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A2CG49 (KALRN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
Protein Duo
Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain
Gene names
Name:Kalrn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2964 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 By similarity. UniProtKB P97924

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB O60229

Cofactor

Magnesium By similarity. UniProtKB O60229

Subunit structure

Interacts with the C-terminal of peptidylglycine alpha-amidating monooxygenase (PAM) and with the huntingtin-associated protein 1 (HAP1). Interacts with FASLG By similarity. UniProtKB P97924

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity UniProtKB O60229 UniProtKB P97924.

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. UniProtKB P97924

Post-translational modification

Autophosphorylated By similarity. UniProtKB O60229

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.

Alternative products

This entry describes 9 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 Ref.2 (identifier: A2CG49-1)

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 Ref.2 (identifier: A2CG49-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2371-2375: KSCSW → TLLKP
     2376-2964: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 3 Ref.1 (identifier: A2CG49-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2731: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 4 Ref.1 (identifier: A2CG49-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1669: Missing.
     1670-1697: QEGLVPSSALCISHSRSSVEMDCFFPLK → MKGGDQAYTRGPSLGWLFAKCCCCFPCR
     1828-1858: Missing.
     2285-2285: Missing.
     2372-2374: SCS → EPY
     2375-2964: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 5 Ref.1 (identifier: A2CG49-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-623: Missing.
     923-923: E → ESLFHATSLQ
     1617-1636: LSGGCELTVVLQDFSAGHSS → DGNLVPRWHLGPGDPFSTYV
     1637-2964: Missing.
Note: Produced by alternative initiation at Met-624 of isoform 1. Inferred by similarity.
Isoform 6 Ref.1 (identifier: A2CG49-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1669: Missing.
     1670-1697: QEGLVPSSALCISHSRSSVEMDCFFPLK → MKGGDQAYTRGPSLGWLFAKCCCCFPCR
     2285-2285: Missing.
     2357-2364: KATAAAES → QSQSRGRK
     2365-2964: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 7 Ref.1 (identifier: A2CG49-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVLS → MNPPEGASEEGGAADSDVDAFFRT
     1859-1898: TLEGGSYRGS...LEEEQKAKAL → VSGHAGGSSE...HPNFTNRNCI
Note: Produced by alternative splicing.
Isoform 8 Ref.1 (identifier: A2CG49-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVLS → MTDRFWDQWYLWYLRLLRLLDR
     923-923: E → ESLFHATSLQ
     1617-1636: LSGGCELTVVLQDFSAGHSS → DGNLVPRWHLGPGDPFSTYV
     1637-2964: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 9 Ref.1 (identifier: A2CG49-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVLS → MTDRFWDQWYLWYLRLLRLLDR
     1617-1636: LSGGCELTVVLQDFSAGHSS → DGNLVPRWHLGPGDPFSTYV
     1637-2964: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 29642964Kalirin
PRO_0000308173

Regions

Domain17 – 162146CRAL-TRIO
Repeat170 – 290121Spectrin 1
Repeat292 – 398107Spectrin 2
Repeat518 – 624107Spectrin 3
Repeat872 – 977106Spectrin 4
Repeat1103 – 119593Spectrin 5
Domain1254 – 1429176DH 1
Domain1441 – 1553113PH 1
Domain1619 – 168466SH3 1
Domain1900 – 2075176DH 2
Domain2087 – 2197111PH 2
Domain2292 – 235766SH3 2
Domain2443 – 253694Ig-like C2-type
Domain2543 – 263795Fibronectin type-III
Domain2656 – 2910255Protein kinase
Nucleotide binding2662 – 26709ATP By similarity UniProtKB P28523
Compositional bias664 – 6696Poly-Gln

Sites

Active site27751Proton acceptor By similarity UniProtKB P28523
Binding site26851ATP By similarity UniProtKB O60229

Amino acid modifications

Modified residue17221Phosphoserine Ref.5
Modified residue17251Phosphoserine By similarity
Modified residue17711Phosphoserine Ref.5
Modified residue17891Phosphoserine By similarity
Modified residue22331Phosphoserine By similarity
Disulfide bond2464 ↔ 2520 By similarity UniProtKB O60229

Natural variations

Alternative sequence1 – 27312731Missing in isoform 3. Ref.1
VSP_052562
Alternative sequence1 – 16691669Missing in isoform 4 and isoform 6. Ref.1
VSP_052563
Alternative sequence1 – 623623Missing in isoform 5. Ref.1
VSP_052564
Alternative sequence1 – 44MVLS → MNPPEGASEEGGAADSDVDA FFRT in isoform 7. Ref.1
VSP_052565
Alternative sequence1 – 44MVLS → MTDRFWDQWYLWYLRLLRLL DR in isoform 8 and isoform 9. Ref.1
VSP_052566
Alternative sequence9231E → ESLFHATSLQ in isoform 5 and isoform 8. Ref.1
VSP_052567
Alternative sequence1617 – 163620LSGGC…AGHSS → DGNLVPRWHLGPGDPFSTYV in isoform 5, isoform 8 and isoform 9. Ref.1
VSP_052568
Alternative sequence1637 – 29641328Missing in isoform 5, isoform 8 and isoform 9. Ref.1
VSP_052569
Alternative sequence1670 – 169728QEGLV…FFPLK → MKGGDQAYTRGPSLGWLFAK CCCCFPCR in isoform 4 and isoform 6. Ref.1
VSP_052570
Alternative sequence1828 – 185831Missing in isoform 4. Ref.1
VSP_052571
Alternative sequence1859 – 189840TLEGG…KAKAL → VSGHAGGSSELPLTSVWLPG PQPGPRTGLPHPNFTNRNCI in isoform 7. Ref.1
VSP_052572
Alternative sequence22851Missing in isoform 4 and isoform 6. Ref.1
VSP_052573
Alternative sequence2357 – 23648KATAAAES → QSQSRGRK in isoform 6. Ref.1
VSP_052574
Alternative sequence2365 – 2964600Missing in isoform 6. Ref.1
VSP_052575
Alternative sequence2371 – 23755KSCSW → TLLKP in isoform 2. Ref.2
VSP_052576
Alternative sequence2372 – 23743SCS → EPY in isoform 4. Ref.1
VSP_052577
Alternative sequence2375 – 2964590Missing in isoform 4. Ref.1
VSP_052578
Alternative sequence2376 – 2964589Missing in isoform 2. Ref.2
VSP_052579

Experimental info

Sequence conflict18241Q → H in BAC40535. Ref.1
Sequence conflict23161G → S in BAB25925. Ref.1
Sequence conflict23441E → K in BAB25925. Ref.1
Sequence conflict23551L → F in BAB25925. Ref.1
Isoform 5:
Sequence conflict7111E → K in BAE34776. Ref.1

Secondary structure

............ 2964
Helix Strand Turn

Details...

Sequences

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

Last modified February 20, 2007. Version 1.
Checksum: 76064FE06AA2BD9C

FASTA2,964337,000
        10         20         30         40         50         60 
MVLSGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL TFPARSNHDR IRQEDLRKLV 

        70         80         90        100        110        120 
TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA FPAEIHVALI IKPDNFWQKQ 

       130        140        150        160        170        180 
KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY NHEEWIELRL SLEEFFNSAV 

       190        200        210        220        230        240 
HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVL KAPVEELDRE GQRLLQCIRC 

       250        260        270        280        290        300 
SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM WHVRKLKLDQ CFQLRLFEQD 

       310        320        330        340        350        360 
AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA MNSMNAYVNI NRIMSVASRL 

       370        380        390        400        410        420 
SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA VFHQKAEQFL SGVDAWCKMC 

       430        440        450        460        470        480 
SEGGLPSEMQ DLELAIHHHQ SLYEQVTQAY TEVSQDGKAL LDVLQRPLSP GNSESLTATA 

       490        500        510        520        530        540 
NYSKAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL CVFQQDVQQV LDWIENHGEA 

       550        560        570        580        590        600 
FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL EAAEQLAQTG ECDPEEIYKA 

       610        620        630        640        650        660 
ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME DLQKEVLEDV CADSVDAVQE 

       670        680        690        700        710        720 
LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP TEARDSAMSN NKTPHSSSIS 

       730        740        750        760        770        780 
HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT IEVTAELDAW NEDLLRQMND 

       790        800        810        820        830        840 
FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY IMEVQASGIE LICEKDLDLA 

       850        860        870        880        890        900 
AQVQELLEFL HEKQHELELN AEQTHKRLEQ CLQLRHLQAE VKQVLGWIRN GESMLNASLV 

       910        920        930        940        950        960 
NASSLSEAEQ LQREHEQFQL AIEKTHQSAL QVQQKAEALL QAGHYDADAI RECAEKVALH 

       970        980        990       1000       1010       1020 
WQQLMLKMED RLKLVNASVA FYKTSEQVCS VLESLEQEYR RDEDWCGGRD KLGPAAEMDH 

      1030       1040       1050       1060       1070       1080 
VIPLLSKHLE QKEAFLKACT LARRNAEVFL KYIHRNNVSM PSVASHTRGP EQQVKAILSE 

      1090       1100       1110       1120       1130       1140 
LLQRENRVLH FWTLKKRRLD QCQQYVVFER SAKQALDWIQ ETGEYYLSTH TSTGETTEET 

      1150       1160       1170       1180       1190       1200 
QELLKEYGEF RVPAKQTKEK VKLLIQLADS FVEKGHIHAT EIRKWVTTVD KHYRDFSLRM 

      1210       1220       1230       1240       1250       1260 
GKYRYSLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA NHEINEEKRK SARKKEFIMA 

      1270       1280       1290       1300       1310       1320 
ELLQTEKAYV RDLHECLETY LWEMTSGVEE IPPGILNKEH IIFGNIQEIY DFHNNIFLKE 

      1330       1340       1350       1360       1370       1380 
LEKYEQLPED VGHCFVTWAD KFQMYVTYCK NKPDSNQLIL EHAGTFFDEI QQRHGLANSI 

      1390       1400       1410       1420       1430       1440 
SSYLIKPVQR VTKYQLLLKE LLTCCEEGKG ELKDGLEVML SVPKKANDAM HVSMLEGFDE 

      1450       1460       1470       1480       1490       1500 
NLDVQGELIL QDAFQVWDPK SLIRKGRERH LFLFEISLVF SKEIKDSSGH TKYVYKNKLL 

      1510       1520       1530       1540       1550       1560 
TSELGVTEHV EGDPCKFALW SGRTPSSDNK TVLKASNIET KQEWIKNIRE VIQERIIHLK 

      1570       1580       1590       1600       1610       1620 
GALKEPIQLP KTPAKLRNNS KRDGVEDGDS QGDGSSQPDT ISIASRTSQN TVESDKLSGG 

      1630       1640       1650       1660       1670       1680 
CELTVVLQDF SAGHSSELSI QVGQTVELLE RPSERPGWCL VRTTERSPPQ EGLVPSSALC 

      1690       1700       1710       1720       1730       1740 
ISHSRSSVEM DCFFPLKDSY SHSSSENGGK SESVAHLQSQ PSLNSIHSSP GPKRSTNTLK 

      1750       1760       1770       1780       1790       1800 
KWLTSPVRRL NSGKADGNIK KQKKVRDGRK SFDLGSPKPG DETTPQGDSA DEKSKKGWGE 

      1810       1820       1830       1840       1850       1860 
DEPDEESHTP LPPPMKIFDN DPTQDEMSSL LAARQAPPDV PTAADLVSAI EKLVKNKLTL 

      1870       1880       1890       1900       1910       1920 
EGGSYRGSLK DPTGCLNEGM TPPTPPRNLE EEQKAKALRG RMFVLNELVQ TEKDYVKDLG 

      1930       1940       1950       1960       1970       1980 
IVVEGFMKRI EEKGVPEDMR GKEKIVFGNI HQIYDWHKDF FLAELEKCIQ EQDRLAQLFI 

      1990       2000       2010       2020       2030       2040 
KHERKLHIYV WYCQNKPRSE YIVAEYDAYF EEVKQEINQR LTLSDFLIKP IQRITKYQLL 

      2050       2060       2070       2080       2090       2100 
LKDFLRYSEK AGLECSDIEK AVELMCLVPK RCNDMMNLGR LQGFEGTLTA QGKLLQQDTF 

      2110       2120       2130       2140       2150       2160 
YVIELDAGMQ SRTKERRVFL FEQIVIFSEL LRKGSLTPGY MFKRSIKMNY LVLEDNVDGD 

      2170       2180       2190       2200       2210       2220 
PCKFALMNRE TSERVILQAA NSDIQQAWVQ DINQVLETQR DFLNALQSPI EYQRKERSTA 

      2230       2240       2250       2260       2270       2280 
VIRSQPPRVP QASPRPYSSG PVGSEKPPKG SSYNPPLPPL KISTSNGSPG FDYHQPGDKF 

      2290       2300       2310       2320       2330       2340 
DASKQNDLGG CNGTSTMTVI KDYYALKENE ICVSQGEVVQ VLAVNQQNMC LVYQPASDHS 

      2350       2360       2370       2380       2390       2400 
PAAEGWVPGS ILAPLAKATA AAESSDGSIK KSCSWHTLRM RKRADVENSG KNEATGPRKP 

      2410       2420       2430       2440       2450       2460 
KDILGNKVSV KETNSSEESE CDDLDPNTSM EILNPNFIQE VAPEFLVPLV DVTCLLGDTV 

      2470       2480       2490       2500       2510       2520 
LLQCKACGRP KPSITWKGPD QNILDTDNSS ATYTISSCDS GESTLKICNL MPQDSGIYTC 

      2530       2540       2550       2560       2570       2580 
IAANDHGTAS TSATVKVQGV PAAPNRPIAQ ERSCTSVILR WLPPASTGNC TISGYTVEYR 

      2590       2600       2610       2620       2630       2640 
EEGSQVWQQS VASTLDTYLV IEDLSPGCPY QFRVSASNPW GISLPSEPSE FVRLPEYDAA 

      2650       2660       2670       2680       2690       2700 
ADGATISWKE NFDSAYTELN EIGRGRFSIV KKCIHKATRK DVAVKFVSKK MKKKEQAAHE 

      2710       2720       2730       2740       2750       2760 
AALLQHLQHP QYVTLHDTYE SPTSYILILE LMDDGRLLDY LMNHDELMEE KVAFYIRDIM 

      2770       2780       2790       2800       2810       2820 
EALQYLHNCR VAHLDIKPEN LLIDLRIPVP RVKLIDLEDA VQISGHFHIH HLLGNPEFAA 

      2830       2840       2850       2860       2870       2880 
PEVIQGIPVS LGTDIWSIGV LTYVMLSGVS PFLDESKEET CINVCRVDFS FPHEYFCGVS 

      2890       2900       2910       2920       2930       2940 
NAARDFINVI LQEDFRRRPT AATCLQHPWL QPHNGSYSKI PLDTSRLACF IERRKHQNDV 

      2950       2960 
RPIPNVKSYI VNRVNQGTSL SHNP 

« Hide

Isoform 2 [UniParc].

Checksum: 56F56B5B2D7DF990
Show »

FASTA2,375271,141
Isoform 3 [UniParc].

Checksum: 97FE34463CE6BF04
Show »

FASTA23326,709
Isoform 4 [UniParc].

Checksum: 1534A65BEB4A2EC6
Show »

FASTA67375,717
Isoform 5 [UniParc].

Checksum: FDA70F10D8DAA1DC
Show »

FASTA1,022117,971
Isoform 6 [UniParc].

Checksum: E610DD0659D34AC6
Show »

FASTA69478,009
Isoform 7 [UniParc].

