(data stored in ACNUC5448 zone)

HOGENOM: HS3_PE3715

ID   HS3_PE3715                           STANDARD;      PRT;   2986 AA.
AC   HS3_PE3715; O60229; A8MSI4; Q6ZN45; Q8TBQ5; Q9NSZ4; Q9Y2A5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Kalirin; EC=2.7.11 1;AltName: Full=Huntingtin-associated
DE   protein-interacting protein;AltName: Full=Protein Duo;AltName:
DE   Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology
DE   domain; (HS3.PE3715).
GN   Name=KALRN; Synonyms=DUET, DUO, HAPIP, TRAD;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS3.PE3715.
CC       Homo sapiens chromosome 3 GRCh37  sequence 1..197962430 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KALRN_HUMAN
CC   -!- FUNCTION: Promotes the exchange of GDP by GTP. Activates specific
CC       Rho GTPase family members, thereby inducing various signaling
CC       mechanisms that regulate neuronal shape, growth, and plasticity,
CC       through their effects on the actin cytoskeleton. Induces
CC       lamellipodia independent of its GEF activity.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha-
CC       amidating monooxygenase (PAM) and with the huntingtin-associated
CC       protein 1 (HAP1) (By similarity). Interacts with FASLG.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=Associated with the cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=6;
CC       Name=1;
CC         IsoId=O60229-1; Sequence=Displayed;
CC         Note=Produced by alternative splicing;
CC       Name=2;
CC         IsoId=O60229-2; Sequence=VSP_028910, VSP_028911;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=3;
CC         IsoId=O60229-3; Sequence=VSP_028905, VSP_028906, VSP_028907,
CC                                  VSP_028908;
CC         Note=Produced by alternative initiation at Met-624 of isoform 1.
CC         Inferred by similarity;
CC       Name=4; Synonyms=DUET, TRAD;
CC         IsoId=O60229-4; Sequence=VSP_028903, VSP_028912;
CC         Note=Produced by alternative splicing;
CC       Name=5;
CC         IsoId=O60229-5; Sequence=VSP_028904, VSP_028909, VSP_028913,
CC                                  VSP_028914, VSP_028915;
CC         Note=Produced by alternative splicing;
CC       Name=6;
CC         IsoId=O60229-6; Sequence=VSP_028903, VSP_028912, VSP_028913;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is brain specific. Highly expressed
CC       in cerebral cortex, putamen, amygdala, hippocampus and caudate
CC       nucleus. Weakly expressed in brain stem and cerebellum. Isoform 4
CC       is expressed in skeletal muscle.
CC   -!- DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1
CC       and RhoA which are bound by DH1 and DH2 respectively. The two GEF
CC       domains appear to play differing roles in neuronal development and
CC       axonal outgrowth. SH3 1 binds to the first GEF domain inhibiting
CC       GEF activity only when in the presence of a PXXP peptide,
CC       suggesting that the SH3 domain/peptide interaction mediates
CC       binding to GEF1. CRK1 SH3 domain binds to and inhibits GEF1
CC       activity (By similarity).
CC   -!- PTM: Autophosphorylated.
CC   -!- DISEASE: Genetic variation in KALRN is associated with
CC       susceptibility to coronary heart disease type 5 (CHDS5)
CC       [MIM:608901]. CHD is the leading cause of death and disability
CC       worldwide. CHD is multifactorial disease with a strong genetic
CC       component. Classic epidemiologic studies have revealed many risk
CC       factors for CHD, including age, sex, hypertension, dyslipidemia,
CC       diabetes mellitus, smoking, and physical inactivity.
CC   -!- MISCELLANEOUS: Called DUO because the encoded protein is closely
CC       related to but shorter than TRIO.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 2 DH (DBL-homology) domains.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SIMILARITY: Contains 5 spectrin repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58015.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC   -!- GENE_FAMILY: HOG000044462 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000160145;ENST00000360013;ENSP00000353109.
DR   EMBL; AB011422; - ;
DR   EMBL; AC022336; - ;
DR   EMBL; AC069233; - ;
DR   EMBL; AC080008; - ;
DR   EMBL; AC112129; - ;
DR   EMBL; AC117401; - ;
DR   EMBL; AK125979; - ;
DR   EMBL; AK131379; - ;
DR   EMBL; AL137629; - ;
DR   EMBL; BC026865; - ;
DR   EMBL; BC058015; - ;
DR   EMBL; U94190; - ;
DR   UniProtKB/Swiss-Prot; O60229; A8MSI4; Q6ZN45; Q8TBQ5; Q9NSZ4; Q9Y2A5; -.
DR   EMBL; U94190; AAC15791.1; -; mRNA.
DR   EMBL; AB011422; BAA76314.1; -; mRNA.
DR   EMBL; AK125979; BAC86373.1; -; mRNA.
DR   EMBL; AK131379; BAD18530.1; -; mRNA.
DR   EMBL; AC022336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC080008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026865; AAH26865.1; -; mRNA.
