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Protein

N-chimaerin

Gene

Chn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein for p21-rac and a phorbol ester receptor. May play an important role in neuronal signal-transduction mechanisms (By similarity). Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri205 – 25551Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • GTPase activator activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • ephrin receptor signaling pathway Source: UniProtKB
  • intracellular signal transduction Source: InterPro
  • motor neuron axon guidance Source: UniProtKB
  • regulation of axonogenesis Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
N-chimaerin
Alternative name(s):
A-chimaerin
Alpha-chimerin
N-chimerin
Short name:
NC
Rho GTPase-activating protein 2
Gene namesi
Name:Chn1
Synonyms:Arhgap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1915674. Chn1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile but display a loss of coordination of limb movement which phenocopies the one of Epha4 mutant mice.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 459458N-chimaerinPRO_0000056695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei192 – 1921PhosphothreonineBy similarity
Modified residuei340 – 3401PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ91V57.
PaxDbiQ91V57.
PRIDEiQ91V57.

PTM databases

iPTMnetiQ91V57.
PhosphoSiteiQ91V57.

Expressioni

Gene expression databases

BgeeiQ91V57.
CleanExiMM_CHN1.
ExpressionAtlasiQ91V57. baseline and differential.
GenevisibleiQ91V57. MM.

Interactioni

Subunit structurei

Interacts with EPHA4; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation. May also interact with EPHB1 and EPHB2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Epha4Q031372EBI-1539203,EBI-1539152

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi224378. 3 interactions.
IntActiQ91V57. 1 interaction.
MINTiMINT-1341718.
STRINGi10090.ENSMUSP00000107655.

Structurei

3D structure databases

ProteinModelPortaliQ91V57.
SMRiQ91V57. Positions 15-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 13587SH2PROSITE-ProRule annotationAdd
BLAST
Domaini268 – 459192Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri205 – 25551Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

SH2 domain, Zinc-finger

Phylogenomic databases

eggNOGiKOG1453. Eukaryota.
ENOG410YM3I. LUCA.
GeneTreeiENSGT00840000129703.
HOGENOMiHOG000231926.
HOVERGENiHBG080489.
InParanoidiQ91V57.
OMAiAHHILEM.
OrthoDBiEOG73JKVC.
PhylomeDBiQ91V57.
TreeFamiTF342052.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR017356. CHN1/CHN2.
IPR020454. DAG/PE-bd.
IPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF038015. N-chimaerin. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q91V57-1) [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

        10         20         30         40         50
MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRVTCTCEVE NRPKYYGREY
60 70 80 90 100
HGMISREETD QLLSVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD
110 120 130 140 150
GKHFVGEKRF ESIHDLVTDG LITLYIETKA AEYIAKMTIN PIYEHIGYTT
160 170 180 190 200
LNREPAYKQH MAVLKETHDE KEATGQDGVS EKRLTSLVRR ATLKENEQIP
210 220 230 240 250
KYEKVHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG LNVHKQCSKM
260 270 280 290 300
VPNDCKPDLK HVKKVYSCDL TTLVKAHITK RPMVVDMCIR EIESRGLNSE
310 320 330 340 350
GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL
360 370 380 390 400
PIPLITYDAY PKFIESAKIM DPDEQLETLH EALRSLPPAH CETLRYLMAH
410 420 430 440 450
LKRVTLHEKE NLMSAENLGI VFGPTLMRSP ELDPMAALND IRYQRLVVEL

LIKNEDILF
Length:459
Mass (Da):53,193
Last modified:September 5, 2006 - v2
Checksum:iEE10CCDA8229C0B0
GO
Isoform 2 (identifier: Q91V57-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: MALTLFDTDE...TGQDGVSEKR → MPSKESWSGR...QPLKLFAYSQ

Show »
Length:334
Mass (Da):38,121
Checksum:i9EC5DA66D58A36C4
GO
Isoform 3 (identifier: Q91V57-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-249: Missing.

Note: No experimental confirmation available.
Show »
Length:210
Mass (Da):24,096
Checksum:i57F077920F5B0326
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531N → I in AAH54770 (PubMed:15489334).Curated
Sequence conflicti275 – 2751K → E in BAE28074 (PubMed:16141072).Curated
Sequence conflicti331 – 3311N → K in BAC33996 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 249249Missing in isoform 3. 1 PublicationVSP_020146Add
BLAST
Alternative sequencei1 – 183183MALTL…VSEKR → MPSKESWSGRKANRATVHKA KPEGRQQGLLIAALGMKLGS QKSSVTIWQPLKLFAYSQ in isoform 2. 3 PublicationsVSP_020145Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332069 mRNA. Translation: AAK56097.1.
AF332070 mRNA. Translation: AAK56098.1.
AK049943 mRNA. Translation: BAC33996.1.
AK007182 mRNA. Translation: BAB24888.1.
AK075606 mRNA. Translation: BAC35853.1.
AK147686 mRNA. Translation: BAE28074.1.
AL928889 Genomic DNA. Translation: CAM19182.1.
BC010825 mRNA. Translation: AAH10825.1.
BC024796 mRNA. Translation: AAH24796.1.
BC025023 mRNA. Translation: AAH25023.1.
BC054770 mRNA. Translation: AAH54770.1.
CCDSiCCDS16133.1. [Q91V57-2]
CCDS38145.1. [Q91V57-3]
CCDS50608.1. [Q91V57-1]
RefSeqiNP_001106717.2. NM_001113246.2. [Q91V57-1]
NP_083992.1. NM_029716.3. [Q91V57-3]
NP_786928.2. NM_175752.3. [Q91V57-2]
UniGeneiMm.257073.

Genome annotation databases

EnsembliENSMUST00000070579; ENSMUSP00000070301; ENSMUSG00000056486. [Q91V57-3]
ENSMUST00000102677; ENSMUSP00000099738; ENSMUSG00000056486. [Q91V57-2]
ENSMUST00000112024; ENSMUSP00000107655; ENSMUSG00000056486. [Q91V57-1]
ENSMUST00000180045; ENSMUSP00000137106; ENSMUSG00000056486. [Q91V57-3]
GeneIDi108699.
KEGGimmu:108699.
UCSCiuc008kda.2. mouse. [Q91V57-2]
uc008kdb.2. mouse. [Q91V57-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332069 mRNA. Translation: AAK56097.1.
AF332070 mRNA. Translation: AAK56098.1.
AK049943 mRNA. Translation: BAC33996.1.
AK007182 mRNA. Translation: BAB24888.1.
AK075606 mRNA. Translation: BAC35853.1.
AK147686 mRNA. Translation: BAE28074.1.
AL928889 Genomic DNA. Translation: CAM19182.1.
BC010825 mRNA. Translation: AAH10825.1.
BC024796 mRNA. Translation: AAH24796.1.
BC025023 mRNA. Translation: AAH25023.1.
BC054770 mRNA. Translation: AAH54770.1.
CCDSiCCDS16133.1. [Q91V57-2]
CCDS38145.1. [Q91V57-3]
CCDS50608.1. [Q91V57-1]
RefSeqiNP_001106717.2. NM_001113246.2. [Q91V57-1]
NP_083992.1. NM_029716.3. [Q91V57-3]
NP_786928.2. NM_175752.3. [Q91V57-2]
UniGeneiMm.257073.

3D structure databases

ProteinModelPortaliQ91V57.
SMRiQ91V57. Positions 15-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224378. 3 interactions.
IntActiQ91V57. 1 interaction.
MINTiMINT-1341718.
STRINGi10090.ENSMUSP00000107655.

PTM databases

iPTMnetiQ91V57.
PhosphoSiteiQ91V57.

Proteomic databases

MaxQBiQ91V57.
PaxDbiQ91V57.
PRIDEiQ91V57.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070579; ENSMUSP00000070301; ENSMUSG00000056486. [Q91V57-3]
ENSMUST00000102677; ENSMUSP00000099738; ENSMUSG00000056486. [Q91V57-2]
ENSMUST00000112024; ENSMUSP00000107655; ENSMUSG00000056486. [Q91V57-1]
ENSMUST00000180045; ENSMUSP00000137106; ENSMUSG00000056486. [Q91V57-3]
GeneIDi108699.
KEGGimmu:108699.
UCSCiuc008kda.2. mouse. [Q91V57-2]
uc008kdb.2. mouse. [Q91V57-1]

Organism-specific databases

CTDi1123.
MGIiMGI:1915674. Chn1.

Phylogenomic databases

eggNOGiKOG1453. Eukaryota.
ENOG410YM3I. LUCA.
GeneTreeiENSGT00840000129703.
HOGENOMiHOG000231926.
HOVERGENiHBG080489.
InParanoidiQ91V57.
OMAiAHHILEM.
OrthoDBiEOG73JKVC.
PhylomeDBiQ91V57.
TreeFamiTF342052.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

PROiQ91V57.
SOURCEiSearch...

Gene expression databases

BgeeiQ91V57.
CleanExiMM_CHN1.
ExpressionAtlasiQ91V57. baseline and differential.
GenevisibleiQ91V57. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR017356. CHN1/CHN2.
IPR020454. DAG/PE-bd.
IPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF038015. N-chimaerin. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: ILS and ISS.
  2. "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.
    , 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 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 2).
    Strain: C57BL/6J.
    Tissue: Brain, Colon and Eye.
  5. "Rac-GAP alpha-chimerin regulates motor-circuit formation as a key mediator of EphrinB3/EphA4 forward signaling."
    Iwasato T., Katoh H., Nishimaru H., Ishikawa Y., Inoue H., Saito Y.M., Ando R., Iwama M., Takahashi R., Negishi M., Itohara S.
    Cell 130:742-753(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, INTERACTION WITH EPHA4.
  6. "alpha2-Chimaerin is an essential EphA4 effector in the assembly of neuronal locomotor circuits."
    Beg A.A., Sommer J.E., Martin J.H., Scheiffele P.
    Neuron 55:768-778(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EPHA4 SIGNALING, INTERACTION WITH EPHA4; EPHB1 AND EPHB2, PHOSPHORYLATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiCHIN_MOUSE
AccessioniPrimary (citable) accession number: Q91V57
Secondary accession number(s): A2ATM0
, Q3UGY3, Q7TQE5, Q8BWU6, Q9D9B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: September 5, 2006
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.