRK LTAVRTQAVI CIQSYYRGFK VRKDIQNMHR AATLIQSFYR 2700
MHRAKVDYET KKTAIVVIQN YYRLYVRVKT ERKNFLAVQK SVRTIQAAFR GMKVRQKLKN 2760
VSEEKMAAIV NQSALCCYRS KTQYEAVQSE GVMIQEWYKA SGLACSQEAE YHSQSRAAVT 2820
IQKAFCRMVT RKLETQKCAA LRIQFFLQMA VYRRRFVQQK RAAITLQHYF RTWQTRKQFL 2880
LYRKAAVVLQ NHYRAFLSAK HQRQVYLQIR SSVIIIQARS KGFIQKRKFQ EIKNSTIKIQ 2940
AMWRRYRAKK YLCKVKAACK IQAWYRCWRA HKEYLAILKA VKIIQGCFYT KLERTRFLNV 3000
RASAIIIQRK WRAILPAKIA HEHFLMIKRH RAACLIQAHY RGYKGRQVFL RQKSAALIIQ 3060
KYIRAREAGK HERIKYIEFK KSTVILQALV RGWLVRKRFL EQRAKIRLLH FTAAAYYHLN 3120
AVRIQRAYKL YLAVKNANKQ VNSVICIQRW FRARLQEKRF IQKYHSIKKI EHEGQECLSQ 3180
RNRAASVIQK AVRHFLLRKK QEKFTSGIIK IQALWRGYSW RKKNDCTKIK AIRLSLQVVN 3240
REIREENKLY KRTALALHYL LTYKHLSAIL EALKHLEVVT RLSPLCCENM AQSGAISKIF 3300
VLIRSCNRSI PCMEVIRYAV QVLLNVSKYE KTTSAVYDVE NCIDILLELL QIYREKPGNK 3360
VADKGGSIFT KTCCLLAILL KTTNRASDVR SRSKVVDRIY SLYKLTAHKH KMNTERILYK 3420
QKKNSSISIP FIPETPVRTR IVSRLKPDWV LRRDNMEEIT NPLQAIQMVM DTLGIPY 3477 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000922; C:spindle pole; IEA:Compara.
 GO:0048589; P:developmental growth; IEA:Compara.
 GO:0021873; P:forebrain neuroblast division; IEA:Compara.
 GO:0051661; P:maintenance of centrosome location; IEA:Compara.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0045769; P:negative regulation of asymmetric cell division; IEA:Compara.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0048477; P:oogenesis; IEA:Compara.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IEA:Compara.
 GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR022613; CAMSAP_CH.
 IPR001715; CH-domain.
 IPR000048; IQ_motif_EF-hand-BS.
 IPR027417; P-loop_NTPase. 
Pfam
 PF11971; CAMSAP_CH
 PF00612; IQ 
SMART
 SM00033; CH
 SM00015; IQ 
PROSITE
 PS50021; CH
 PS50096; IQ 
PRINTS