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Reviewed, UniProtKB/Swiss-Prot P97924 (KALRN_RAT)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kalirin
    EC=2.7.11.1
Alternative name(s):
    Huntingtin-associated protein-interacting protein
    Protein Duo
    Serine/threonine kinase with Dbl- and pleckstrin homology domain
    PAM COOH-terminal interactor protein 10
      Short name=P-CIP10
Gene names
Name: Kalrn
Synonyms: Duo, Hapip
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2959 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Isoforms 1 and 7 are necessary for neuronal development and axonal outgrowth. Isoform 6 is required for dendritic spine formation. Ref.3 Ref.5 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Subunit structure

Interacts with the C-terminal of peptidylglycine alpha-amidating monooxygenase (PAM) and with the huntingtin-associated protein 1 (HAP1). Ref.2 Ref.8

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Note: Isoform 6 is largely associated with synaptosomal membranes and to punctate structures in cortical neurons. Isoforms 1 and 7 are expressed in neuronal cell bodies, isoform 7 is also found in neuronal processes. Ref.3 Ref.4

Tissue specificity

Highly expressed in the brain and nervous system. Isoform 6 is highly enriched in the postsynaptic density fraction of the cerebral cortex. Ref.3 Ref.4

Developmental stage

Isoforms 1 and 7 are prevelant 2 dpp, isoform 6 is not detectable until 2 weeks after birth. Ref.7

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. Ref.7 Ref.8

Post-translational modification

Autophosphorylated By similarity.

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative initiation
Alternative splicing
   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 term3D-structure
Gene Ontology (GO)
   Biological processaxonogenesis

Inferred from direct assay. Source: RGD

intracellular signaling cascade

Inferred from direct assay. Source: HGNC

protein amino acid phosphorylation

Inferred from electronic annotation. Source: InterPro

regulation of Rho protein signal transduction

Inferred from electronic annotation. Source: InterPro

regulation of dendrite development

Inferred from direct assay. Source: RGD

vesicle-mediated transport Ref.6

Inferred from direct assay. Source: RGD

   Cellular componentcell soma Ref.4

Inferred from direct assay. Source: RGD

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection Ref.4

Inferred from direct assay. Source: RGD

perinuclear region of cytoplasm Ref.4

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Rho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.1 Ref.6

Inferred from physical interaction. Source: IntAct

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PamP974671EBI-1397166,EBI-1397216From a different organism.

Alternative products

This entry describes 8 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P97924-1)

Also known as: Kalirin-12A;

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: P97924-2)

Also known as: Kalirin-8B; P-CIP10B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVLS → MNPPEGASEEGGAADSDVDAFFRT
     1860-1899: TLEGGSYRGS...LEEEQKAKAL → VSGHAGGSRV...HPDFVYSNCI
     1900-2959: Missing.
Note: Produced by alternative splicing.
Isoform 3 (identifier: P97924-3)

Also known as: Kalirin-8A; P-CIP10A;

The sequence of this isoform differs from the canonical sequence as follows:
     1860-1899: TLEGGSYRGS...LEEEQKAKAL → VSGHAGGSRV...HPDFVYSNCI
     1900-2959: Missing.
Note: Produced by alternative splicing.
Isoform 4 (identifier: P97924-4)

The sequence of this isoform differs from the canonical sequence as follows:
     923-923: E → ESLFHATSLQ
Note: Produced by alternative splicing.
Isoform 5 (identifier: P97924-5)

Also known as: Delta Kalirin-7;

The sequence of this isoform differs from the canonical sequence as follows:
     1-623: Missing.
     1617-1636: LSGGCELTVVLQDFSAAHSS → DGNLVPRWHLGPGDPFSTYV
     1637-2959: Missing.
Note: Produced by alternative initiation at Met-624 of isoform 6.
Isoform 6 (identifier: P97924-6)

Also known as: Kalirin-7; HAPIP;

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVLS → MTDRFWDQWYLWYLRLLRLLDR
     1617-1636: LSGGCELTVVLQDFSAAHSS → DGNLVPRWHLGPGDPFSTYV
     1637-2959: Missing.
Note: Produced by alternative splicing.
Isoform 7 (identifier: P97924-7)

Also known as: Kalirin-9A;

The sequence of this isoform differs from the canonical sequence as follows:
     2372-2376: KSCSW → TLLKP
     2377-2959: Missing.
Note: Produced by alternative splicing.
Isoform 8 (identifier: P97924-8)

The sequence of this isoform differs from the canonical sequence as follows:
     705-718: DSAVSNNKTPHSSS → SAWAVIPVGNASG
     719-2959: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 29592959Kalirin
PRO_0000080956

Regions

Domain17 – 162146CRAL-TRIO
Repeat170 – 290121Spectrin 1
Repeat292 – 398107Spectrin 2
Repeat518 – 624107Spectrin 3
Repeat872 – 977106Spectrin 4
Repeat1103 – 1209107Spectrin 5
Domain1254 – 1429176DH 1
Domain1441 – 1553113PH 1
Domain1619 – 168466SH3 1
Domain1901 – 2076176DH 2
Domain2088 – 2198111PH 2
Domain2293 – 235866SH3 2
Domain2444 – 253794Ig-like C2-type
Domain2542 – 263392Fibronectin type-III
Domain2657 – 2911255Protein kinase
Nucleotide binding2663 – 26719ATP By similarity
Compositional bias664 – 6696Poly-Gln

Sites

Active site27761Proton acceptor By similarity
Binding site26861ATP By similarity

Amino acid modifications

Modified residue17231Phosphoserine By similarity
Modified residue17261Phosphoserine By similarity
Modified residue17291Phosphoserine By similarity
Modified residue17461Phosphoserine By similarity
Modified residue17721Phosphoserine By similarity
Modified residue17901Phosphoserine By similarity
Modified residue22091Phosphoserine By similarity
Modified residue22341Phosphoserine By similarity
Disulfide bond2465 ↔ 2521 By similarity

Natural variations

Alternative sequence1 – 623623Missing in isoform 5.
VSP_028893
Alternative sequence1 – 44MVLS → MNPPEGASEEGGAADSDVDA FFRT in isoform 2.
VSP_028891
Alternative sequence1 – 44MVLS → MTDRFWDQWYLWYLRLLRLL DR in isoform 6.
VSP_028892
Alternative sequence705 – 71814DSAVS…PHSSS → SAWAVIPVGNASG in isoform 8.
VSP_028894
Alternative sequence719 – 29592241Missing in isoform 8.
VSP_028895
Alternative sequence9231E → ESLFHATSLQ in isoform 4.
VSP_028896
Alternative sequence1617 – 163620LSGGC…AAHSS → DGNLVPRWHLGPGDPFSTYV in isoform 5 and isoform 6.
VSP_028897
Alternative sequence1637 – 29591323Missing in isoform 5 and isoform 6.
VSP_028898
Alternative sequence1860 – 189940TLEGG…KAKAL → VSGHAGGSRVLPLTSMWLPG PQLGPQISYLHPDFVYSNCI in isoform 2 and isoform 3.
VSP_028899
Alternative sequence1900 – 29591060Missing in isoform 2 and isoform 3.
VSP_028900
Alternative sequence2372 – 23765KSCSW → TLLKP in isoform 7.
VSP_028901
Alternative sequence2377 – 2959583Missing in isoform 7.
VSP_028902

Experimental info

Sequence conflict461T → S in AAT39517. Ref.5
Sequence conflict621N → Y in AAT39517. Ref.5

Secondary structure

.......... 2959
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Kalirin-12A) [UniParc].

Last modified October 23, 2007. Version 3.
Checksum: 1A3C6770D1CBCC1F

FASTA2,959336,587
        10         20         30         40         50         60 
MVLSGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL TFPARTNHDR IRQEDLRKLV 

        70         80         90        100        110        120 
TNLASVPSED 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 TEARDSAVSN NKTPHSSSIS 

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

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

       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 
GKYRYTLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA NHEVNEEKRK 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 SAAHSSELSI QVGQTVELLE RPSERPGWCL VRTTERSPPQ EGLVPSSTLC 

      1690       1700       1710       1720       1730       1740 
ISHSRSSVEM DCFFPLVKDS YSHSSGENGG KSESVANLQS QPSLNSIHSS PGPKRSTNTL 

      1750       1760       1770       1780       1790       1800 
KKWLTSPVRR LNSGKADGNI KKQKKVRDGR KSFDLGSPKP GDETTPQGDS ADEKSKKGWG 

      1810       1820       1830       1840       1850       1860 
EDEPDEESHT PLPPPMKIFD NDPTQDEMSS LLAARQAPTD VPTAADLVSA IEKLVKSKLT 

      1870       1880       1890       1900       1910       1920 
LEGGSYRGSL KDPTVCLNEG MAPPTPPRNL EEEQKAKALR GRMFVLNELV QTEKDYVKDL 

      1930       1940       1950       1960       1970       1980 
GIVVEGFMKR IEEKGVPEDM RGKEKIVFGN IHQIYDWHKD FFLAELEKCI QEQDRLAQLF 

      1990       2000       2010       2020       2030       2040 
IKHERKLHIY VWYCQNKPRS EYIVAEYDAY FEEVKQEINQ RLTLSDFLIK PIQRITKYQL 

      2050       2060       2070       2080       2090       2100 
LLKDFLRYSE KAGLECSDIE KAVELMCLVP KRCNDMMNLG RLQGFEGTLT AQGKLLQQDT 

      2110       2120       2130       2140       2150       2160 
FYVIELDAGM QSRTKERRVF LFEQIVIFSE LLRKGSLTPG YMFKRSIKMN YLVLEEDVDD 

      2170       2180       2190       2200       2210       2220 
DPCKFALMNR ETSERVILQA ANSDIQQAWV QDINQVLETQ RDFLNALQSP IEYQRKERST 

      2230       2240       2250       2260       2270       2280 
AVIRSQPPRV PQASPRPYSS VPVGSEKPPK GSSYNPPLPP LKISTSNGSP GFDYHQPGDK 

      2290       2300       2310       2320       2330       2340 
FDASKQNDLG GCNGTSTMAV IKDYYALKEN EICVSQGEVV QVLAVNQQNM CLVYQPASDH 

      2350       2360       2370       2380       2390       2400 
SPAAEGWVPG SILAPLTKAT APAESSDESI KKSCSWHTLR MRKRADVENT GKNEATGPRK 

      2410       2420       2430       2440       2450       2460 
PKDILGNKAS VKETNSSEES ECDDLDPNTS MEILNPNFIQ EVAPEFLVPL VDVTCLLGDT 

      2470       2480       2490       2500       2510       2520 
VLLQCKACGR PKPTITWKGP DQNILDTDNS SATYTISSCD SGESTLKICN LMPQDSGIYT 

      2530       2540       2550       2560       2570       2580 
CIATNDHGTA STSATVKVQG VPAAPNRPIA QERSCTSVIL RWLPPASTGN CTISGYTVEY 

      2590       2600       2610       2620       2630       2640 
REEGSQVWQQ SVASTLDTYL VIEDLSPGCP YQFRVSASNP WGISLPSEPS EFVHLPEYDA 

      2650       2660       2670       2680       2690       2700 
AADGATISWK ENFDSAYTEL NEIGRGRFSI VKKCIHKATR KDVAVKFVSK KMKKKEQAAH 

      2710       2720       2730       2740       2750       2760 
EAALLQHLQH PQYVTLHDTY ESPTSYILIL ELMDDGRLLD YLMNHDELME EKVAFYIRDI 

      2770       2780       2790       2800       2810       2820 
MEALQYLHNC RVAHLDIKPE NLLIDLRIPV PRVKLIDLED AVQISGHFHI HHLLGNPEFA 

      2830       2840       2850       2860       2870       2880 
APEVIQGIPV SLGTDIWSIG VLTYVMLSGV SPFLDESKEE TCINVCRVDF SFPHEYFCGV 

      2890       2900       2910       2920       2930       2940 
SNAARDFINV ILQEDFRRRP TAATCLQHPW LQPHNGSYSK IPLDTSRLAC FIERRKHQND 

      2950 
VRPIPNVKSY IVNRVNQGT 

« Hide

Isoform 2 (Kalirin-8B) (P-CIP10B).

Checksum: E4DBB818E890F453
Show »

FASTA1,919218,841
Isoform 3 (Kalirin-8A) (P-CIP10A).

Checksum: E3545E4CB9F59A1E
Show »

FASTA1,899216,819
Isoform 4.

Checksum: 6B8B3C0E9FD8CDDC
Show »

FASTA2,968337,572
Isoform 5 (Delta Kalirin-7).

Checksum: 8C24887FBE316B64
Show »

FASTA1,013116,939
Isoform 6 (Kalirin-7) (HAPIP).

Checksum: C2C267C2226EF596
Show »

FASTA1,654191,116
Isoform 7 (Kalirin-9A).

Checksum: 3AEC5B08F483E75C
Show »

FASTA2,376271,353
Isoform 8.

Checksum: 08AB2C8397ED9654
Show »

FASTA71781,973

References

[1]"Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme."
Alam M.R., Caldwell B.D., Johnson R.C., Darlington D.N., Mains R.E., Eipper B.A.
J. Biol. Chem. 271:28636-28640(1996) [PubMed: 8910496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Hippocampus.
[2]"Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine alpha-amidating monooxygenase, an integral membrane peptide-processing enzyme."
Alam M.R., Johnson R.C., Darlington D.N., Hand T.A., Mains R.E., Eipper B.A.
J. Biol. Chem. 272:12667-12675(1997) [PubMed: 9139723] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH PAM.
Tissue: Hippocampus.
[3]"An isoform of kalirin, a brain-specific GDP/GTP exchange factor, is enriched in the postsynaptic density fraction."
Penzes P., Johnson R.C., Alam M.R., Kambampati V., Mains R.E., Eipper B.A.
J. Biol. Chem. 275:6395-6403(2000) [PubMed: 10692441] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Isoforms of kalirin, a neuronal Dbl family member, generated through use of different 5'- and 3'-ends along with an internal translational initiation site."
Johnson R.C., Penzes P., Eipper B.A., Mains R.E.
J. Biol. Chem. 275:19324-19333(2000) [PubMed: 10777487] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 5 AND 7), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Induction of lamellipodia by Kalirin does not require its guanine nucleotide exchange factor activity."
Schiller M.R., Blangy A., Huang J., Mains R.E., Eipper B.A.
Exp. Cell Res. 307:402-417(2005) [PubMed: 15950621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), FUNCTION.
[6]"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: 9285789] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 638-1216 (ISOFORM 4).
Tissue: Brain cortex and Hippocampus.
[7]"Distinct roles for the two Rho GDP/GTP exchange factor domains of kalirin in regulation of neurite growth and neuronal morphology."
Penzes P., Johnson R.C., Kambampati V., Mains R.E., Eipper B.A.
J. Neurosci. 21:8426-8434(2001) [PubMed: 11606631] [Abstract]
Cited for: FUNCTION, DOMAIN, DEVELOPMENTAL STAGE.
[8]"Regulation of RhoGEF activity by intramolecular and intermolecular SH3 domain interactions."
Schiller M.R., Chakrabarti K., King G.F., Schiller N.I., Eipper B.A., Maciejewski M.W.
J. Biol. Chem. 281:18774-18786(2006) [PubMed: 16644733] [Abstract]
Cited for: STRUCTURE BY NMR OF 1617-1707, DOMAIN, INTERACTION WITH CRK1.

Cross-references

Sequence databases

U88156 mRNA. Translation: AAB66366.1.
U88157 mRNA. Translation: AAB66367.1.
AF230644 mRNA. Translation: AAF69144.1.
AF229255 mRNA. Translation: AAF66014.1.
AF232668 mRNA. Translation: AAF66018.1.
AF232669 mRNA. Translation: AAF66019.1.
AY621095 mRNA. Translation: AAT39517.1.
U94189 mRNA. Translation: AAC15790.1.
IPIIPI00200504.
IPI00400488.
IPI00476515.
IPI00567732.
IPI00869510.
IPI00869788.
IPI00870072.
IPI00870649.
PIRT32732.
T42098.
RefSeqNP_114451.1.
UniGeneRn.87882

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1U3ONMR-A1617-1686[»]
SMRP97924. Positions 1272-1575.
ModBaseSearch...

Protein-protein interaction databases

IntActP97924. 2 interactions.

PTM databases

PhosphoSiteP97924.

Proteomic databases

PRIDEP97924.

Genome annotation databases

EnsemblENSRNOG00000001706. Rattus norvegicus. [Contig view]
GeneID84009.
KEGGrno:84009.

Organism-specific databases

RGD621865. Hapip.

Phylogenomic databases

HOVERGENP97924.

Enzyme and pathway databases

BRENDA2.7.11.1. 248.

Gene expression databases

ArrayExpressP97924.
GermOnlineENSRNOG00000001706. Rattus norvegicus.

Family and domain databases

InterProIPR001251. CRAL_bd_TRIO_C.
IPR000219. DH-domain.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR001331. GDS_CDC24_CS.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
Gene3DG3DSA:3.40.525.10. CRAL_bd_TRIO_C. 1 hit.
G3DSA:2.60.40.30. FN_III-like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.30.29.30. PH_type. 2 hits.
G3DSA:1.20.900.10. RhoGEF. 2 hits.
PfamPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
PF00169. PH. 2 hits.
PF00069. Pkinase. 1 hit.
PF00621. RhoGEF. 2 hits.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
PF00435. Spectrin. 5 hits.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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]
PROSITEPS50191. CRAL_TRIO. 1 hit.
PS00741. DH_1. False negative.
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 Resources

NextBio616533.

Entry information

Entry nameKALRN_RAT
AccessionPrimary (citable) accession number: P97924
Secondary accession number(s): O70135 expand/collapse secondary AC list , Q6IV51, Q9JIF1, Q9JIF2, Q9JIG0, Q9JIH3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 23, 2007
Last modified: June 16, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents