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O60229

- KALRN_HUMAN

UniProt

O60229 - KALRN_HUMAN

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Protein

Kalirin

Gene
KALRN, DUET, DUO, HAPIP, TRAD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi2689 – 26979ATP By similarity

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. protein phosphorylation Source: ProtInc
  7. regulation of GTPase activity Source: GOC
  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
Complete GO annotation...

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. Cytoplasmcytoskeleton
Note: Associated with the cytoskeleton.1 Publication

GO - Cellular componenti

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

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication

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 ↔ 2547 By similarity

Post-translational modificationi

Autophosphorylated.1 Publication

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.1 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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.
Contains 2 PH domains.
Contains 2 SH3 domains.
Contains 5 spectrin repeats.

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.

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. VSP_028903Add
BLAST
Alternative sequencei1 – 16271627Missing in isoform 5. VSP_028904Add
BLAST
Alternative sequencei1 – 641641Missing in isoform 3. VSP_028905Add
BLAST
Alternative sequencei709 – 72113Missing in isoform 3. VSP_028906Add
BLAST
Alternative sequencei1465 – 150541FDENL…FEISL → SCPPSTGEASSLPRHGGACI MGGKWHEVRQGARLEERRND K in isoform 3. VSP_028907Add
BLAST
Alternative sequencei1506 – 29851480Missing in isoform 3. VSP_028908Add
BLAST
Alternative sequencei1628 – 164316ISIAS…VDSDK → MLKWISWRQSKANKAQ in isoform 5. VSP_028909Add
BLAST
Alternative sequencei1644 – 166320LSGGC…AGHSS → DGNLVPRWHLGPGDPFSTYV in isoform 2. VSP_028910Add
BLAST
Alternative sequencei1664 – 29851322Missing in isoform 2. VSP_028911Add
BLAST
Alternative sequencei1698 – 172528EGLVP…FPLVK → MKGGDRAYTRGPSLGWLFAK CCCCFPCR in isoform 4 and isoform 6. VSP_028912Add
BLAST
Alternative sequencei1857 – 188731Missing in isoform 5 and isoform 6. VSP_028913Add
BLAST
Alternative sequencei1857 – 18571S → SS in isoform 4. VSP_047353
Alternative sequencei2313 – 23131Missing in isoform 5. VSP_028914
Alternative sequencei2398 – 2985588Missing in isoform 5. VSP_028915Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2458 – 24581E → G in BAA76314. 1 Publication

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]
ENST00000428018; ENSP00000402419; ENSG00000160145. [O60229-6]
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 ]
ENST00000428018 ; ENSP00000402419 ; ENSG00000160145 . [O60229-6 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 147 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

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