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O60229

- KALRN_HUMAN

UniProt

O60229 - KALRN_HUMAN

Protein

Kalirin

Gene

KALRN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei2712 – 27121ATP
    Active sitei2802 – 28021Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi2689 – 26979ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. guanyl-nucleotide exchange factor activity Source: ProtInc
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: ProtInc
    6. Rho guanyl-nucleotide exchange factor activity Source: InterPro

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. intracellular signal transduction Source: HGNC
    3. nervous system development Source: HGNC
    4. neurotrophin TRK receptor signaling pathway Source: Reactome
    5. positive regulation of apoptotic process Source: Reactome
    6. positive regulation of GTPase activity Source: GOC
    7. protein phosphorylation Source: ProtInc
    8. regulation of small GTPase mediated signal transduction Source: Reactome
    9. signal transduction Source: ProtInc
    10. small GTPase mediated signal transduction Source: Reactome
    11. vesicle-mediated transport Source: ProtInc

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinkiO60229.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kalirin (EC:2.7.11.1)
    Alternative name(s):
    Huntingtin-associated protein-interacting protein
    Protein Duo
    Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain
    Gene namesi
    Name:KALRN
    Synonyms:DUET, DUO, HAPIP, TRAD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:4814. KALRN.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Associated with the cytoskeleton.

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Coronary heart disease 5 (CHDS5) [MIM:608901]: A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2712 – 27121K → A: Loss of autophosphorylation. 1 Publication

    Organism-specific databases

    MIMi608901. phenotype.
    PharmGKBiPA29189.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 29852985KalirinPRO_0000080955Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1750 – 17501Phosphoserine1 Publication
    Modified residuei1753 – 17531Phosphoserine1 Publication
    Modified residuei1799 – 17991Phosphoserine2 Publications
    Modified residuei1817 – 18171Phosphoserine1 Publication
    Modified residuei2261 – 22611Phosphoserine1 Publication
    Disulfide bondi2491 ↔ 2547PROSITE-ProRule annotation

    Post-translational modificationi

    Autophosphorylated.2 Publications

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiO60229.
    PaxDbiO60229.
    PRIDEiO60229.

    PTM databases

    PhosphoSiteiO60229.

    Expressioni

    Tissue specificityi

    Isoform 2 is brain specific. Highly expressed in cerebral cortex, putamen, amygdala, hippocampus and caudate nucleus. Weakly expressed in brain stem and cerebellum. Isoform 4 is expressed in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiO60229.
    BgeeiO60229.
    CleanExiHS_KALRN.
    GenevestigatoriO60229.

    Organism-specific databases

    HPAiCAB026456.
    HPA011913.

    Interactioni

    Subunit structurei

    Interacts with the C-terminal of peptidylglycine alpha-amidating monooxygenase (PAM) and with the huntingtin-associated protein 1 (HAP1) By similarity. Interacts with FASLG.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SNCAIPQ9Y6H5-13EBI-9075360,EBI-9075374

    Protein-protein interaction databases

    BioGridi114478. 15 interactions.
    IntActiO60229. 11 interactions.
    MINTiMINT-2865643.
    STRINGi9606.ENSP00000240874.

    Structurei

    3D structure databases

    ProteinModelPortaliO60229.
    SMRiO60229. Positions 1279-1582, 1645-1711, 1918-2247, 2324-2389.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 180146CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST
    Repeati188 – 308121Spectrin 1Add
    BLAST
    Repeati310 – 416107Spectrin 2Add
    BLAST
    Repeati536 – 642107Spectrin 3Add
    BLAST
    Repeati890 – 1004115Spectrin 4Add
    BLAST
    Repeati1130 – 122293Spectrin 5Add
    BLAST
    Domaini1281 – 1456176DH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1468 – 1580113PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1646 – 171166SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1928 – 2103176DH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2115 – 2225111PH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2320 – 238566SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2470 – 256394Ig-like C2-typeAdd
    BLAST
    Domaini2570 – 266495Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini2683 – 2937255Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi682 – 6876Poly-Gln

    Domaini

    The two GEF domains catalyze nucleotide exchange for RAC1 and RhoA which are bound by DH1 and DH2 respectively. The two GEF domains appear to play differing roles in neuronal development and axonal outgrowth. SH3 1 binds to the first GEF domain inhibiting GEF activity only when in the presence of a PXXP peptide, suggesting that the SH3 domain/peptide interaction mediates binding to GEF1. CRK1 SH3 domain binds to and inhibits GEF1 activity By similarity.By similarity

    Sequence similaritiesi

    Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
    Contains 2 DH (DBL-homology) domains.PROSITE-ProRule annotation
    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 2 SH3 domains.PROSITE-ProRule annotation
    Contains 5 spectrin repeats.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG331990.
    HOGENOMiHOG000044462.
    HOVERGENiHBG108598.
    InParanoidiO60229.
    KOiK15048.
    PhylomeDBiO60229.
    TreeFamiTF318080.

    Family and domain databases

    Gene3Di1.20.900.10. 2 hits.
    2.30.29.30. 2 hits.
    2.60.40.10. 2 hits.
    3.40.525.10. 1 hit.
    InterProiIPR001251. CRAL-TRIO_dom.
    IPR000219. DH-domain.
    IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR028569. Kalirin.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PANTHERiPTHR22826:SF49. PTHR22826:SF49. 1 hit.
    PfamiPF13716. CRAL_TRIO_2. 1 hit.
    PF00041. fn3. 1 hit.
    PF07679. I-set. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00621. RhoGEF. 2 hits.
    PF00435. Spectrin. 4 hits.
    [Graphical view]
    SMARTiSM00060. FN3. 1 hit.
    SM00408. IGc2. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 2 hits.
    SM00220. S_TKc. 1 hit.
    SM00516. SEC14. 1 hit.
    SM00326. SH3. 2 hits.
    SM00150. SPEC. 7 hits.
    [Graphical view]
    SUPFAMiSSF48065. SSF48065. 2 hits.
    SSF49265. SSF49265. 1 hit.
    SSF50044. SSF50044. 2 hits.
    SSF52087. SSF52087. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50191. CRAL_TRIO. 1 hit.
    PS50010. DH_2. 2 hits.
    PS50853. FN3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: O60229-1) [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

    MTDRFWDQWY LWYLRLLRLL DRGSFRNDGL KASDVLPILK EKVAFVSGGR     50
    DKRGGPILTF PARSNHDRIR QEDLRKLVTY LASVPSEDVC KRGFTVIIDM 100
    RGSKWDLIKP LLKTLQEAFP AEIHVALIIK PDNFWQKQKT NFGSSKFIFE 150
    TSMVSVEGLT KLVDPSQLTE EFDGSLDYNH EEWIELRLSL EEFFNSAVHL 200
    LSRLEDLQEM LARKEFPVDV EGSRRLIDEH TQLKKKVLKA PVEELDREGQ 250
    RLLQCIRCSD GFSGRNCIPG SADFQSLVPK ITSLLDKLHS TRQHLHQMWH 300
    VRKLKLDQCF QLRLFEQDAE KMFDWISHNK ELFLQSHTEI GVSYQYALDL 350
    QTQHNHFAMN SMNAYVNINR IMSVASRLSE AGHYASQQIK QISTQLDQEW 400
    KSFAAALDER STILAMSAVF HQKAEQFLSG VDAWCKMCSE GGLPSEMQDL 450
    ELAIHHHQTL YEQVTQAYTE VSQDGKALLD VLQRPLSPGN SESLTATANY 500
    SKAVHQVLDV VHEVLHHQRR LESIWQHRKV RLHQRLQLCV FQQDVQQVLD 550
    WIENHGEAFL SKHTGVGKSL HRARALQKRH DDFEEVAQNT YTNADKLLEA 600
    AEQLAQTGEC DPEEIYKAAR HLEVRIQDFV RRVEQRKLLL DMSVSFHTHT 650
    KELWTWMEDL QKEMLEDVCA DSVDAVQELI KQFQQQQTAT LDATLNVIKE 700
    GEDLIQQLRS APPSLGEPSE ARDSAVSNNK TPHSSSISHI ESVLQQLDDA 750
    QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE VTAELDAWNE DLLRQMNDFN 800
    TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIT EVQASGIELI 850
    CEKDIDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK 900
    QVLGWIRNGE SMLNASLVNA SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ 950
    KTHQSALQVQ QKAEVLLQAG HYDADAIREC AEKVALHWQQ LMLKMEDRLK 1000
    LVNASVAFYK TSEQVCSVLE SLEQEYRRDE DWCGGRDKLG PAAEIDHVIP 1050
    LISKHLEQKE AFLKACTLAR RNAEVFLKYI HRNNVSMPSV ASHTRGPEQQ 1100
    VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK QALDWIQETG 1150
    EFYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE 1200
    KGHIHATEIR KWVTTVDKHY RDFSLRMGKY RYSLEKALGV NTEDNKDLEL 1250
    DIIPASLSDR EVKLRDANHE VNEEKRKSAR KKEFIMAELL QTEKAYVRDL 1300
    HECLETYLWE MTSGVEEIPP GILNKEHIIF GNIQEIYDFH NNIFLKELEK 1350
    YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP DSNQLILEHA GTFFDEIQQR 1400
    HGLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGELK DGLEVMLSVP 1450
    KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI RKGRERHLFL 1500
    FEISLVFSKE IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR 1550
    TPSSDNKTVL KASNIETKQE WIKNIREVIQ ERIIHLKGAL KEPLQLPKTP 1600
    AKQRNNSKRD GVEDIDSQGD GSSQPDTISI ASRTSQNTVD SDKLSGGCEL 1650
    TVVLQDFSAG HSSELTIQVG QTVELLERPS ERPGWCLVRT TERSPPLEGL 1700
    VPSSALCISH SRSSVEMDCF FPLVKDAYSH SSSENGGKSE SVANLQAQPS 1750
    LNSIHSSPGP KRSTNTLKKW LTSPVRRLNS GKADGNIKKQ KKVRDGRKSF 1800
    DLGSPKPGDE TTPQGDSADE KSKKGWGEDE PDEESHTPLP PPMKIFDNDP 1850
    TQDEMSSLLA ARQASTEVPT AADLVNAIEK LVKNKLSLEG SSYRGSLKDP 1900
    AGCLNEGMAP PTPPKNPEEE QKAKALRGRM FVLNELVQTE KDYVKDLGIV 1950
    VEGFMKRIEE KGVPEDMRGK DKIVFGNIHQ IYDWHKDFFL AELEKCIQEQ 2000
    DRLAQLFIKH ERKLHIYVWY CQNKPRSEYI VAEYDAYFEE VKQEINQRLT 2050
    LSDFLIKPIQ RITKYQLLLK DFLRYSEKAG LECSDIEKAV ELMCLVPKRC 2100
    NDMMNLGRLQ GFEGTLTAQG KLLQQDTFYV IELDAGMQSR TKERRVFLFE 2150
    QIVIFSELLR KGSLTPGYMF KRSIKMNYLV LEENVDNDPC KFALMNRETS 2200
    ERVVLQAANA DIQQAWVQDI NQVLETQRDF LNALQSPIEY QRKERSTAVM 2250
    RSQPARLPQA SPRPYSSVPA GSEKPPKGSS YNPPLPPLKI STSNGSPGFE 2300
    YHQPGDKFEA SKQNDLGGCN GTSSMAVIKD YYALKENEIC VSQGEVVQVL 2350
    AVNQQNMCLV YQPASDHSPA AEGWVPGSIL APLTKATAAE SSDGSIKKSC 2400
    SWHTLRMRKR AEVENTGKNE ATGPRKPKDI LGNKVSVKET NSSEESECDD 2450
    LDPNTSMEIL NPNFIQEVAP EFLVPLVDVT CLLGDTVILQ CKVCGRPKPT 2500
    ITWKGPDQNI LDTDNSSATY TVSSCDSGEI TLKICNLMPQ DSGIYTCIAT 2550
    NDHGTTSTSA TVKVQGVPAA PNRPIAQERS CTSVILRWLP PSSTGNCTIS 2600
    GYTVEYREEG SQIWQQSVAS TLDTYLVIED LSPGCPYQFR VSASNPWGIS 2650
    LPSEPSEFVR LPEYDAAADG ATISWKENFD SAYTELNEIG RGRFSIVKKC 2700
    IHKATRKDVA VKFVSKKMKK KEQAAHEAAL LQHLQHPQYI TLHDTYESPT 2750
    SYILILELMD DGRLLDYLMN HDELMEEKVA FYIRDIMEAL QYLHNCRVAH 2800
    LDIKPENLLI DLRIPVPRVK LIDLEDAVQI SGHFHIHHLL GNPEFAAPEV 2850
    IQGIPVSLGT DIWSIGVLTY VMLSGVSPFL DESKEETCIN VCRVDFSFPH 2900
    EYFCGVSNAA RDFINVILQE DFRRRPTAAT CLQHPWLQPH NGSYSKIPLD 2950
    TSRLACFIER RKHQNDVRPI PNVKSYIVNR VNQGT 2985

    Note: Produced by alternative splicing.

    Length:2,985
    Mass (Da):340,174
    Last modified:October 23, 2007 - v2
    Checksum:iF4C01D0F2422A92F
    GO
    Isoform 2 (identifier: O60229-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1644-1663: LSGGCELTVVLQDFSAGHSS → DGNLVPRWHLGPGDPFSTYV
         1664-2985: Missing.

    Note: Produced by alternative splicing. No experimental confirmation available.

    Show »
    Length:1,663
    Mass (Da):192,229
    Checksum:iFAE683734C83417C
    GO
    Isoform 3 (identifier: O60229-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-641: Missing.
         709-721: Missing.
         1465-1505: FDENLDVQGE...RHLFLFEISL → SCPPSTGEAS...ARLEERRNDK
         1506-2985: Missing.

    Note: Produced by alternative initiation at Met-624 of isoform 1. Inferred by similarity.

    Show »
    Length:851
    Mass (Da):98,659
    Checksum:i3F611F4EF00D376C
    GO
    Isoform 4 (identifier: O60229-4) [UniParc]FASTAAdd to Basket

    Also known as: DUET, TRAD

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1697: Missing.
         1698-1725: EGLVPSSALCISHSRSSVEMDCFFPLVK → MKGGDRAYTRGPSLGWLFAKCCCCFPCR
         1857-1857: S → SS

    Note: Produced by alternative splicing.

    Show »
    Length:1,289
    Mass (Da):144,485
    Checksum:iC0C2F3DBC8C2B34A
    GO
    Isoform 5 (identifier: O60229-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1627: Missing.
         1628-1643: ISIASRTSQNTVDSDK → MLKWISWRQSKANKAQ
         1857-1887: Missing.
         2313-2313: Missing.
         2398-2985: Missing.

    Note: Produced by alternative splicing.

    Show »
    Length:738
    Mass (Da):82,806
    Checksum:i1C9AC959DC07903E
    GO
    Isoform 6 (identifier: O60229-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1697: Missing.
         1698-1725: EGLVPSSALCISHSRSSVEMDCFFPLVK → MKGGDRAYTRGPSLGWLFAKCCCCFPCR
         1857-1887: Missing.

    Note: Produced by alternative splicing. No experimental confirmation available.

    Show »
    Length:1,257
    Mass (Da):141,164
    Checksum:iA45112D100678192
    GO

    Sequence cautioni

    The sequence AAH58015.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2458 – 24581E → G in BAA76314. (PubMed:10023074)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti196 – 1961S → L.1 Publication
    VAR_041898
    Natural varianti213 – 2131R → W in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035976
    Natural varianti1326 – 13261E → D.
    Corresponds to variant rs2289838 [ dbSNP | Ensembl ].
    VAR_020192
    Natural varianti1896 – 18961S → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035625
    Natural varianti1929 – 19291R → M.
    Corresponds to variant rs35298864 [ dbSNP | Ensembl ].
    VAR_057190

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 16971697Missing in isoform 4 and isoform 6. 1 PublicationVSP_028903Add
    BLAST
    Alternative sequencei1 – 16271627Missing in isoform 5. 3 PublicationsVSP_028904Add
    BLAST
    Alternative sequencei1 – 641641Missing in isoform 3. 2 PublicationsVSP_028905Add
    BLAST
    Alternative sequencei709 – 72113Missing in isoform 3. 2 PublicationsVSP_028906Add
    BLAST
    Alternative sequencei1465 – 150541FDENL…FEISL → SCPPSTGEASSLPRHGGACI MGGKWHEVRQGARLEERRND K in isoform 3. 2 PublicationsVSP_028907Add
    BLAST
    Alternative sequencei1506 – 29851480Missing in isoform 3. 2 PublicationsVSP_028908Add
    BLAST
    Alternative sequencei1628 – 164316ISIAS…VDSDK → MLKWISWRQSKANKAQ in isoform 5. 3 PublicationsVSP_028909Add
    BLAST
    Alternative sequencei1644 – 166320LSGGC…AGHSS → DGNLVPRWHLGPGDPFSTYV in isoform 2. 1 PublicationVSP_028910Add
    BLAST
    Alternative sequencei1664 – 29851322Missing in isoform 2. 1 PublicationVSP_028911Add
    BLAST
    Alternative sequencei1698 – 172528EGLVP…FPLVK → MKGGDRAYTRGPSLGWLFAK CCCCFPCR in isoform 4 and isoform 6. 1 PublicationVSP_028912Add
    BLAST
    Alternative sequencei1857 – 188731Missing in isoform 5 and isoform 6. 3 PublicationsVSP_028913Add
    BLAST
    Alternative sequencei1857 – 18571S → SS in isoform 4. 1 PublicationVSP_047353
    Alternative sequencei2313 – 23131Missing in isoform 5. 3 PublicationsVSP_028914
    Alternative sequencei2398 – 2985588Missing in isoform 5. 3 PublicationsVSP_028915Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94190 mRNA. Translation: AAC15791.1.
    AB011422 mRNA. Translation: BAA76314.1.
    AK125979 mRNA. Translation: BAC86373.1.
    AK131379 mRNA. Translation: BAD18530.1.
    AC022336 Genomic DNA. No translation available.
    AC069233 Genomic DNA. No translation available.
    AC080008 Genomic DNA. No translation available.
    AC112129 Genomic DNA. No translation available.
    AC117401 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79410.1.
    BC026865 mRNA. Translation: AAH26865.1.
    BC058015 mRNA. Translation: AAH58015.1. Sequence problems.
    AL137629 mRNA. Translation: CAB70850.1.
    CCDSiCCDS3027.1. [O60229-2]
    CCDS3028.1. [O60229-4]
    PIRiT46482.
    RefSeqiNP_001019831.2. NM_001024660.3.
    NP_003938.1. NM_003947.4. [O60229-2]
    NP_008995.2. NM_007064.3. [O60229-4]
    UniGeneiHs.13281.
    Hs.8004.

    Genome annotation databases

    EnsembliENST00000240874; ENSP00000240874; ENSG00000160145. [O60229-2]
    ENST00000291478; ENSP00000291478; ENSG00000160145. [O60229-4]
    ENST00000393496; ENSP00000377134; ENSG00000160145. [O60229-5]
    GeneIDi8997.
    KEGGihsa:8997.
    UCSCiuc003ehf.1. human. [O60229-2]
    uc003ehh.1. human. [O60229-3]
    uc003ehi.3. human. [O60229-5]
    uc003ehk.3. human.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94190 mRNA. Translation: AAC15791.1 .
    AB011422 mRNA. Translation: BAA76314.1 .
    AK125979 mRNA. Translation: BAC86373.1 .
    AK131379 mRNA. Translation: BAD18530.1 .
    AC022336 Genomic DNA. No translation available.
    AC069233 Genomic DNA. No translation available.
    AC080008 Genomic DNA. No translation available.
    AC112129 Genomic DNA. No translation available.
    AC117401 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79410.1 .
    BC026865 mRNA. Translation: AAH26865.1 .
    BC058015 mRNA. Translation: AAH58015.1 . Sequence problems.
    AL137629 mRNA. Translation: CAB70850.1 .
    CCDSi CCDS3027.1. [O60229-2 ]
    CCDS3028.1. [O60229-4 ]
    PIRi T46482.
    RefSeqi NP_001019831.2. NM_001024660.3.
    NP_003938.1. NM_003947.4. [O60229-2 ]
    NP_008995.2. NM_007064.3. [O60229-4 ]
    UniGenei Hs.13281.
    Hs.8004.

    3D structure databases

    ProteinModelPortali O60229.
    SMRi O60229. Positions 1279-1582, 1645-1711, 1918-2247, 2324-2389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114478. 15 interactions.
    IntActi O60229. 11 interactions.
    MINTi MINT-2865643.
    STRINGi 9606.ENSP00000240874.

    PTM databases

    PhosphoSitei O60229.

    Proteomic databases

    MaxQBi O60229.
    PaxDbi O60229.
    PRIDEi O60229.

    Protocols and materials databases

    DNASUi 8997.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000240874 ; ENSP00000240874 ; ENSG00000160145 . [O60229-2 ]
    ENST00000291478 ; ENSP00000291478 ; ENSG00000160145 . [O60229-4 ]
    ENST00000393496 ; ENSP00000377134 ; ENSG00000160145 . [O60229-5 ]
    GeneIDi 8997.
    KEGGi hsa:8997.
    UCSCi uc003ehf.1. human. [O60229-2 ]
    uc003ehh.1. human. [O60229-3 ]
    uc003ehi.3. human. [O60229-5 ]
    uc003ehk.3. human.

    Organism-specific databases

    CTDi 8997.
    GeneCardsi GC03P123798.
    HGNCi HGNC:4814. KALRN.
    HPAi CAB026456.
    HPA011913.
    MIMi 604605. gene.
    608901. phenotype.
    neXtProti NX_O60229.
    PharmGKBi PA29189.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331990.
    HOGENOMi HOG000044462.
    HOVERGENi HBG108598.
    InParanoidi O60229.
    KOi K15048.
    PhylomeDBi O60229.
    TreeFami TF318080.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinki O60229.

    Miscellaneous databases

    ChiTaRSi KALRN. human.
    GeneWikii Kalirin.
    GenomeRNAii 8997.
    NextBioi 33739.
    PROi O60229.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60229.
    Bgeei O60229.
    CleanExi HS_KALRN.
    Genevestigatori O60229.

    Family and domain databases

    Gene3Di 1.20.900.10. 2 hits.
    2.30.29.30. 2 hits.
    2.60.40.10. 2 hits.
    3.40.525.10. 1 hit.
    InterProi IPR001251. CRAL-TRIO_dom.
    IPR000219. DH-domain.
    IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR028569. Kalirin.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    PANTHERi PTHR22826:SF49. PTHR22826:SF49. 1 hit.
    Pfami PF13716. CRAL_TRIO_2. 1 hit.
    PF00041. fn3. 1 hit.
    PF07679. I-set. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00621. RhoGEF. 2 hits.
    PF00435. Spectrin. 4 hits.
    [Graphical view ]
    SMARTi SM00060. FN3. 1 hit.
    SM00408. IGc2. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 2 hits.
    SM00220. S_TKc. 1 hit.
    SM00516. SEC14. 1 hit.
    SM00326. SH3. 2 hits.
    SM00150. SPEC. 7 hits.
    [Graphical view ]
    SUPFAMi SSF48065. SSF48065. 2 hits.
    SSF49265. SSF49265. 1 hit.
    SSF50044. SSF50044. 2 hits.
    SSF52087. SSF52087. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50191. CRAL_TRIO. 1 hit.
    PS50010. DH_2. 2 hits.
    PS50853. FN3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Huntingtin-associated protein 1 (HAP1) binds to a Trio-like polypeptide, with a rac1 guanine nucleotide exchange factor domain."
      Colomer V., Engelender S., Sharp A.H., Duan K., Cooper J.K., Lanahan A., Lyford G., Worley P., Ross C.A.
      Hum. Mol. Genet. 6:1519-1525(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Frontal cortex.
    2. "Duet is a novel serine/threonine kinase with Dbl-homology (DH) and pleckstrin-homology (PH) domains."
      Kawai T., Sanjo H., Akira S.
      Gene 227:249-255(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, MUTAGENESIS OF LYS-2712, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Skeletal muscle.
    3. "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] (ISOFORMS 3 AND 5).
      Tissue: Amygdala and Testis.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1-1917 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2104-2985 (ISOFORM 5).
      Tissue: Kidney.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2016-2985 (ISOFORM 5).
      Tissue: Testis.
    8. Cited for: INVOLVEMENT IN CHDS5.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1750; SER-1753; SER-1799; SER-1817 AND SER-2261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    12. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-213 AND CYS-1896.
    13. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-196.

    Entry informationi

    Entry nameiKALRN_HUMAN
    AccessioniPrimary (citable) accession number: O60229
    Secondary accession number(s): A8MSI4
    , C9JQ37, Q6ZN45, Q8TBQ5, Q9NSZ4, Q9Y2A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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

    Called DUO because the encoded protein is closely related to but shorter than TRIO.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3