Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O60229 (KALRN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KALRN
Synonyms:DUET, DUO, HAPIP, TRAD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2985 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Subunit structure

Interacts with the C-terminal of peptidylglycine alpha-amidating monooxygenase (PAM) and with the huntingtin-associated protein 1 (HAP1) By similarity. Interacts with FASLG. Ref.11

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Note: Associated with the cytoskeleton. Ref.2

Tissue specificity

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. Ref.2

Domain

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.

Post-translational modification

Autophosphorylated. Ref.2

Involvement in disease

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. Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 CRAL-TRIO domain.

Contains 2 DH (DBL-homology) domains.

Contains 1 fibronectin type-III domain.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 2 PH domains.

Contains 1 protein kinase domain.

Contains 2 SH3 domains.

Contains 5 spectrin repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
SH3 domain
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionGuanine-nucleotide releasing factor
Kinase
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from sequence or structural similarity. Source: HGNC

nervous system development

Inferred from sequence or structural similarity. Source: HGNC

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

protein phosphorylation

Traceable author statement Ref.2. Source: ProtInc

regulation of GTPase activity

Traceable author statement Ref.1. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.1. Source: ProtInc

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

vesicle-mediated transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.2. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Rho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

guanyl-nucleotide exchange factor activity

Traceable author statement Ref.1. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNCAIPQ9Y6H5-13EBI-9075360,EBI-9075374

Alternative products

This entry describes 6 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: O60229-1)

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.
Note: Produced by alternative splicing.
Isoform 2 (identifier: O60229-2)

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.
Isoform 3 (identifier: O60229-3)

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.
Isoform 4 (identifier: O60229-4)

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.
Isoform 5 (identifier: O60229-5)

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.
Isoform 6 (identifier: O60229-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 29852985Kalirin
PRO_0000080955

Regions

Domain35 – 180146CRAL-TRIO
Repeat188 – 308121Spectrin 1
Repeat310 – 416107Spectrin 2
Repeat536 – 642107Spectrin 3
Repeat890 – 1004115Spectrin 4
Repeat1130 – 122293Spectrin 5
Domain1281 – 1456176DH 1
Domain1468 – 1580113PH 1
Domain1646 – 171166SH3 1
Domain1928 – 2103176DH 2
Domain2115 – 2225111PH 2
Domain2320 – 238566SH3 2
Domain2470 – 256394Ig-like C2-type
Domain2570 – 266495Fibronectin type-III
Domain2683 – 2937255Protein kinase
Nucleotide binding2689 – 26979ATP By similarity
Compositional bias682 – 6876Poly-Gln

Sites

Active site28021Proton acceptor By similarity
Binding site27121ATP

Amino acid modifications

Modified residue17501Phosphoserine Ref.9
Modified residue17531Phosphoserine Ref.9
Modified residue17991Phosphoserine Ref.9 Ref.10
Modified residue18171Phosphoserine Ref.9
Modified residue22611Phosphoserine Ref.9
Disulfide bond2491 ↔ 2547 By similarity

Natural variations

Alternative sequence1 – 16971697Missing in isoform 4 and isoform 6.
VSP_028903
Alternative sequence1 – 16271627Missing in isoform 5.
VSP_028904
Alternative sequence1 – 641641Missing in isoform 3.
VSP_028905
Alternative sequence709 – 72113Missing in isoform 3.
VSP_028906
Alternative sequence1465 – 150541FDENL…FEISL → SCPPSTGEASSLPRHGGACI MGGKWHEVRQGARLEERRND K in isoform 3.
VSP_028907
Alternative sequence1506 – 29851480Missing in isoform 3.
VSP_028908
Alternative sequence1628 – 164316ISIAS…VDSDK → MLKWISWRQSKANKAQ in isoform 5.
VSP_028909
Alternative sequence1644 – 166320LSGGC…AGHSS → DGNLVPRWHLGPGDPFSTYV in isoform 2.
VSP_028910
Alternative sequence1664 – 29851322Missing in isoform 2.
VSP_028911
Alternative sequence1698 – 172528EGLVP…FPLVK → MKGGDRAYTRGPSLGWLFAK CCCCFPCR in isoform 4 and isoform 6.
VSP_028912
Alternative sequence1857 – 188731Missing in isoform 5 and isoform 6.
VSP_028913
Alternative sequence18571S → SS in isoform 4.
VSP_047353
Alternative sequence23131Missing in isoform 5.
VSP_028914
Alternative sequence2398 – 2985588Missing in isoform 5.
VSP_028915
Natural variant1961S → L. Ref.13
VAR_041898
Natural variant2131R → W in a colorectal cancer sample; somatic mutation. Ref.12
VAR_035976
Natural variant13261E → D.
Corresponds to variant rs2289838 [ dbSNP | Ensembl ].
VAR_020192
Natural variant18961S → C in a breast cancer sample; somatic mutation. Ref.12
VAR_035625
Natural variant19291R → M.
Corresponds to variant rs35298864 [ dbSNP | Ensembl ].
VAR_057190

Experimental info

Mutagenesis27121K → A: Loss of autophosphorylation. Ref.2
Sequence conflict24581E → G in BAA76314. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: F4C01D0F2422A92F

FASTA2,985340,174
        10         20         30         40         50         60 
MTDRFWDQWY LWYLRLLRLL DRGSFRNDGL KASDVLPILK EKVAFVSGGR DKRGGPILTF 

        70         80         90        100        110        120 
PARSNHDRIR QEDLRKLVTY LASVPSEDVC KRGFTVIIDM RGSKWDLIKP LLKTLQEAFP 

       130        140        150        160        170        180 
AEIHVALIIK PDNFWQKQKT NFGSSKFIFE TSMVSVEGLT KLVDPSQLTE EFDGSLDYNH 

       190        200        210        220        230        240 
EEWIELRLSL EEFFNSAVHL LSRLEDLQEM LARKEFPVDV EGSRRLIDEH TQLKKKVLKA 

       250        260        270        280        290        300 
PVEELDREGQ RLLQCIRCSD GFSGRNCIPG SADFQSLVPK ITSLLDKLHS TRQHLHQMWH 

       310        320        330        340        350        360 
VRKLKLDQCF QLRLFEQDAE KMFDWISHNK ELFLQSHTEI GVSYQYALDL QTQHNHFAMN 

       370        380        390        400        410        420 
SMNAYVNINR IMSVASRLSE AGHYASQQIK QISTQLDQEW KSFAAALDER STILAMSAVF 

       430        440        450        460        470        480 
HQKAEQFLSG VDAWCKMCSE GGLPSEMQDL ELAIHHHQTL YEQVTQAYTE VSQDGKALLD 

       490        500        510        520        530        540 
VLQRPLSPGN SESLTATANY SKAVHQVLDV VHEVLHHQRR LESIWQHRKV RLHQRLQLCV 

       550        560        570        580        590        600 
FQQDVQQVLD WIENHGEAFL SKHTGVGKSL HRARALQKRH DDFEEVAQNT YTNADKLLEA 

       610        620        630        640        650        660 
AEQLAQTGEC DPEEIYKAAR HLEVRIQDFV RRVEQRKLLL DMSVSFHTHT KELWTWMEDL 

       670        680        690        700        710        720 
QKEMLEDVCA DSVDAVQELI KQFQQQQTAT LDATLNVIKE GEDLIQQLRS APPSLGEPSE 

       730        740        750        760        770        780 
ARDSAVSNNK TPHSSSISHI ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE 

       790        800        810        820        830        840 
VTAELDAWNE DLLRQMNDFN TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIT 

       850        860        870        880        890        900 
EVQASGIELI CEKDIDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK 

       910        920        930        940        950        960 
QVLGWIRNGE SMLNASLVNA SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ KTHQSALQVQ 

       970        980        990       1000       1010       1020 
QKAEVLLQAG HYDADAIREC AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE 

      1030       1040       1050       1060       1070       1080 
SLEQEYRRDE DWCGGRDKLG PAAEIDHVIP LISKHLEQKE AFLKACTLAR RNAEVFLKYI 

      1090       1100       1110       1120       1130       1140 
HRNNVSMPSV ASHTRGPEQQ VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK 

      1150       1160       1170       1180       1190       1200 
QALDWIQETG EFYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE 

      1210       1220       1230       1240       1250       1260 
KGHIHATEIR KWVTTVDKHY RDFSLRMGKY RYSLEKALGV NTEDNKDLEL DIIPASLSDR 

      1270       1280       1290       1300       1310       1320 
EVKLRDANHE VNEEKRKSAR KKEFIMAELL QTEKAYVRDL HECLETYLWE MTSGVEEIPP 

      1330       1340       1350       1360       1370       1380 
GILNKEHIIF GNIQEIYDFH NNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP 

      1390       1400       1410       1420       1430       1440 
DSNQLILEHA GTFFDEIQQR HGLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGELK 

      1450       1460       1470       1480       1490       1500 
DGLEVMLSVP KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI RKGRERHLFL 

      1510       1520       1530       1540       1550       1560 
FEISLVFSKE IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR TPSSDNKTVL 

      1570       1580       1590       1600       1610       1620 
KASNIETKQE WIKNIREVIQ ERIIHLKGAL KEPLQLPKTP AKQRNNSKRD GVEDIDSQGD 

      1630       1640       1650       1660       1670       1680 
GSSQPDTISI ASRTSQNTVD SDKLSGGCEL TVVLQDFSAG HSSELTIQVG QTVELLERPS 

      1690       1700       1710       1720       1730       1740 
ERPGWCLVRT TERSPPLEGL VPSSALCISH SRSSVEMDCF FPLVKDAYSH SSSENGGKSE 

      1750       1760       1770       1780       1790       1800 
SVANLQAQPS LNSIHSSPGP KRSTNTLKKW LTSPVRRLNS GKADGNIKKQ KKVRDGRKSF 

      1810       1820       1830       1840       1850       1860 
DLGSPKPGDE TTPQGDSADE KSKKGWGEDE PDEESHTPLP PPMKIFDNDP TQDEMSSLLA 

      1870       1880       1890       1900       1910       1920 
ARQASTEVPT AADLVNAIEK LVKNKLSLEG SSYRGSLKDP AGCLNEGMAP PTPPKNPEEE 

      1930       1940       1950       1960       1970       1980 
QKAKALRGRM FVLNELVQTE KDYVKDLGIV VEGFMKRIEE KGVPEDMRGK DKIVFGNIHQ 

      1990       2000       2010       2020       2030       2040 
IYDWHKDFFL AELEKCIQEQ DRLAQLFIKH ERKLHIYVWY CQNKPRSEYI VAEYDAYFEE 

      2050       2060       2070       2080       2090       2100 
VKQEINQRLT LSDFLIKPIQ RITKYQLLLK DFLRYSEKAG LECSDIEKAV ELMCLVPKRC 

      2110       2120       2130       2140       2150       2160 
NDMMNLGRLQ GFEGTLTAQG KLLQQDTFYV IELDAGMQSR TKERRVFLFE QIVIFSELLR 

      2170       2180       2190       2200       2210       2220 
KGSLTPGYMF KRSIKMNYLV LEENVDNDPC KFALMNRETS ERVVLQAANA DIQQAWVQDI 

      2230       2240       2250       2260       2270       2280 
NQVLETQRDF LNALQSPIEY QRKERSTAVM RSQPARLPQA SPRPYSSVPA GSEKPPKGSS 

      2290       2300       2310       2320       2330       2340 
YNPPLPPLKI STSNGSPGFE YHQPGDKFEA SKQNDLGGCN GTSSMAVIKD YYALKENEIC 

      2350       2360       2370       2380       2390       2400 
VSQGEVVQVL AVNQQNMCLV YQPASDHSPA AEGWVPGSIL APLTKATAAE SSDGSIKKSC 

      2410       2420       2430       2440       2450       2460 
SWHTLRMRKR AEVENTGKNE ATGPRKPKDI LGNKVSVKET NSSEESECDD LDPNTSMEIL 

      2470       2480       2490       2500       2510       2520 
NPNFIQEVAP EFLVPLVDVT CLLGDTVILQ CKVCGRPKPT ITWKGPDQNI LDTDNSSATY 

      2530       2540       2550       2560       2570       2580 
TVSSCDSGEI TLKICNLMPQ DSGIYTCIAT NDHGTTSTSA TVKVQGVPAA PNRPIAQERS 

      2590       2600       2610       2620       2630       2640 
CTSVILRWLP PSSTGNCTIS GYTVEYREEG SQIWQQSVAS TLDTYLVIED LSPGCPYQFR 

      2650       2660       2670       2680       2690       2700 
VSASNPWGIS LPSEPSEFVR LPEYDAAADG ATISWKENFD SAYTELNEIG RGRFSIVKKC 

      2710       2720       2730       2740       2750       2760 
IHKATRKDVA VKFVSKKMKK KEQAAHEAAL LQHLQHPQYI TLHDTYESPT SYILILELMD 

      2770       2780       2790       2800       2810       2820 
DGRLLDYLMN HDELMEEKVA FYIRDIMEAL QYLHNCRVAH LDIKPENLLI DLRIPVPRVK 

      2830       2840       2850       2860       2870       2880 
LIDLEDAVQI SGHFHIHHLL GNPEFAAPEV IQGIPVSLGT DIWSIGVLTY VMLSGVSPFL 

      2890       2900       2910       2920       2930       2940 
DESKEETCIN VCRVDFSFPH EYFCGVSNAA RDFINVILQE DFRRRPTAAT CLQHPWLQPH 

      2950       2960       2970       2980 
NGSYSKIPLD TSRLACFIER RKHQNDVRPI PNVKSYIVNR VNQGT 

« Hide

Isoform 2 [UniParc].