Checksum: 012852FBADE5C66B
Show »

FASTA2,984338,885
Isoform 8 [UniParc].

Checksum: 409352E757B550F5
Show »

FASTA1,663192,182
Isoform 9 [UniParc].

Checksum: 5EE5FD961CE9AB09
Show »

FASTA1,654191,197

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2108-2964 (ISOFORM 2).
Strain: C57BL/6J and NOD.
Tissue: Egg, Embryonic head, Stomach, Thymus and Visual cortex.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 9).
Tissue: Brain.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2034-2042, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1722 AND SER-1771, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK008844 mRNA. Translation: BAB25925.1.
AK081504 mRNA. Translation: BAC38239.1.
AK088732 mRNA. Translation: BAC40535.1.
AK139581 mRNA. Translation: BAE24075.1.
AK158544 mRNA. Translation: BAE34552.1.
AK159031 mRNA. Translation: BAE34776.1.
CT010573 expand/collapse EMBL AC list , AC154524, AC155257, AC165079 Genomic DNA. Translation: CAM18305.1.
CT010573, AC154524, AC165079 Genomic DNA. Translation: CAM18306.1.
CT010573, AC154524, AC154588 Genomic DNA. Translation: CAM18307.1.
CT010573, AC154524, AC154588 Genomic DNA. Translation: CAM18308.1.
CT010573, AC154524, AC154588 Genomic DNA. Translation: CAM18309.1.
BC157950 mRNA. Translation: AAI57951.1.
BC172101 mRNA. Translation: AAI72101.1.
CCDSCCDS49836.1. [A2CG49-9]
RefSeqNP_001157740.1. NM_001164268.1. [A2CG49-9]
XP_006522445.1. XM_006522382.1. [A2CG49-8]
UniGeneMm.82274.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFWNMR-A2295-2354[»]
ProteinModelPortalA2CG49.
SMRA2CG49. Positions 172-392, 784-971, 1252-1555, 1618-1684, 1890-2219, 2296-2361, 2429-2944.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActA2CG49. 5 interactions.

PTM databases

PhosphoSiteA2CG49.

Proteomic databases

MaxQBA2CG49.
PaxDbA2CG49.
PRIDEA2CG49.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076810; ENSMUSP00000076088; ENSMUSG00000061751. [A2CG49-1]
ENSMUST00000089655; ENSMUSP00000087084; ENSMUSG00000061751. [A2CG49-8]
ENSMUST00000114953; ENSMUSP00000110603; ENSMUSG00000061751. [A2CG49-5]
ENSMUST00000114954; ENSMUSP00000110604; ENSMUSG00000061751. [A2CG49-5]
ENSMUST00000114960; ENSMUSP00000110611; ENSMUSG00000061751. [A2CG49-9]
GeneID545156.
KEGGmmu:545156.
UCSCuc007zar.2. mouse. [A2CG49-3]
uc007zas.1. mouse. [A2CG49-6]
uc007zat.1. mouse. [A2CG49-4]
uc007zav.1. mouse. [A2CG49-5]
uc007zax.2. mouse. [A2CG49-9]
uc012aew.1. mouse. [A2CG49-1]

Organism-specific databases

CTD8997.
MGIMGI:2685385. Kalrn.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108506.
HOVERGENHBG108598.
KOK15048.
OMADCFFPSG.
PhylomeDBA2CG49.
TreeFamTF318080.

Gene expression databases

ArrayExpressA2CG49.
BgeeA2CG49.
CleanExMM_KALRN.
GenevestigatorA2CG49.

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.
PF00018. SH3_1. 1 hit.
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. mouse.
EvolutionaryTraceA2CG49.
NextBio412318.
PROA2CG49.
SOURCESearch...

Entry information

Entry nameKALRN_MOUSE
AccessionPrimary (citable) accession number: A2CG49
Secondary accession number(s): A2CG50 expand/collapse secondary AC list , A2CG51, A2CG52, A2CG53, B2RXR5, Q3TXY8, Q3TYL1, Q3UTA5, Q8BTT9, Q8C4Q2, Q9CVA9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot