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P15882 (CHIN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-chimaerin
Alternative name(s):
A-chimaerin
Alpha-chimerin
N-chimerin
Short name=NC
Rho GTPase-activating protein 2
Gene names
Name:CHN1
Synonyms:ARHGAP2, CHN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance.

Subunit structure

Interacts with EPHA4; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation By similarity.

Tissue specificity

In neurons in brain regions that are involved in learning and memory processes.

Developmental stage

Increases in amount during brain development coincident with synaptogenesis.

Post-translational modification

Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent By similarity.

Involvement in disease

Duane retraction syndrome 2 (DURS2) [MIM:604356]: Duane retraction syndrome is a congenital eye movement disorder characterized by a failure of cranial nerve VI (the abducens nerve) to develop normally, resulting in restriction or absence of abduction, adduction, or both, and narrowing of the palpebral fissure and retraction of the globe on attempted adduction. Undiagnosed in children, it can lead to amblyopia, a permanent uncorrectable loss of vision.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 Rho-GAP domain.

Contains 1 SH2 domain.

Sequence caution

The sequence CAA35769.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha-2 (identifier: P15882-1)

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.
Isoform Alpha-1 (identifier: P15882-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: MALTLFDTDE...TGQDGVSEKR → MPSKESWSGR...QPLKLFAYSQ
Isoform 3 (identifier: P15882-3)

The sequence of this isoform differs from the canonical sequence as follows:
     184-209: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 459458N-chimaerin
PRO_0000056694

Regions

Domain49 – 13587SH2
Domain268 – 459192Rho-GAP
Zinc finger205 – 25551Phorbol-ester/DAG-type

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue3401Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 183183MALTL…VSEKR → MPSKESWSGRKTNRAAVHKS KQEGRQQDLLIAALGMKLGS PKSSVTIWQPLKLFAYSQ in isoform Alpha-1.
VSP_001636
Alternative sequence184 – 20926Missing in isoform 3.
VSP_043297
Natural variant201L → F in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). Ref.12
VAR_047940
Natural variant1261I → M in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro. Ref.12
VAR_047941
Natural variant1431Y → H in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). Ref.12
VAR_047942
Natural variant2231A → V in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). Ref.12
VAR_047943
Natural variant2281G → S in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. Ref.12
VAR_047944
Natural variant2521P → Q in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). Ref.12
VAR_047945
Natural variant3131E → K in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. Ref.12
VAR_047946

Secondary structure

................................................................. 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha-2 [UniParc].

Last modified July 11, 2002. Version 3.
Checksum: 04C4CC9BCC611389

FASTA45953,172
        10         20         30         40         50         60 
MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRITCTCEVE NRPKYYGREF HGMISREAAD 

        70         80         90        100        110        120 
QLLIVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD GKHFVGEKRF ESIHDLVTDG 

       130        140        150        160        170        180 
LITLYIETKA AEYIAKMTIN PIYEHVGYTT LNREPAYKKH MPVLKETHDE RDSTGQDGVS 

       190        200        210        220        230        240 
EKRLTSLVRR ATLKENEQIP KYEKIHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG 

       250        260        270        280        290        300 
LNVHKQCSKM VPNDCKPDLK HVKKVYSCDL TTLVKAHTTK RPMVVDMCIR EIESRGLNSE 

       310        320        330        340        350        360 
GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL PIPLITYDAY 

       370        380        390        400        410        420 
PKFIESAKIM DPDEQLETLH EALKLLPPAH CETLRYLMAH LKRVTLHEKE NLMNAENLGI 

       430        440        450 
VFGPTLMRSP ELDAMAALND IRYQRLVVEL LIKNEDILF 

« Hide

Isoform Alpha-1 [UniParc].

Checksum: 2E5BF139A231D13C
Show »

FASTA33438,196
Isoform 3 [UniParc].

Checksum: EB3E22E1C704D1BF
Show »

FASTA43350,034

References

« Hide 'large scale' references
[1]"Novel human brain cDNA encoding a 34,000 Mr protein n-chimaerin, related to both the regulatory domain of protein kinase C and BCR, the product of the breakpoint cluster region gene."
Hall C., Monfries C., Smith P., Lim H.H., Kozma R., Ahmed S., Vanniasingham V., Leung T., Lim L.
J. Mol. Biol. 211:11-16(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
Tissue: Retina.
[2]"Developmental regulation and neuronal expression of the mRNA of rat n-chimaerin, a p21rac GAP:cDNA sequence."
Lim H.H., Michael G.J., Smith P., Lim L., Hall C.
Biochem. J. 287:415-422(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Alpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testes."
Hall C., Sin W.C., Teo M., Michael G.J., Smith P., Dong J.M., Lim H.H., Manser E., Spurr N.K., Jones T.A., Lim L.
Mol. Cell. Biol. 13:4986-4998(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
[4]"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 ALPHA-1; ALPHA-2 AND 3).
Tissue: Brain, Hippocampus and Small intestine.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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 ALPHA-2).
Tissue: Eye.
[8]"Promoter region of the transcriptional unit for human alpha 1-chimaerin, a neuron-specific GTPase-activating protein for p21rac."
Dong J.M., Smith P., Hall C., Lim L.
Eur. J. Biochem. 227:636-646(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-1).
Tissue: Fibroblast.
[9]"Human brain n-chimaerin cDNA encodes a novel phorbol ester receptor."
Ahmed S., Kozma R., Monfries C., Hall C., Lim H.H., Smith P., Lim L.
Biochem. J. 272:767-773(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHORBOL-ESTER BINDING.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Crystal structure of human chimerin 1 (CHN1)."
Structural genomics consortium (SGC)
Submitted (JUL-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-459 IN COMPLEX WITH ZINC IONS.
[12]"Human CHN1 mutations hyperactivate alpha2-chimaerin and cause Duane's retraction syndrome."
Miyake N., Chilton J., Psatha M., Cheng L., Andrews C., Chan W.-M., Law K., Crosier M., Lindsay S., Cheung M., Allen J., Gutowski N.J., Ellard S., Young E., Iannaccone A., Appukuttan B., Stout J.T., Christiansen S. expand/collapse author list , Ciccarelli M.L., Baldi A., Campioni M., Zenteno J.C., Davenport D., Mariani L.E., Sahin M., Guthrie S., Engle E.C.
Science 321:839-843(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DURS2 PHE-20; MET-126; HIS-143; VAL-223; SER-228; GLN-252 AND LYS-313, CHARACTERIZATION OF VARIANTS DURS2 PHE-20; MET-126; HIS-143; VAL-223; SER-228; GLN-252 AND LYS-313.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51408 mRNA. Translation: CAA35769.1. Different initiation.
Z22641 mRNA. Translation: CAA80354.1.
AK055060 mRNA. Translation: BAG51458.1.
AK289941 mRNA. Translation: BAF82630.1.
AK300890 mRNA. Translation: BAG62531.1.
AC007435 Genomic DNA. No translation available.
AC018890 Genomic DNA. Translation: AAY14688.1.
AC020596 Genomic DNA. Translation: AAY14940.1.
CH471058 Genomic DNA. Translation: EAX11117.1.
CH471058 Genomic DNA. Translation: EAX11118.1.
CH471058 Genomic DNA. Translation: EAX11119.1.
BC011393 mRNA. Translation: AAH11393.1.
S75654 Genomic DNA. Translation: AAB33506.1.
PIRA48090.
I53329.
RefSeqNP_001020372.2. NM_001025201.3.
NP_001193531.1. NM_001206602.1.
NP_001813.1. NM_001822.5.
UniGeneHs.380138.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OSAX-ray1.80A260-459[»]
3CXLX-ray2.60A15-459[»]
ProteinModelPortalP15882.
SMRP15882. Positions 15-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107547. 6 interactions.
IntActP15882. 5 interactions.
MINTMINT-1173390.
STRING9606.ENSP00000386741.

PTM databases

PhosphoSiteP15882.

Polymorphism databases

DMDM21903393.

Proteomic databases

PaxDbP15882.
PRIDEP15882.

Protocols and materials databases

DNASU1123.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295497; ENSP00000295497; ENSG00000128656. [P15882-2]
ENST00000409156; ENSP00000386470; ENSG00000128656. [P15882-3]
ENST00000409900; ENSP00000386741; ENSG00000128656. [P15882-1]
GeneID1123.
KEGGhsa:1123.
UCSCuc002ujg.3. human. [P15882-2]
uc002uji.3. human. [P15882-1]
uc010zeq.2. human. [P15882-3]

Organism-specific databases

CTD1123.
GeneCardsGC02M175664.
HGNCHGNC:1943. CHN1.
HPAHPA036111.
MIM118423. gene.
604356. phenotype.
neXtProtNX_P15882.
Orphanet233. Duane retraction syndrome.
PharmGKBPA26473.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295484.
HOGENOMHOG000231926.
HOVERGENHBG080489.
InParanoidP15882.
OMAFRLYHDG.
OrthoDBEOG73JKVC.
PhylomeDBP15882.
TreeFamTF342052.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP15882.

Gene expression databases

ArrayExpressP15882.
BgeeP15882.
CleanExHS_CHN1.
GenevestigatorP15882.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.30.505.10. 1 hit.
InterProIPR020454. DAG/PE-bd.
IPR017356. N-chimaerin.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFPIRSF038015. N-chimaerin. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50238. RHOGAP. 1 hit.
PS50001. SH2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15882.
GenomeRNAi1123.
NextBio4662.
PROP15882.
SOURCESearch...

Entry information

Entry nameCHIN_HUMAN
AccessionPrimary (citable) accession number: P15882
Secondary accession number(s): A8K1M6 expand/collapse secondary AC list , B3KNU6, B4DV19, Q53SD6, Q53SH5, Q96FB0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 11, 2002
Last modified: April 16, 2014
This is version 154 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 2

Human chromosome 2: entries, gene names and cross-references to MIM