Checksum: FAE683734C83417C
Show »

FASTA1,663192,229
Isoform 3 [UniParc].

Checksum: 3F611F4EF00D376C
Show »

FASTA85198,659
Isoform 4 (DUET) (TRAD) [UniParc].

Checksum: C0C2F3DBC8C2B34A
Show »

FASTA1,289144,485
Isoform 5 [UniParc].

Checksum: 1C9AC959DC07903E
Show »

FASTA73882,806
Isoform 6 [UniParc].

Checksum: A45112D100678192
Show »

FASTA1,257141,164

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2016-2985 (ISOFORM 5).
Tissue: Testis.
[8]"Peakwide mapping on chromosome 3q13 identifies the kalirin gene as a novel candidate gene for coronary artery disease."
Wang L., Hauser E.R., Shah S.H., Pericak-Vance M.A., Haynes C., Crosslin D., Harris M. II, Nelson S., Hale A.B., Granger C.B., Haines J.L., Jones C.J.H., Crossman D., Seo D., Gregory S.G., Kraus W.E., Goldschmidt-Clermont P.J., Vance J.M.
Am. J. Hum. Genet. 80:650-663(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CHDS5.
[9]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT46482.
RefSeqNP_001019831.2. NM_001024660.3.
NP_003938.1. NM_003947.4.
NP_008995.2. NM_007064.3.
UniGeneHs.8004.

3D structure databases

ProteinModelPortalO60229.
SMRO60229. Positions 1279-1582, 1645-1711, 1918-2247, 2324-2389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114478. 15 interactions.
IntActO60229. 11 interactions.
MINTMINT-2865643.
STRING9606.ENSP00000240874.

PTM databases

PhosphoSiteO60229.

Proteomic databases

PaxDbO60229.
PRIDEO60229.

Protocols and materials databases

DNASU8997.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240874; ENSP00000240874; ENSG00000160145. [O60229-2]
ENST00000291478; ENSP00000291478; ENSG00000160145. [O60229-4]
ENST00000393496; ENSP00000377134; ENSG00000160145. [O60229-5]
ENST00000428018; ENSP00000402419; ENSG00000160145. [O60229-6]
GeneID8997.
KEGGhsa:8997.
UCSCuc003ehf.1. human. [O60229-2]
uc003ehh.1. human. [O60229-3]
uc003ehi.3. human. [O60229-5]

Organism-specific databases

CTD8997.
GeneCardsGC03P123798.
HGNCHGNC:4814. KALRN.
HPACAB026456.
HPA011913.
MIM604605. gene.
608901. phenotype.
neXtProtNX_O60229.
PharmGKBPA29189.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331990.
HOGENOMHOG000044462.
HOVERGENHBG108598.
InParanoidO60229.
KOK15048.
PhylomeDBO60229.
TreeFamTF318080.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkO60229.

Gene expression databases

ArrayExpressO60229.
BgeeO60229.
CleanExHS_KALRN.
GenevestigatorO60229.

Family and domain databases

Gene3D1.20.900.10. 2 hits.
2.30.29.30. 2 hits.
2.60.40.10. 2 hits.
3.40.525.10. 1 hit.
InterProIPR001251. 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.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
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]
PANTHERPTHR22826:SF49. PTHR22826:SF49. 1 hit.
PfamPF13716. 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]
SMARTSM00060. 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]
SUPFAMSSF48065. SSF48065. 2 hits.
SSF49265. SSF49265. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF52087. SSF52087. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50191. 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]
ProtoNetSearch...

Other

ChiTaRSKALRN. human.
GeneWikiKalirin.
GenomeRNAi8997.
NextBio33739.
PROO60229.
SOURCESearch...

Entry information

Entry nameKALRN_HUMAN
AccessionPrimary (citable) accession number: O60229
Secondary accession number(s): A8MSI4 expand/collapse secondary AC list , C9JQ37, Q6ZN45, Q8TBQ5, Q9NSZ4, Q9Y2A5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM