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Q9NZN5 (ARHGC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho guanine nucleotide exchange factor 12
Alternative name(s):
Leukemia-associated RhoGEF
Gene names
Name:ARHGEF12
Synonyms:KIAA0382, LARG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Ref.5

Subunit structure

Interacts with GNA12 and GNA13, probably through the RGS-like domain. Interacts with RHOA, PLXNB1 and PLXNB2. Interacts through its PDZ domain with IGF1R beta subunit. Interacts with GCSAM. Ref.5 Ref.6 Ref.7 Ref.8 Ref.15 Ref.18 Ref.19

Subcellular location

Cytoplasm Probable. Membrane Probable. Note: Translocated to the membrane upon stimulation Probable.

Tissue specificity

Ubiquitously expressed. Isoform 2 is found in jejunum and testis.

Involvement in disease

A chromosomal aberration involving ARHGEF12 may be a cause of acute leukemia. Translocation t(11;11)(q23;23) with KMT2A/MLL1.

Sequence similarities

Contains 1 DH (DBL-homology) domain.

Contains 1 PDZ (DHR) domain.

Contains 1 PH domain.

Contains 1 RGSL (RGS-like) domain.

Sequence caution

The sequence AAH63117.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
   Molecular functionGTPase activation
Guanine-nucleotide releasing factor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 15755723. Source: MGI

apoptotic signaling pathway

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15755723. Source: MGI

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein coupled receptor binding

Inferred from direct assay PubMed 15755723. Source: MGI

GTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

Rho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IGF1RP080697EBI-821440,EBI-475981
Lpar1P617933EBI-821440,EBI-7512335From a different organism.
RHOAP615862EBI-821440,EBI-446668

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZN5-1)

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 2 (identifier: Q9NZN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     48-66: Missing.
Note: Contains a phosphoserine at position 41.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 15441543Rho guanine nucleotide exchange factor 12
PRO_0000080930

Regions

Domain72 – 15180PDZ
Domain367 – 558192RGSL
Domain787 – 977191DH
Domain1019 – 1132114PH
Coiled coil194 – 26269 Potential

Sites

Site308 – 3092Breakpoint for translocation to form KMT2A/MLL1-ARHGEF12 oncogene

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue3411Phosphoserine Ref.12
Modified residue6371Phosphoserine Ref.16
Modified residue7361Phosphothreonine Ref.11
Modified residue13271Phosphoserine By similarity

Natural variations

Alternative sequence48 – 6619Missing in isoform 2.
VSP_008131
Natural variant9731Y → F. Ref.3
Corresponds to variant rs2305013 [ dbSNP | Ensembl ].
VAR_020191

Secondary structure

.......................................................................... 1544
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0B7E319CF7C7A224

FASTA1,544173,232
        10         20         30         40         50         60 
MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTDSS SKKTKSSSEE 

        70         80         90        100        110        120 
SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED GAAMRAGVQT GDRIIKVNGT 

       130        140        150        160        170        180 
LVTHSNHLEV VKLIKSGSYV ALTVQGRPPG SPQIPLADSE VEPSVIGHMS PIMTSPHSPG 

       190        200        210        220        230        240 
ASGNMERITS PVLMGEENNV VHNQKVEILR KMLQKEQERL QLLQEDYNRT PAQRLLKEIQ 

       250        260        270        280        290        300 
EAKKHIPQLQ EQLSKATGSA QDGAVVTPSR PLGDTLTVSE AETDPGDVLG RTDCSSGDAS 

       310        320        330        340        350        360 
RPSSDNADSP KSGPKERIYL EENPEKSETI QDTDTQSLVG SPSTRIAPHI IGAEDDDFGT 

       370        380        390        400        410        420 
EHEQINGQCS CFQSIELLKS RPAHLAVFLH HVVSQFDPAT LLCYLYSDLY KHTNSKETRR 

       430        440        450        460        470        480 
IFLEFHQFFL DRSAHLKVSV PDEMSADLEK RRPELIPEDL HRHYIQTMQE RVHPEVQRHL 

       490        500        510        520        530        540 
EDFRQKRSMG LTLAESELTK LDAERDKDRL TLEKERTCAE QIVAKIEEVL MTAQAVEEDK 

       550        560        570        580        590        600 
SSTMQYVILM YMKHLGVKVK EPRNLEHKRG RIGFLPKIKQ SMKKDKEGEE KGKRRGFPSI 

       610        620        630        640        650        660 
LGPPRRPSRH DNSAIGRAME LQKARHPKHL STPSSVSPEP QDSAKLRQSG LANEGTDAGY 

       670        680        690        700        710        720 
LPANSMSSVA SGASFSQEGG KENDTGSKQV GETSAPGDTL DGTPRTLNTV FDFPPPPLDQ 

       730        740        750        760        770        780 
VQEEECEVER VTEHGTPKPF RKFDSVAFGE SQSEDEQFEN DLETDPPNWQ QLVSREVLLG 

       790        800        810        820        830        840 
LKPCEIKRQE VINELFYTER AHVRTLKVLD QVFYQRVSRE GILSPSELRK IFSNLEDILQ 

       850        860        870        880        890        900 
LHIGLNEQMK AVRKRNETSV IDQIGEDLLT WFSGPGEEKL KHAAATFCSN QPFALEMIKS 

       910        920        930        940        950        960 
RQKKDSRFQT FVQDAESNPL CRRLQLKDII PTQMQRLTKY PLLLDNIAKY TEWPTEREKV 

       970        980        990       1000       1010       1020 
KKAADHCRQI LNYVNQAVKE AENKQRLEDY QRRLDTSSLK LSEYPNVEEL RNLDLTKRKM 

      1030       1040       1050       1060       1070       1080 
IHEGPLVWKV NRDKTIDLYT LLLEDILVLL QKQDDRLVLR CHSKILASTA DSKHTFSPVI 

      1090       1100       1110       1120       1130       1140 
KLSTVLVRQV ATDNKALFVI SMSDNGAQIY ELVAQTVSEK TVWQDLICRM AASVKEQSTK 

      1150       1160       1170       1180       1190       1200 
PIPLPQSTPG EGDNDEEDPS KLKEEQHGIS VTGLQSPDRD LGLESTLISS KPQSHSLSTS 

      1210       1220       1230       1240       1250       1260 
GKSEVRDLFV AERQFAKEQH TDGTLKEVGE DYQIAIPDSH LPVSEERWAL DALRNLGLLK 

      1270       1280       1290       1300       1310       1320 
QLLVQQLGLT EKSVQEDWQH FPRYRTASQG PQTDSVIQNS ENIKAYHSGE GHMPFRTGTG 

      1330       1340       1350       1360       1370       1380 
DIATCYSPRT STESFAPRDS VGLAPQDSQA SNILVMDHMI MTPEMPTMEP EGGLDDSGEH 

      1390       1400       1410       1420       1430       1440 
FFDAREAHSD ENPSEGDGAV NKEEKDVNLR ISGNYLILDG YDPVQESSTD EEVASSLTLQ 

      1450       1460       1470       1480       1490       1500 
PMTGIPAVES THQQQHSPQN THSDGAISPF TPEFLVQQRW GAMEYSCFEI QSPSSCADSQ 

      1510       1520       1530       1540 
SQIMEYIHKI EADLEHLKKV EESYTILCQR LAGSALTDKH SDKS 

« Hide

Isoform 2 [UniParc].

Checksum: 47FF1323DE2DFF55
Show »

FASTA1,525171,115

References

« Hide 'large scale' references
[1]"Identification of a gene at 11q23 encoding a guanine nucleotide exchange factor: evidence for its fusion with MLL in acute myeloid leukemia."
Kourlas P.J., Strout M.P., Becknell B., Veronese M.L., Croce C.M., Theil K.S., Krahe R., Ruutu T., Knuutila S., Bloomfield C.D., Caligiuri M.A.
Proc. Natl. Acad. Sci. U.S.A. 97:2145-2150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHROMOSOMAL TRANSLOCATION.
Tissue: Prostate.
[2]"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] OF 1-584 (ISOFORM 2).
Tissue: Thyroid.
[3]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-1544, VARIANT PHE-973.
Tissue: Brain.
[4]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links heterotrimeric G proteins of the G(12) family to Rho."
Fukuhara S., Chikumi H., Gutkind J.S.
FEBS Lett. 485:183-188(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RHOA; GNA12 AND GNA13.
[6]"Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF."
Taya S., Inagaki N., Sengiku H., Makino H., Iwamatsu A., Urakawa I., Nagao K., Kataoka S., Kaibuchi K.
J. Cell Biol. 155:809-820(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGF1R.
[7]"B plexins activate Rho through PDZ-RhoGEF."
Driessens M.H.E., Olivo C., Nagata K., Inagaki M., Collard J.G.
FEBS Lett. 529:168-172(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1 AND PLXNB2.
[8]"Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF."
Perrot V., Vazquez-Prado J., Gutkind J.S.
J. Biol. Chem. 277:43115-43120(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1 AND PLXNB2.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"HGAL, a germinal center specific protein, decreases lymphoma cell motility by modulation of the RhoA signaling pathway."
Jiang X., Lu X., McNamara G., Liu X., Cubedo E., Sarosiek K.A., Sanchez-Garcia I., Helfman D.M., Lossos I.S.
Blood 116:5217-5227(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GCSAM.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor."
Kristelly R., Gao G., Tesmer J.J.
J. Biol. Chem. 279:47352-47362(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 766-1138 IN COMPLEX WITH RHOA, SUBUNIT.
[19]"Conformational change upon ligand binding and dynamics of the PDZ domain from leukemia-associated Rho guanine nucleotide exchange factor."
Liu J., Zhang J., Yang Y., Huang H., Shen W., Hu Q., Wang X., Wu J., Shi Y.
Protein Sci. 17:1003-1014(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 67-151 IN COMPLEX WITH PLXNB1, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF180681 mRNA. Translation: AAF36817.1.
AB002380 mRNA. Translation: BAA20836.2.
BC063117 mRNA. Translation: AAH63117.1. Sequence problems.
RefSeqNP_001185594.1. NM_001198665.1.
NP_056128.1. NM_015313.2.
UniGeneHs.24598.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXDX-ray2.13A766-1138[»]
1X86X-ray3.22A/C/E/G766-1138[»]
2OMJNMR-A67-151[»]
2OS6NMR-A67-151[»]
ProteinModelPortalQ9NZN5.
SMRQ9NZN5. Positions 67-151, 766-1138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116945. 13 interactions.
DIPDIP-37887N.
IntActQ9NZN5. 10 interactions.
MINTMINT-1774807.
STRING9606.ENSP00000380942.

PTM databases

PhosphoSiteQ9NZN5.

Polymorphism databases

DMDM34395525.

Proteomic databases

PaxDbQ9NZN5.
PRIDEQ9NZN5.

Protocols and materials databases

DNASU23365.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356641; ENSP00000349056; ENSG00000196914. [Q9NZN5-2]
ENST00000397843; ENSP00000380942; ENSG00000196914. [Q9NZN5-1]
GeneID23365.
KEGGhsa:23365.
UCSCuc001pxl.2. human. [Q9NZN5-1]
uc009zat.3. human. [Q9NZN5-2]

Organism-specific databases

CTD23365.
GeneCardsGC11P120207.
H-InvDBHIX0010202.
HIX0036240.
HGNCHGNC:14193. ARHGEF12.
HPACAB025581.
HPA018911.
MIM604763. gene.
neXtProtNX_Q9NZN5.
PharmGKBPA24969.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5422.
HOGENOMHOG000034046.
HOVERGENHBG050571.
InParanoidQ9NZN5.
KOK07532.
OMAMTPEMPT.
OrthoDBEOG7GJ6CF.
PhylomeDBQ9NZN5.
TreeFamTF106495.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9NZN5.
BgeeQ9NZN5.
CleanExHS_ARHGEF12.
GenevestigatorQ9NZN5.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR016137. Regulat_G_prot_signal_superfam.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERPTHR22825. PTHR22825. 1 hit.
PfamPF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGEF12. human.
EvolutionaryTraceQ9NZN5.
GeneWikiARHGEF12.
GenomeRNAi23365.
NextBio45421.
PROQ9NZN5.
SOURCESearch...

Entry information

Entry nameARHGC_HUMAN
AccessionPrimary (citable) accession number: Q9NZN5
Secondary accession number(s): O15086, Q6P526
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 125 of the entry and version 1 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 11

Human chromosome 11: entries, gene names and cross-references to MIM