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P15882

- CHIN_HUMAN

UniProt

P15882 - CHIN_HUMAN

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Protein
N-chimaerin
Gene
CHN1, ARHGAP2, CHN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri205 – 25551Phorbol-ester/DAG-type
Add
BLAST

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. SH3/SH2 adaptor activity Source: ProtInc
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. ephrin receptor signaling pathway Source: UniProtKB
  2. motor neuron axon guidance Source: UniProtKB
  3. positive regulation of signal transduction Source: GOC
  4. regulation of Rac GTPase activity Source: Ensembl
  5. regulation of axonogenesis Source: UniProtKB
  6. regulation of small GTPase mediated signal transduction Source: Reactome
  7. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
SignaLinkiP15882.

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, CHN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:1943. CHN1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201L → 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). 1 Publication
VAR_047940
Natural varianti126 – 1261I → M in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro. 1 Publication
VAR_047941
Natural varianti143 – 1431Y → 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). 1 Publication
VAR_047942
Natural varianti223 – 2231A → 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). 1 Publication
VAR_047943
Natural varianti228 – 2281G → S in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
VAR_047944
Natural varianti252 – 2521P → 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). 1 Publication
VAR_047945
Natural varianti313 – 3131E → K in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
VAR_047946

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi604356. phenotype.
Orphaneti233. Duane retraction syndrome.
PharmGKBiPA26473.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 459458N-chimaerin
PRO_0000056694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei340 – 3401Phosphothreonine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15882.
PaxDbiP15882.
PRIDEiP15882.

PTM databases

PhosphoSiteiP15882.

Expressioni

Tissue specificityi

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

Developmental stagei

Increases in amount during brain development coincident with synaptogenesis.

Gene expression databases

ArrayExpressiP15882.
BgeeiP15882.
CleanExiHS_CHN1.
GenevestigatoriP15882.

Organism-specific databases

HPAiHPA036111.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107547. 6 interactions.
IntActiP15882. 5 interactions.
MINTiMINT-1173390.
STRINGi9606.ENSP00000386741.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 268
Helixi56 – 638
Beta strandi69 – 746
Beta strandi76 – 783
Beta strandi82 – 876
Beta strandi89 – 968
Beta strandi98 – 10710
Helixi113 – 12917
Helixi131 – 1366
Turni143 – 1453
Beta strandi146 – 1483
Helixi164 – 1663
Beta strandi208 – 2114
Turni220 – 2223
Beta strandi228 – 2303
Beta strandi233 – 2364
Turni237 – 2393
Helixi245 – 2484
Helixi257 – 2615
Helixi270 – 2778
Helixi283 – 29513
Turni300 – 3045
Helixi309 – 32214
Helixi323 – 3253
Turni330 – 3323
Helixi336 – 34813
Turni357 – 3593
Helixi360 – 3689
Helixi372 – 38413
Helixi388 – 40619
Helixi408 – 4114
Helixi415 – 42612
Helixi434 – 45320
Helixi455 – 4584

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OSAX-ray1.80A260-459[»]
3CXLX-ray2.60A15-459[»]
ProteinModelPortaliP15882.
SMRiP15882. Positions 15-459.

Miscellaneous databases

EvolutionaryTraceiP15882.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 13587SH2
Add
BLAST
Domaini268 – 459192Rho-GAP
Add
BLAST

Sequence similaritiesi

Contains 1 Rho-GAP domain.
Contains 1 SH2 domain.

Keywords - Domaini

SH2 domain, Zinc-finger

Phylogenomic databases

eggNOGiNOG295484.
HOGENOMiHOG000231926.
HOVERGENiHBG080489.
InParanoidiP15882.
OMAiNREPAHK.
OrthoDBiEOG73JKVC.
PhylomeDBiP15882.
TreeFamiTF342052.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR020454. 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]
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. Align

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

MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRITCTCEVE NRPKYYGREF    50
HGMISREAAD QLLIVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD 100
GKHFVGEKRF ESIHDLVTDG LITLYIETKA AEYIAKMTIN PIYEHVGYTT 150
LNREPAYKKH MPVLKETHDE RDSTGQDGVS EKRLTSLVRR ATLKENEQIP 200
KYEKIHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG LNVHKQCSKM 250
VPNDCKPDLK HVKKVYSCDL TTLVKAHTTK RPMVVDMCIR EIESRGLNSE 300
GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL 350
PIPLITYDAY PKFIESAKIM DPDEQLETLH EALKLLPPAH CETLRYLMAH 400
LKRVTLHEKE NLMNAENLGI VFGPTLMRSP ELDAMAALND IRYQRLVVEL 450
LIKNEDILF 459
Length:459
Mass (Da):53,172
Last modified:July 11, 2002 - v3
Checksum:i04C4CC9BCC611389
GO
Isoform Alpha-1 (identifier: P15882-2) [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):38,196
Checksum:i2E5BF139A231D13C
GO
Isoform 3 (identifier: P15882-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-209: Missing.

Note: No experimental confirmation available.

Show »
Length:433
Mass (Da):50,034
Checksum:iEB3E22E1C704D1BF
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201L → 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). 1 Publication
VAR_047940
Natural varianti126 – 1261I → M in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro. 1 Publication
VAR_047941
Natural varianti143 – 1431Y → 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). 1 Publication
VAR_047942
Natural varianti223 – 2231A → 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). 1 Publication
VAR_047943
Natural varianti228 – 2281G → S in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
VAR_047944
Natural varianti252 – 2521P → 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). 1 Publication
VAR_047945
Natural varianti313 – 3131E → K in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
VAR_047946

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 183183MALTL…VSEKR → MPSKESWSGRKTNRAAVHKS KQEGRQQDLLIAALGMKLGS PKSSVTIWQPLKLFAYSQ in isoform Alpha-1.
VSP_001636Add
BLAST
Alternative sequencei184 – 20926Missing in isoform 3.
VSP_043297Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS46454.1. [P15882-3]
CCDS46455.1. [P15882-1]
CCDS56147.1. [P15882-2]
PIRiA48090.
I53329.
RefSeqiNP_001020372.2. NM_001025201.3. [P15882-3]
NP_001193531.1. NM_001206602.1. [P15882-2]
NP_001813.1. NM_001822.5. [P15882-1]
UniGeneiHs.380138.

Genome annotation databases

EnsembliENST00000295497; ENSP00000295497; ENSG00000128656. [P15882-2]
ENST00000409156; ENSP00000386470; ENSG00000128656. [P15882-3]
ENST00000409900; ENSP00000386741; ENSG00000128656. [P15882-1]
GeneIDi1123.
KEGGihsa:1123.
UCSCiuc002ujg.3. human. [P15882-2]
uc002uji.3. human. [P15882-1]
uc010zeq.2. human. [P15882-3]

Polymorphism databases

DMDMi21903393.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS46454.1. [P15882-3 ]
CCDS46455.1. [P15882-1 ]
CCDS56147.1. [P15882-2 ]
PIRi A48090.
I53329.
RefSeqi NP_001020372.2. NM_001025201.3. [P15882-3 ]
NP_001193531.1. NM_001206602.1. [P15882-2 ]
NP_001813.1. NM_001822.5. [P15882-1 ]
UniGenei Hs.380138.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OSA X-ray 1.80 A 260-459 [» ]
3CXL X-ray 2.60 A 15-459 [» ]
ProteinModelPortali P15882.
SMRi P15882. Positions 15-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107547. 6 interactions.
IntActi P15882. 5 interactions.
MINTi MINT-1173390.
STRINGi 9606.ENSP00000386741.

PTM databases

PhosphoSitei P15882.

Polymorphism databases

DMDMi 21903393.

Proteomic databases

MaxQBi P15882.
PaxDbi P15882.
PRIDEi P15882.

Protocols and materials databases

DNASUi 1123.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295497 ; ENSP00000295497 ; ENSG00000128656 . [P15882-2 ]
ENST00000409156 ; ENSP00000386470 ; ENSG00000128656 . [P15882-3 ]
ENST00000409900 ; ENSP00000386741 ; ENSG00000128656 . [P15882-1 ]
GeneIDi 1123.
KEGGi hsa:1123.
UCSCi uc002ujg.3. human. [P15882-2 ]
uc002uji.3. human. [P15882-1 ]
uc010zeq.2. human. [P15882-3 ]

Organism-specific databases

CTDi 1123.
GeneCardsi GC02M175664.
GeneReviewsi CHN1.
HGNCi HGNC:1943. CHN1.
HPAi HPA036111.
MIMi 118423. gene.
604356. phenotype.
neXtProti NX_P15882.
Orphaneti 233. Duane retraction syndrome.
PharmGKBi PA26473.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295484.
HOGENOMi HOG000231926.
HOVERGENi HBG080489.
InParanoidi P15882.
OMAi NREPAHK.
OrthoDBi EOG73JKVC.
PhylomeDBi P15882.
TreeFami TF342052.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
SignaLinki P15882.

Miscellaneous databases

EvolutionaryTracei P15882.
GenomeRNAii 1123.
NextBioi 4662.
PROi P15882.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15882.
Bgeei P15882.
CleanExi HS_CHN1.
Genevestigatori P15882.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR020454. 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 ]
Pfami PF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PIRSFi PIRSF038015. N-chimaerin. 1 hit.
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50238. RHOGAP. 1 hit.
PS50001. SH2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiCHIN_HUMAN
AccessioniPrimary (citable) accession number: P15882
Secondary accession number(s): A8K1M6
, B3KNU6, B4DV19, Q53SD6, Q53SH5, Q96FB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 11, 2002
Last modified: September 3, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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