DR   EMBL; BC058015; AAH58015.1; ALT_SEQ; mRNA.
DR   EMBL; AL137629; CAB70850.1; -; mRNA.
DR   IPI; IPI00021156; -.
DR   IPI; IPI00028382; -.
DR   IPI; IPI00410727; -.
DR   IPI; IPI00410728; -.
DR   IPI; IPI00607777; -.
DR   IPI; IPI00794432; -.
DR   PIR; T46482; T46482.
DR   RefSeq; NP_001019831.2; NM_001024660.3.
DR   RefSeq; NP_003938.1; NM_003947.4.
DR   RefSeq; NP_008995.2; NM_007064.3.
DR   UniGene; Hs.8004; -.
DR   ProteinModelPortal; O60229; -.
DR   SMR; O60229; 187-416, 737-1004, 1279-1582, 1645-1711, 1918-2247, 2324-2389, 2467-2665, 2675-2971.
DR   IntAct; O60229; 6.
DR   MINT; MINT-2865643; -.
DR   STRING; O60229; -.
DR   PhosphoSite; O60229; -.
DR   PRIDE; O60229; -.
DR   Ensembl; ENST00000360013; ENSP00000353109; ENSG00000160145.
DR   GeneID; 8997; -.
DR   KEGG; hsa:8997; -.
DR   UCSC; uc003ehf.1; human.
DR   UCSC; uc003ehi.2; human.
DR   UCSC; uc003ehk.1; human.
DR   CTD; 8997; -.
DR   GeneCards; GC03P121187; -.
DR   HGNC; HGNC:4814; KALRN.
DR   HPA; CAB026456; -.
DR   HPA; HPA011913; -.
DR   MIM; 604605; gene.
DR   MIM; 608901; phenotype.
DR   neXtProt; NX_O60229; -.
DR   eggNOG; prNOG16621; -.
DR   GeneTree; ENSGT00560000076675; -.
DR   InParanoid; O60229; -.
DR   Pathway_Interaction_DB; arf6downstreampathway; Arf6 downstream pathway.
DR   Pathway_Interaction_DB; ephbfwdpathway; EPHB forward signaling.
DR   Reactome; REACT_11044; Signaling by Rho GTPases.
DR   Reactome; REACT_11061; Signalling by NGF.
DR   Reactome; REACT_14797; Signaling by GPCR.
DR   NextBio; 33739; -.
DR   ArrayExpress; O60229; -.
DR   Bgee; O60229; -.
DR   CleanEx; HS_KALRN; -.
DR   Genevestigator; O60229; -.
DR   GermOnline; ENSG00000160145; Homo sapiens.
DR   GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR   GO; GO:0006915; P:apoptosis; EXP:Reactome.
DR   GO; GO:0008624; P:induction of apoptosis by extracellular signals; EXP:Reactome.
DR   GO; GO:0048011; P:nerve growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0007399; P:nervous system development; ISS:HGNC.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00621; RhoGEF; 2.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 2.
DR   SMART; SM00150; SPEC; 7.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF48065; DH-domain; 2.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   HOGENOMDNA; HS3.PE3715; -.
KW   ENSG000001601451755old_1320000031; ENSP000003531097901old_1320000031;
KW   AB011422; AC022336; AC069233; AC080008; AC112129; AC117401; AK125979;
KW   AL137629; BC026865; BC058015; U94190;
KW   Alternative initiation; Alternative splicing; ATP-binding;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Disulfide bond;
KW   Guanine-nucleotide releasing factor; Immunoglobulin domain; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
SQ   SEQUENCE   2986 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDRFWDQWY LWYLRLLRLL DRGSFRNDGL KASDVLPILK EKVAFVSGGR DKRGGPILTF
     PARSNHDRIR QEDLRKLVTY LASVPSEDVC KRGFTVIIDM RGSKWDLIKP LLKTLQEAFP
     AEIHVALIIK PDNFWQKQKT NFGSSKFIFE TSMVSVEGLT KLVDPSQLTE EFDGSLDYNH
     EEWIELRLSL EEFFNSAVHL LSRLEDLQEM LARKEFPVDV EGSRRLIDEH TQLKKKVLKA
     PVEELDREGQ RLLQCIRCSD GFSGRNCIPG SADFQSLVPK ITSLLDKLHS TRQHLHQMWH
     VRKLKLDQCF QLRLFEQDAE KMFDWISHNK ELFLQSHTEI GVSYQYALDL QTQHNHFAMN
     SMNAYVNINR IMSVASRLSE AGHYASQQIK QISTQLDQEW KSFAAALDER STILAMSAVF
     HQKAEQFLSG VDAWCKMCSE GGLPSEMQDL ELAIHHHQTL YEQVTQAYTE VSQDGKALLD
     VLQRPLSPGN SESLTATANY SKAVHQVLDV VHEVLHHQRR LESIWQHRKV RLHQRLQLCV
     FQQDVQQVLD WIENHGEAFL SKHTGVGKSL HRARALQKRH DDFEEVAQNT YTNADKLLEA
     AEQLAQTGEC DPEEIYKAAR HLEVRIQDFV RRVEQRKLLL DMSVSFHTHT KELWTWMEDL
     QKEMLEDVCA DSVDAVQELI KQFQQQQTAT LDATLNVIKE GEDLIQQLRS APPSLGEPSE
     ARDSAVSNNK TPHSSSISHI ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE
     VTAELDAWNE DLLRQMNDFN TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIT
     EVQASGIELI CEKDIDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK
     QVLGWIRNGE SMLNASLVNA SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ KTHQSALQVQ
     QKAEVLLQAG HYDADAIREC AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE
     SLEQEYRRDE DWCGGRDKLG PAAEIDHVIP LISKHLEQKE AFLKACTLAR RNAEVFLKYI
     HRNNVSMPSV ASHTRGPEQQ VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK
     QALDWIQETG EFYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE
     KGHIHATEIR KWVTTVDKHY RDFSLRMGKY RYSLEKALGV NTEDNKDLEL DIIPASLSDR
     EVKLRDANHE VNEEKRKSAR KKEFIMAELL QTEKAYVRDL HECLETYLWE MTSGVEEIPP
     GILNKEHIIF GNIQEIYDFH NNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP
     DSNQLILEHA GTFFDEIQQR HGLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGELK
     DGLEVMLSVP KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI RKGRERHLFL
     FEISLVFSKE IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR TPSSDNKTVL
     KASNIETKQE WIKNIREVIQ ERIIHLKGAL KEPLQLPKTP AKQRNNSKRD GVEDIDSQGD
     GSSQPDTISI ASRTSQNTVD SDKLSGGCEL TVVLQDFSAG HSSELTIQVG QTVELLERPS
     ERPGWCLVRT TERSPPLEGL VPSSALCISH SRSSVEMDCF FPLVKDAYSH SSSENGGKSE
     SVANLQAQPS LNSIHSSPGP KRSTNTLKKW LTSPVRRLNS GKADGNIKKQ KKVRDGRKSF
     DLGSPKPGDE TTPQGDSADE KSKKGWGEDE PDEESHTPLP PPMKIFDNDP TQDEMSSSLL
     AARQASTEVP TAADLVNAIE KLVKNKLSLE GSSYRGSLKD PAGCLNEGMA PPTPPKNPEE
     EQKAKALRGR MFVLNELVQT EKDYVKDLGI VVEGFMKRIE EKGVPEDMRG KDKIVFGNIH
     QIYDWHKDFF LAELEKCIQE QDRLAQLFIK HERKLHIYVW YCQNKPRSEY IVAEYDAYFE
     EVKQEINQRL TLSDFLIKPI QRITKYQLLL KDFLRYSEKA GLECSDIEKA VELMCLVPKR
     CNDMMNLGRL QGFEGTLTAQ GKLLQQDTFY VIELDAGMQS RTKERRVFLF EQIVIFSELL
     RKGSLTPGYM FKRSIKMNYL VLEENVDNDP CKFALMNRET SERVVLQAAN ADIQQAWVQD
     INQVLETQRD FLNALQSPIE YQRKERSTAV MRSQPARLPQ ASPRPYSSVP AGSEKPPKGS
     SYNPPLPPLK ISTSNGSPGF EYHQPGDKFE ASKQNDLGGC NGTSSMAVIK DYYALKENEI
     CVSQGEVVQV LAVNQQNMCL VYQPASDHSP AAEGWVPGSI LAPLTKATAA ESSDGSIKKS
     CSWHTLRMRK RAEVENTGKN EATGPRKPKD ILGNKVSVKE TNSSEESECD DLDPNTSMEI
     LNPNFIQEVA PEFLVPLVDV TCLLGDTVIL QCKVCGRPKP TITWKGPDQN ILDTDNSSAT
     YTVSSCDSGE ITLKICNLMP QDSGIYTCIA TNDHGTTSTS ATVKVQGVPA APNRPIAQER
     SCTSVILRWL PPSSTGNCTI SGYTVEYREE GSQIWQQSVA STLDTYLVIE DLSPGCPYQF
     RVSASNPWGI SLPSEPSEFV RLPEYDAAAD GATISWKENF DSAYTELNEI GRGRFSIVKK
     CIHKATRKDV AVKFVSKKMK KKEQAAHEAA LLQHLQHPQY ITLHDTYESP TSYILILELM
     DDGRLLDYLM NHDELMEEKV AFYIRDIMEA LQYLHNCRVA HLDIKPENLL IDLRIPVPRV
     KLIDLEDAVQ ISGHFHIHHL LGNPEFAAPE VIQGIPVSLG TDIWSIGVLT YVMLSGVSPF
     LDESKEETCI NVCRVDFSFP HEYFCGVSNA ARDFINVILQ EDFRRRPTAA TCLQHPWLQP
     HNGSYSKIPL DTSRLACFIE RRKHQNDVRP IPNVKSYIVN RVNQGT
//

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