Reviewed, UniProtKB/Swiss-Prot P52757 (CHIO_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-chimaerin
Alternative name(s):
    Beta-chimerin
    Rho GTPase-activating protein 3

Gene names

Name:	CHN2
Synonyms:	ARHGAP3, BCH

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors.
Subcellular location	Membrane; Peripheral membrane proteinPotential.
Tissue specificity	Highest levels in the brain and pancreas. Also expressed in the heart, placenta, and weakly in the kidney and liver. Expression is much reduced in the malignant gliomas, compared to normal brain or low-grade astrocytomas.
Sequence similarities	Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 Rho-GAP domain. Contains 1 SH2 domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Phorbol-ester binding SH2 domain Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	GTPase activation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTPase activator activity Ref.2 Traceable author statement. Source: ProtInc SH3/SH2 adaptor activity Ref.1 Traceable author statement. Source: ProtInc diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]

Isoform Beta-2 (identifier: P52757-1)

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 Beta-1 (identifier: P52757-2)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 468

468

Beta-chimaerin

PRO_0000056697

Regions

Domain

59 – 127

69

SH2

Domain

277 – 468

192

Rho-GAP

Zinc finger

214 – 264

51

Phorbol-ester/DAG-type

Natural variations

Natural variant

204

1

H → R: dbSNP rs3750103.

VAR_022118

Experimental info

Sequence conflict

1 – 6

6

MAASSN → MRLL Ref.1

Secondary structure

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468

Helix Strand Turn

Details...

Helix

29 – 36

8

Beta strand

58 – 63

6

Helix

66 – 73

8

Beta strand

79 – 84

6

Beta strand

86 – 88

3

Beta strand

92 – 98

7

Beta strand

101 – 104

4

Beta strand

108 – 114

7

Beta strand

116 – 118

3

Helix

125 – 138

14

Helix

141 – 146

6

Helix

153 – 155

3

Beta strand

156 – 161

6

Turn

229 – 231

3

Turn

237 – 240

4

Beta strand

246 – 248

3

Helix

255 – 257

3

Turn

266 – 269

4

Helix

279 – 286

8

Helix

292 – 303

12

Beta strand

306 – 308

3

Turn

309 – 313

5

Helix

318 – 328

11

Turn

331 – 334

4

Beta strand

339 – 342

4

Helix

346 – 358

13

Helix

369 – 373

5

Turn

374 – 377

4

Helix

381 – 392

12

Helix

397 – 405

9

Turn

406 – 410

5

Helix

411 – 414

4

Turn

415 – 419

5

Helix

424 – 431

8

Turn

432 – 434

3

Helix

445 – 448

4

Helix

450 – 462

13

Helix

464 – 467

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-2 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 63254958E0B5804C	FASTA	468	53,924
	10 20 30 40 50 60 MAASSNSSLS GSSVSSDAEE YQPPIWKSYL YQLQQEAPRP KRIICPREVE NRPKYYGREF 70 80 90 100 110 120 HGIISREQAD ELLGGVEGAY ILRESQRQPG CYTLALRFGN QTLNYRLFHD GKHFVGEKRF 130 140 150 160 170 180 ESIHDLVTDG LITLYIETKA AEYISKMTTN PIYEHIGYAT LLREKVSRRL SRSKNEPRKT 190 200 210 220 230 240 NVTHEEHTAV EKISSLVRRA ALTHNDNHFN YEKTHNFKVH TFRGPHWCEY CANFMWGLIA 250 260 270 280 290 300 QGVRCSDCGL NVHKQCSKHV PNDCQPDLKR IKKVYCCDLT TLVKAHNTQR PMVVDICIRE 310 320 330 340 350 360 IEARGLKSEG LYRVSGFTEH IEDVKMAFDR DGEKADISAN VYPDINIITG ALKLYFRDLP 370 380 390 400 410 420 IPVITYDTYS KFIDAAKISN ADERLEAVHE VLMLLPPAHY ETLRYLMIHL KKVTMNEKDN 430 440 450 460 FMNAENLGIV FGPTLMRPPE DSTLTTLHDM RYQKLIVQIL IENEDVLF
	Isoform Beta-1 (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cerebellar beta 2-chimaerin, a GTPase-activating protein for p21 ras-related rac is specifically expressed in granule cells and has a unique N-terminal SH2 domain." Leung T., How B.-E., Manser E., Lim L. J. Biol. Chem. 269:12888-12892(1994) [PubMed: 8175705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cerebellum.
[2]	"Identification and characterization of human beta 2-chimaerin: association with malignant transformation in astrocytoma." Yuan S., Miller D.W., Barnett G.H., Hahn J.F., Williams B.R.G. Cancer Res. 55:3456-3461(1995) [PubMed: 7614486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L29126 mRNA. Translation: AAA19191.1.
U07223 mRNA. Translation: AAA16836.1.
U28926 mRNA. Translation: AAA86528.1.
AC004417 Genomic DNA. Translation: AAC06177.1.
AC007255 Genomic DNA. Translation: AAS07498.1.
BC112155 mRNA. Translation: AAI12156.1.

PIR

A53764.

RefSeq

NP_001035025.1.
NP_004058.1.

UniGene

Hs.654611
Hs.654753
Hs.663145
Hs.705872

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XA6	X-ray	3.20	A	7-468	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P52757.

PTM databases

PhosphoSite

P52757.

Genome annotation databases

Ensembl

ENSG00000106069. Homo sapiens. [Contig view]

GeneID

1124.

KEGG

hsa:1124.

Organism-specific databases

H-InvDB

HIX0006558.

HGNC

HGNC:1944. CHN2.

MIM

602857. gene.

PharmGKB

PA26474.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P52757.

HOVERGEN

P52757.

Enzyme and pathway databases

Reactome

REACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpress

P52757.

CleanEx

HS_CHN2.

GermOnline

ENSG00000106069. Homo sapiens.

Family and domain databases

InterPro

IPR002219. DAG_PE_bd.
IPR017356. N-chimaerin.
IPR000198. RhoGAP.
IPR000980. SH2.
[Graphical view]

Gene3D

G3DSA:1.10.555.10. RhoGAP. 1 hit.
G3DSA:3.30.505.10. SH2. 1 hit.

Pfam

PF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]

PIRSF

PIRSF038015. N-chimaerin. 1 hit.

PRINTS

PR00008. DAGPEDOMAIN.
PR00401. SH2DOMAIN.

ProDom

PD000093. SH2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]

PROSITE

PS50238. RHOGAP. 1 hit.
PS50001. SH2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P52757.

NextBio

4668.

SOURCE

Search...

Entry information

Entry name

CHIO_HUMAN

Accession

Primary (citable) accession number: P52757
Secondary accession number(s): Q2M203, Q75MM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)