Q13905 (RPGF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rap guanine nucleotide exchange factor 1

Alternative name(s):
CRK SH3-binding GNRP
Guanine nucleotide-releasing factor 2
Protein C3G

Gene names

Name:	RAPGEF1
Synonyms:	GRF2

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	1077 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Ref.2
Subunit structure	Interacts with CRK via its SH3-binding sites. Ref.5 Ref.6
Tissue specificity	Ubiquitously expressed in adult and fetus. Expression is high in adult skeletal muscle and placenta and in fetal brain and heart. Low levels of expression in adult and fetal liver.
Post-translational modification	Phosphorylation at Tyr-504 enhances activity as Rap guanine nucleotide exchange factor.
Sequence similarities	Contains 1 N-terminal Ras-GEF domain. Contains 1 Ras-GEF domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	SH3-binding
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of MAPKK activity Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Traceable author statement. Source: Reactome endosome Traceable author statement. Source: Reactome
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	3	EBI-976876,EBI-886
FYN	P06241	2	EBI-976876,EBI-515315
NCK1	P16333	2	EBI-976876,EBI-389883
PIK3R1	P27986	2	EBI-976876,EBI-79464
SRC	P12931	2	EBI-976876,EBI-621482

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q13905-1)

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 Short (identifier: Q13905-2)

The sequence of this isoform differs from the canonical sequence as follows:
     50-88: Missing.

Isoform 3 (identifier: Q13905-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MDT → MGNAIEKQKPLKRSHLYPWKQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1077	1077	Rap guanine nucleotide exchange factor 1		PRO_0000068864
Regions
	Domain	688 – 810	123	N-terminal Ras-GEF
	Domain	840 – 1064	225	Ras-GEF
	Motif	281 – 292	12	SH3-binding
	Motif	451 – 462	12	SH3-binding
	Motif	538 – 549	12	SH3-binding
	Motif	606 – 617	12	SH3-binding
	Compositional bias	963 – 966	4	Poly-Ser
Amino acid modifications
	Modified residue	314	1	Phosphoserine Ref.8
	Modified residue	360	1	Phosphoserine Ref.7 Ref.8
	Modified residue	504	1	Phosphotyrosine; by HCK Ref.6
	Modified residue	652	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	1 – 3	3	MDT → MGNAIEKQKPLKRSHLYPWK Q in isoform 3.		VSP_042052
	Alternative sequence	50 – 88	39	Missing in isoform Short.		VSP_001822
Experimental info
	Mutagenesis	504	1	Y → F: Abolishes phosphorylation by HCK. Ref.6
	Sequence conflict	137	1	P → R Ref.2
	Sequence conflict	183	1	E → G Ref.2
	Sequence conflict	217	1	S → C Ref.2
	Sequence conflict	254	1	T → S Ref.2
	Sequence conflict	287	1	P → T in BAA04770. Ref.1
	Sequence conflict	355	1	G → D in BAA04770. Ref.1
	Sequence conflict	636	1	G → V Ref.2
	Sequence conflict	698	1	D → N Ref.2
	Sequence conflict	846 – 847	2	EQ → DE Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified April 3, 2007. Version 3. Checksum: E700631A0EE76CA1	FASTA	1,077	120,548
	10 20 30 40 50 60 MDTDSQRSHL SSFTMKLMDK FHSPKIKRTP SKKGKPAEVS VKIPEKPVNK EATDRFLPEG 70 80 90 100 110 120 YPLPLDLEQQ AVEFMSTSAV ASRSQRQKNL SWLEEKEKEV VSALRYFKTI VDKMAIDKKV 130 140 150 160 170 180 LEMLPGSASK VLEAILPLVQ NDPRIQHSSA LSSCYSRVYQ SLANLIRWSD QVMLEGVNSE 190 200 210 220 230 240 DKEMVTTVKG VIKAVLDGVK ELVRLTIEKQ GRPSPTSPVK PSSPASKPDG PAELPLTDRE 250 260 270 280 290 300 VEILNKTTGM SQSTELLPDA TDEEVAPPKP PLPGIRVVDN SPPPALPPKK RQSAPSPTRV 310 320 330 340 350 360 AVVAPMSRAT SGSSLPVGIN RQDFDVDCYA QRRLSGGSHS YGGESPRLSP CSSIGKLSKS 370 380 390 400 410 420 DEQLSSLDRD SGQCSRNTSC ETLDHYDPDY EFLQQDLSNA DQIPQQTAWN LSPLPESLGE 430 440 450 460 470 480 SGSPFLGPPF QLPLGGHPQP DGPLAPGQQT DTPPALPEKK RRSAASQTAD GSGCRVSYER 490 500 510 520 530 540 HPSQYDNISG EDLQSTAPIP SVPYAPFAAI LPFQHGGSSA PVEFVGDFTA PESTGDPEKP 550 560 570 580 590 600 PPLPEKKNKH MLAYMQLLED YSEPQPSMFY QTPQNEHIYQ QKNKLLMEVY GFSDSFSGVD 610 620 630 640 650 660 SVQELAPPPA LPPKQRQLEP PAGKDGHPRD PSAVSGVPGK DSRDGSERAP KSPDALESAQ 670 680 690 700 710 720 SEEEVDELSL IDHNEIMSRL TLKQEGDDGP DVRGGSGDIL LVHATETDRK DLVLYCEAFL 730 740 750 760 770 780 TTYRTFISPE ELIKKLQYRY EKFSPFADTF KKRVSKNTFF VLVRVVDELC LVELTEEILK 790 800 810 820 830 840 LLMELVFRLV CNGELSLARV LRKNILDKVD QKKLLRCATS SQPLAARGVA ARPGTLHDFH 850 860 870 880 890 900 SHEIAEQLTL LDAELFYKIE IPEVLLWAKE QNEEKSPNLT QFTEHFNNMS YWVRSIIMLQ 910 920 930 940 950 960 EKAQDRERLL LKFIKIMKHL RKLNNFNSYL AILSALDSAP IRRLEWQKQT SEGLAEYCTL 970 980 990 1000 1010 1020 IDSSSSFRAY RAALSEVEPP CIPYLGLILQ DLTFVHLGNP DYIDGKVNFS KRWQQFNILD 1030 1040 1050 1060 1070 SMRCFQQAHY DMRRNDDIIN FFNDFSDHLA EEALWELSLK IKPRNITRRK TDREEKT
	Isoform Short [UniParc]. Checksum: 34F0A1BD9C8B0732	FASTA	1,038	116,141
	10 20 30 40 50 60 MDTDSQRSHL SSFTMKLMDK FHSPKIKRTP SKKGKPAEVS VKIPEKPVNN LSWLEEKEKE 70 80 90 100 110 120 VVSALRYFKT IVDKMAIDKK VLEMLPGSAS KVLEAILPLV QNDPRIQHSS ALSSCYSRVY 130 140 150 160 170 180 QSLANLIRWS DQVMLEGVNS EDKEMVTTVK GVIKAVLDGV KELVRLTIEK QGRPSPTSPV 190 200 210 220 230 240 KPSSPASKPD GPAELPLTDR EVEILNKTTG MSQSTELLPD ATDEEVAPPK PPLPGIRVVD 250 260 270 280 290 300 NSPPPALPPK KRQSAPSPTR VAVVAPMSRA TSGSSLPVGI NRQDFDVDCY AQRRLSGGSH 310 320 330 340 350 360 SYGGESPRLS PCSSIGKLSK SDEQLSSLDR DSGQCSRNTS CETLDHYDPD YEFLQQDLSN 370 380 390 400 410 420 ADQIPQQTAW NLSPLPESLG ESGSPFLGPP FQLPLGGHPQ PDGPLAPGQQ TDTPPALPEK 430 440 450 460 470 480 KRRSAASQTA DGSGCRVSYE RHPSQYDNIS GEDLQSTAPI PSVPYAPFAA ILPFQHGGSS 490 500 510 520 530 540 APVEFVGDFT APESTGDPEK PPPLPEKKNK HMLAYMQLLE DYSEPQPSMF YQTPQNEHIY 550 560 570 580 590 600 QQKNKLLMEV YGFSDSFSGV DSVQELAPPP ALPPKQRQLE PPAGKDGHPR DPSAVSGVPG 610 620 630 640 650 660 KDSRDGSERA PKSPDALESA QSEEEVDELS LIDHNEIMSR LTLKQEGDDG PDVRGGSGDI 670 680 690 700 710 720 LLVHATETDR KDLVLYCEAF LTTYRTFISP EELIKKLQYR YEKFSPFADT FKKRVSKNTF 730 740 750 760 770 780 FVLVRVVDEL CLVELTEEIL KLLMELVFRL VCNGELSLAR VLRKNILDKV DQKKLLRCAT 790 800 810 820 830 840 SSQPLAARGV AARPGTLHDF HSHEIAEQLT LLDAELFYKI EIPEVLLWAK EQNEEKSPNL 850 860 870 880 890 900 TQFTEHFNNM SYWVRSIIML QEKAQDRERL LLKFIKIMKH LRKLNNFNSY LAILSALDSA 910 920 930 940 950 960 PIRRLEWQKQ TSEGLAEYCT LIDSSSSFRA YRAALSEVEP PCIPYLGLIL QDLTFVHLGN 970 980 990 1000 1010 1020 PDYIDGKVNF SKRWQQFNIL DSMRCFQQAH YDMRRNDDII NFFNDFSDHL AEEALWELSL 1030 KIKPRNITRR KTDREEKT
	Isoform 3 [UniParc]. Checksum: 04C19860FF7F11E8	FASTA	1,095	122,735
	10 20 30 40 50 60 MGNAIEKQKP LKRSHLYPWK QDSQRSHLSS FTMKLMDKFH SPKIKRTPSK KGKPAEVSVK 70 80 90 100 110 120 IPEKPVNKEA TDRFLPEGYP LPLDLEQQAV EFMSTSAVAS RSQRQKNLSW LEEKEKEVVS 130 140 150 160 170 180 ALRYFKTIVD KMAIDKKVLE MLPGSASKVL EAILPLVQND PRIQHSSALS SCYSRVYQSL 190 200 210 220 230 240 ANLIRWSDQV MLEGVNSEDK EMVTTVKGVI KAVLDGVKEL VRLTIEKQGR PSPTSPVKPS 250 260 270 280 290 300 SPASKPDGPA ELPLTDREVE ILNKTTGMSQ STELLPDATD EEVAPPKPPL PGIRVVDNSP 310 320 330 340 350 360 PPALPPKKRQ SAPSPTRVAV VAPMSRATSG SSLPVGINRQ DFDVDCYAQR RLSGGSHSYG 370 380 390 400 410 420 GESPRLSPCS SIGKLSKSDE QLSSLDRDSG QCSRNTSCET LDHYDPDYEF LQQDLSNADQ 430 440 450 460 470 480 IPQQTAWNLS PLPESLGESG SPFLGPPFQL PLGGHPQPDG PLAPGQQTDT PPALPEKKRR 490 500 510 520 530 540 SAASQTADGS GCRVSYERHP SQYDNISGED LQSTAPIPSV PYAPFAAILP FQHGGSSAPV 550 560 570 580 590 600 EFVGDFTAPE STGDPEKPPP LPEKKNKHML AYMQLLEDYS EPQPSMFYQT PQNEHIYQQK 610 620 630 640 650 660 NKLLMEVYGF SDSFSGVDSV QELAPPPALP PKQRQLEPPA GKDGHPRDPS AVSGVPGKDS 670 680 690 700 710 720 RDGSERAPKS PDALESAQSE EEVDELSLID HNEIMSRLTL KQEGDDGPDV RGGSGDILLV 730 740 750 760 770 780 HATETDRKDL VLYCEAFLTT YRTFISPEEL IKKLQYRYEK FSPFADTFKK RVSKNTFFVL 790 800 810 820 830 840 VRVVDELCLV ELTEEILKLL MELVFRLVCN GELSLARVLR KNILDKVDQK KLLRCATSSQ 850 860 870 880 890 900 PLAARGVAAR PGTLHDFHSH EIAEQLTLLD AELFYKIEIP EVLLWAKEQN EEKSPNLTQF 910 920 930 940 950 960 TEHFNNMSYW VRSIIMLQEK AQDRERLLLK FIKIMKHLRK LNNFNSYLAI LSALDSAPIR 970 980 990 1000 1010 1020 RLEWQKQTSE GLAEYCTLID SSSSFRAYRA ALSEVEPPCI PYLGLILQDL TFVHLGNPDY 1030 1040 1050 1060 1070 1080 IDGKVNFSKR WQQFNILDSM RCFQQAHYDM RRNDDIINFF NDFSDHLAEE ALWELSLKIK 1090 PRNITRRKTD REEKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins." Tanaka S., Morishita T., Hashimoto Y., Hattori S., Nakamura S., Shibuya M., Matuoka K., Takenawa T., Kurata T., Nagashima K., Matsuda M. Proc. Natl. Acad. Sci. U.S.A. 91:3443-3447(1994) [PubMed: 7512734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), CHARACTERIZATION. Tissue: Placenta and Spleen.
[2]	"Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk." Knudsen B., Feller S., Hanafusa H. J. Biol. Chem. 269:32781-32787(1994) [PubMed: 7806500] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ALTERNATIVE SPLICING.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [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] (ISOFORM 3). Tissue: Skin.
[5]	"Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins." Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T., Nagashima K., Kurata T. J. Biol. Chem. 271:14468-14472(1996) [PubMed: 8662907] [Abstract] Cited for: INTERACTION WITH CRK.
[6]	"Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain." Shivakrupa R., Radha V., Sudhakar C., Swarup G. J. Biol. Chem. 278:52188-52194(2003) [PubMed: 14551197] [Abstract] Cited for: INTERACTION WITH HCK, MUTAGENESIS OF TYR-504, PHOSPHORYLATION AT TYR-504.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-360 AND SER-652, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21239 mRNA. Translation: BAA04770.1. AL160271, AL160276 Genomic DNA. Translation: CAI13382.1. AL160276, AL160271 Genomic DNA. Translation: CAI40646.1. BC041710 mRNA. Translation: AAH41710.1.
IPI	IPI00332841. IPI00394743.
RefSeq	NP_005303.2. NM_005312.2. NP_941372.1. NM_198679.1.
UniGene	Hs.127897.
3D structure databases
ProteinModelPortal	Q13905.
SMR	Q13905. Positions 679-1068.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29392N.
IntAct	Q13905. 11 interactions.
MINT	MINT-107377.
STRING	Q13905.
PTM databases
PhosphoSite	Q13905.
Polymorphism databases
DMDM	143811452.
Proteomic databases
PRIDE	Q13905.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266110; ENSP00000266110; ENSG00000107263. ENST00000372189; ENSP00000361263; ENSG00000107263.
GeneID	2889.
KEGG	hsa:2889.
UCSC	uc004cbc.1. human.
Organism-specific databases
CTD	2889.
GeneCards	GC09M134452.
HGNC	HGNC:4568. RAPGEF1.
HPA	HPA006426.
MIM	600303. gene.
neXtProt	NX_Q13905.
PharmGKB	PA28964.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08153.
GeneTree	ENSGT00600000084163.
HOVERGEN	HBG058477.
OrthoDB	EOG4HX509.
Enzyme and pathway databases
Pathway_Interaction_DB	epopathway. EPO signaling pathway. ifngpathway. IFN-gamma pathway. insulin_pathway. Insulin Pathway. trkrpathway. Neurotrophic factor-mediated Trk receptor signaling. pdgfrapathway. PDGFR-alpha signaling pathway. reelinpathway. Reelin signaling pathway. met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
Reactome	REACT_111102. Signal Transduction. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q13905.
Bgee	Q13905.
CleanEx	HS_RAPGEF1.
Genevestigator	Q13905.
GermOnline	ENSG00000107263. Homo sapiens.
Family and domain databases
InterPro	IPR000651. Ras-like_Gua-exchang_fac_N. IPR019804. Ras_G-nucl-exch_fac_CS. IPR008937. Ras_GEF. IPR023578. Ras_GEF_dom. IPR001895. RasGRF_CDC25. [Graphical view]
Gene3D	G3DSA:1.10.840.10. RasGRF_CDC25. 1 hit.
KO	K06277.
PANTHER	PTHR23113. Ras_GEF. 1 hit.
Pfam	PF00617. RasGEF. 1 hit. PF00618. RasGEF_N. 1 hit. [Graphical view]
SMART	SM00147. RasGEF. 1 hit. SM00229. RasGEFN. 1 hit. [Graphical view]
SUPFAM	SSF48366. Ras_GEF. 1 hit.
PROSITE	PS00720. RASGEF. 1 hit. PS50009. RASGEF_CAT. 1 hit. PS50212. RASGEF_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	11419.
SOURCE	Search...

Entry information

Entry name

RPGF1_HUMAN

Accession

Primary (citable) accession number: Q13905
Secondary accession number(s): Q5JUE4, Q8IV73

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	April 3, 2007
Last modified:	January 25, 2012
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.