CAPR2_HUMAN - dbPTM
CAPR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAPR2_HUMAN
UniProt AC Q6IMN6
Protein Name Caprin-2
Gene Name CAPRIN2 {ECO:0000312|EMBL:AAI17673.1}
Organism Homo sapiens (Human).
Sequence Length 1127
Subcellular Localization Isoform 1: Cytoplasm.
Isoform 2: Mitochondrion. Cytoplasm. Expressed throughout the cytoplasm.
Isoform 5: Mitochondrion. Colocalizes with aggregated mitochondria.
Cell membrane
Peripheral membrane protein .
Protein Description Promotes phosphorylation of the Wnt coreceptor LRP6, leading to increased activity of the canonical Wnt signaling pathway. [PubMed: 18762581 Faciliates constitutive LRP6 phosphorylation by CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate cells for Wnt signaling]
Protein Sequence MEVQVSQASLGFELTSVEKSLREWSRLSREVIAWLCPSSPNFILNFPPPPSASSVSMVQLFSSPFGYQSPSGHSEEEREGNMKSAKPQVNHSQHGESQRALSPLQSTLSSAASPSQAYETYIENGLICLKHKIRNIEKKKLKLEDYKDRLKSGEHLNPDQLEAVEKYEEVLHNLEFAKELQKTFSGLSLDLLKAQKKAQRREHMLKLEAEKKKLRTILQVQYVLQNLTQEHVQKDFKGGLNGAVYLPSKELDYLIKFSKLTCPERNESLSVEDQMEQSSLYFWDLLEGSEKAVVGTTYKHLKDLLSKLLNSGYFESIPVPKNAKEKEVPLEEEMLIQSEKKTQLSKTESVKESESLMEFAQPEIQPQEFLNRRYMTEVDYSNKQGEEQPWEADYARKPNLPKRWDMLTEPDGQEKKQESFKSWEASGKHQEVSKPAVSLEQRKQDTSKLRSTLPEEQKKQEISKSKPSPSQWKQDTPKSKAGYVQEEQKKQETPKLWPVQLQKEQDPKKQTPKSWTPSMQSEQNTTKSWTTPMCEEQDSKQPETPKSWENNVESQKHSLTSQSQISPKSWGVATASLIPNDQLLPRKLNTEPKDVPKPVHQPVGSSSTLPKDPVLRKEKLQDLMTQIQGTCNFMQESVLDFDKPSSAIPTSQPPSATPGSPVASKEQNLSSQSDFLQEPLQATSSPVTCSSNACLVTTDQASSGSETEFMTSETPEAAIPPGKQPSSLASPNPPMAKGSEQGFQSPPASSSSVTINTAPFQAMQTVFNVNAPLPPRKEQEIKESPYSPGYNQSFTTASTQTPPQCQLPSIHVEQTVHSQETAANYHPDGTIQVSNGSLAFYPAQTNVFPRPTQPFVNSRGSVRGCTRGGRLITNSYRSPGGYKGFDTYRGLPSISNGNYSQLQFQAREYSGAPYSQRDNFQQCYKRGGTSGGPRANSRAGWSDSSQVSSPERDNETFNSGDSGQGDSRSMTPVDVPVTNPAATILPVHVYPLPQQMRVAFSAARTSNLAPGTLDQPIVFDLLLNNLGETFDLQLGRFNCPVNGTYVFIFHMLKLAVNVPLYVNLMKNEEVLVSAYANDGAPDHETASNHAILQLFQGDQIWLRLHRGAIYGSSWKYSTFSGYLLYQD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
16PhosphorylationSLGFELTSVEKSLRE
HHCCEEHHHHHHHHH		40.6924719451
20PhosphorylationELTSVEKSLREWSRL
EEHHHHHHHHHHHHH		21.1024719451
102PhosphorylationGESQRALSPLQSTLS
CHHHHHHHHHHHHHH		23.6829507054
106PhosphorylationRALSPLQSTLSSAAS
HHHHHHHHHHHHCCC		38.7122199227
107PhosphorylationALSPLQSTLSSAASP
HHHHHHHHHHHCCCH		20.0722199227
138AcetylationHKIRNIEKKKLKLED
HHHCCCHHHCCCHHH		51.9520167786
146PhosphorylationKKLKLEDYKDRLKSG
HCCCHHHHHHHHHCC		12.86-
185PhosphorylationKELQKTFSGLSLDLL
HHHHHHHCCCCHHHH		44.0223612710
248PhosphorylationNGAVYLPSKELDYLI
CCCEECCHHHHHHHH		35.8524719451
253PhosphorylationLPSKELDYLIKFSKL
CCHHHHHHHHHHHCC		23.97-
338O-linked_GlycosylationEEEMLIQSEKKTQLS
CHHHHHHHHHHHCCC		44.3730379171
394PhosphorylationEQPWEADYARKPNLP
CCCCCCCCCCCCCCC		18.49-
468O-linked_GlycosylationEISKSKPSPSQWKQD
HHHHCCCCHHHHCCC		40.7030379171
483PhosphorylationTPKSKAGYVQEEQKK
CCHHHHCCCCHHHHC		12.10-
511PhosphorylationEQDPKKQTPKSWTPS
CCCCCCCCCCCCCHH		41.3825404012
514PhosphorylationPKKQTPKSWTPSMQS
CCCCCCCCCCHHHCC		37.0729978859
516PhosphorylationKQTPKSWTPSMQSEQ
CCCCCCCCHHHCCCC		16.7525907765
518PhosphorylationTPKSWTPSMQSEQNT
CCCCCCHHHCCCCCC		23.2925907765
521PhosphorylationSWTPSMQSEQNTTKS
CCCHHHCCCCCCCCC		32.2925907765
525PhosphorylationSMQSEQNTTKSWTTP
HHCCCCCCCCCCCCC		34.9825907765
526PhosphorylationMQSEQNTTKSWTTPM
HCCCCCCCCCCCCCC		30.5425907765
528PhosphorylationSEQNTTKSWTTPMCE
CCCCCCCCCCCCCCC		27.8029978859
530PhosphorylationQNTTKSWTTPMCEEQ
CCCCCCCCCCCCCCC		28.2829978859
531PhosphorylationNTTKSWTTPMCEEQD
CCCCCCCCCCCCCCC		11.6329978859
539PhosphorylationPMCEEQDSKQPETPK
CCCCCCCCCCCCCCC		32.6529978859
547PhosphorylationKQPETPKSWENNVES
CCCCCCCHHHCCHHH		40.6022817900
554PhosphorylationSWENNVESQKHSLTS
HHHCCHHHHHHCCCC		40.0022817900
558PhosphorylationNVESQKHSLTSQSQI
CHHHHHHCCCCCCCC		40.1429396449
560PhosphorylationESQKHSLTSQSQISP
HHHHHCCCCCCCCCC		27.9529978859
561PhosphorylationSQKHSLTSQSQISPK
HHHHCCCCCCCCCCC		32.8829978859
563PhosphorylationKHSLTSQSQISPKSW
HHCCCCCCCCCCCHH		29.2829978859
566PhosphorylationLTSQSQISPKSWGVA
CCCCCCCCCCHHCEE		20.7325159151
655PhosphorylationIPTSQPPSATPGSPV
CCCCCCCCCCCCCCC		52.0025627689
657PhosphorylationTSQPPSATPGSPVAS
CCCCCCCCCCCCCCC		32.3025627689
660PhosphorylationPPSATPGSPVASKEQ
CCCCCCCCCCCCHHC		19.8725159151
739PhosphorylationNPPMAKGSEQGFQSP
CCCCCCCCCCCCCCC		26.4924275569
749PhosphorylationGFQSPPASSSSVTIN
CCCCCCCCCCCEEEE		36.2024275569
750PhosphorylationFQSPPASSSSVTINT
CCCCCCCCCCEEEEC		28.8324275569
751PhosphorylationQSPPASSSSVTINTA
CCCCCCCCCEEEECC		26.7424275569
752PhosphorylationSPPASSSSVTINTAP
CCCCCCCCEEEECCC		25.8124275569
877MethylationRLITNSYRSPGGYKG
EEECCCCCCCCCCCC		35.87-
882PhosphorylationSYRSPGGYKGFDTYR
CCCCCCCCCCCCCCC		17.5422817900
883AcetylationYRSPGGYKGFDTYRG
CCCCCCCCCCCCCCC		57.2711688351
887PhosphorylationGGYKGFDTYRGLPSI
CCCCCCCCCCCCCCC		16.9225954137
888PhosphorylationGYKGFDTYRGLPSIS
CCCCCCCCCCCCCCC		12.4325954137
889MethylationYKGFDTYRGLPSISN
CCCCCCCCCCCCCCC		42.12-
895PhosphorylationYRGLPSISNGNYSQL
CCCCCCCCCCCCCCE		42.9225954137
899PhosphorylationPSISNGNYSQLQFQA
CCCCCCCCCCEEEEE		10.1317360941
900PhosphorylationSISNGNYSQLQFQAR
CCCCCCCCCEEEEEE		28.5425954137
909PhosphorylationLQFQAREYSGAPYSQ
EEEEEECCCCCCCCC		13.57-
914PhosphorylationREYSGAPYSQRDNFQ
ECCCCCCCCCCCCHH		19.53-
915PhosphorylationEYSGAPYSQRDNFQQ
CCCCCCCCCCCCHHH		20.0625954137
924PhosphorylationRDNFQQCYKRGGTSG
CCCHHHHHHCCCCCC		10.2016094384
929PhosphorylationQCYKRGGTSGGPRAN
HHHHCCCCCCCCCCC		27.3322210691
930PhosphorylationCYKRGGTSGGPRANS
HHHCCCCCCCCCCCC		45.0622210691
948PhosphorylationWSDSSQVSSPERDNE
CCCCCCCCCCCCCCC		32.3227732954
949PhosphorylationSDSSQVSSPERDNET
CCCCCCCCCCCCCCC		31.7427732954
956PhosphorylationSPERDNETFNSGDSG
CCCCCCCCCCCCCCC		34.08-
959PhosphorylationRDNETFNSGDSGQGD
CCCCCCCCCCCCCCC		39.52-
962PhosphorylationETFNSGDSGQGDSRS
CCCCCCCCCCCCCCC		36.22-
967PhosphorylationGDSGQGDSRSMTPVD
CCCCCCCCCCCCCCC		32.83-
969PhosphorylationSGQGDSRSMTPVDVP
CCCCCCCCCCCCCCC		30.8428348404
971PhosphorylationQGDSRSMTPVDVPVT
CCCCCCCCCCCCCCC		22.7728348404
978O-linked_GlycosylationTPVDVPVTNPAATIL
CCCCCCCCCCCCEEE		29.4330379171
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CAPR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAPR2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CAPR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRP6_HUMANLRP6physical
18762581
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAPR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547; SER-554 ANDTHR-560, AND MASS SPECTROMETRY.
"Cloning and characterization of a gene expressed during terminaldifferentiation that encodes a novel inhibitor of growth.";
Aerbajinai W., Lee Y.T., Wojda U., Barr V.A., Miller J.L.;
J. Biol. Chem. 279:1916-1921(2004).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), FUNCTION, SUBCELLULARLOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-924, AND MASSSPECTROMETRY.
"Complete sequencing and characterization of 21,243 full-length humancDNAs.";
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).
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-776 (ISOFORM 1),NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-776 (ISOFORM 4), ANDVARIANT VAL-519.

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