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Protein

Rho guanine nucleotide exchange factor 18

Gene

ARHGEF18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. Also act as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 18
Alternative name(s):
114 kDa Rho-specific guanine nucleotide exchange factor
Short name:
p114-Rho-GEF
Short name:
p114RhoGEF
Septin-associated RhoGEF
Short name:
SA-RhoGEF
Gene namesi
Name:ARHGEF18
Synonyms:KIAA0521
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:17090. ARHGEF18.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Colocalizes with actin stress fibers.

GO - Cellular componenti

  • apical part of cell Source: MGI
  • cell junction Source: Reactome
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394630.

Polymorphism and mutation databases

BioMutaiARHGEF18.
DMDMi296439444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11731173Rho guanine nucleotide exchange factor 18PRO_0000341415Add
BLAST

Proteomic databases

MaxQBiQ6ZSZ5.
PaxDbiQ6ZSZ5.
PRIDEiQ6ZSZ5.

PTM databases

PhosphoSiteiQ6ZSZ5.

Expressioni

Tissue specificityi

Expressed in all tissues tested with highest expression in kidney and pancreas. Weakly or not expressed in liver, skeletal muscle and testis.3 Publications

Gene expression databases

BgeeiQ6ZSZ5.
CleanExiHS_ARHGEF18.
ExpressionAtlasiQ6ZSZ5. baseline.
GenevisibleiQ6ZSZ5. HS.

Organism-specific databases

HPAiHPA042689.

Interactioni

Subunit structurei

Interacts with SEPT9; interaction may inhibit GEF activity. Interacts with Gbetagamma subunits GNB1 and GNG2.2 Publications

Protein-protein interaction databases

BioGridi116950. 6 interactions.
IntActiQ6ZSZ5. 1 interaction.
STRINGi9606.ENSP00000352995.

Structurei

3D structure databases

ProteinModelPortaliQ6ZSZ5.
SMRiQ6ZSZ5. Positions 220-599.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 456198DHPROSITE-ProRule annotationAdd
BLAST
Domaini496 – 598103PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili799 – 81921Sequence AnalysisAdd
BLAST
Coiled coili850 – 960111Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1104 – 115855Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG243163.
GeneTreeiENSGT00760000119193.
HOGENOMiHOG000236361.
HOVERGENiHBG104846.
InParanoidiQ6ZSZ5.
OMAiPRKWSEN.
OrthoDBiEOG7JDQWP.
PhylomeDBiQ6ZSZ5.
TreeFamiTF325887.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERiPTHR22825. PTHR22825. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZSZ5-1) [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

        10         20         30         40         50
MVTVGTNILP SRPAASANTA REDAALFSRR IPPRHKNGAA QPGAAPGPGA
60 70 80 90 100
PGANMGNAHS KSGDRHSALP GRPELSFYGS FPRKWSENVF LDNELLTSKI
110 120 130 140 150
LSVLRPQSER GFRAGDLRYP THFLSTNSVL ASVTASLKEH PRGTLLSDGS
160 170 180 190 200
PALSRNVGMT VSQKGGPQPT PSPAGPGTQL GPITGEMDEA DSAFLKFKQT
210 220 230 240 250
ADDSLSLTSP NTESIFVEDP YTASLRSEIE SDGHEFEAES WSLAVDAAYA
260 270 280 290 300
KKQKREVVKR QDVLYELMQT EVHHVRTLKI MLKVYSRALQ EELQFSSKAI
310 320 330 340 350
GRLFPCADDL LETHSHFLAR LKERRQESLE EGSDRNYVIQ KIGDLLVQQF
360 370 380 390 400
SGENGERMKE KYGVFCSGHN EAVSHYKLLL QQNKKFQNLI KKIGNFSIVR
410 420 430 440 450
RLGVQECILL VTQRITKYPV LVERIIQNTE AGTEDYEDLT QALNLIKDII
460 470 480 490 500
SQVDAKVSEC EKGQRLREIA GKMDLKSSSK LKNGLTFRKE DMLQRQLHLE
510 520 530 540 550
GMLCWKTTSG RLKDILAILL TDVLLLLQEK DQKYVFASVD SKPPVISLQK
560 570 580 590 600
LIVREVANEE KAMFLISASL QGPEMYEIYT SSKEDRNAWM AHIQRAVESC
610 620 630 640 650
PDEEEGPFSL PEEERKVVEA RATRLRDFQE RLSMKDQLIA QSLLEKQQIY
660 670 680 690 700
LEMAEMGGLE DLPQPRGLFR GGDPSETLQG ELILKSAMSE IEGIQSLICR
710 720 730 740 750
QLGSANGQAE DGGSSTGPPR RAETFAGYDC TNSPTKNGSF KKKVSSTDPR
760 770 780 790 800
PRDWRGPPNS PDLKLSDSDI PGSSEESPQV VEAPGTESDP RLPTVLESEL
810 820 830 840 850
VQRIQTLSQL LLNLQAVIAH QDSYVETQRA AIQEREKQFR LQSTRGNLLL
860 870 880 890 900
EQERQRNFEK QREERAALEK LQSQLRHEQQ RWERERQWQH QELERAGARL
910 920 930 940 950
QEREGEARQL RERLEQERAE LERQRQAYQH DLERLREAQR AVERERERLE
960 970 980 990 1000
LLRRLKKQNT APGALPPDTL AEAQPPSHPP SFNGEGLEGP RVSMLPSGVG
1010 1020 1030 1040 1050
PEYAERPEVA RRDSAPTENR LAKSDVPIQL LSATNQFQRQ AAVQQQIPTK
1060 1070 1080 1090 1100
LAASTKGGKD KGGKSRGSQR WESSASFDLK QQLLLNKLMG KDESTSRNRR
1110 1120 1130 1140 1150
SLSPILPGRH SPAPPPDPGF PAPSPPPADS PSEGFSLKAG GTALLPGPPA
1160 1170
PSPLPATPLS AKEDASKEDV IFF
Length:1,173
Mass (Da):130,780
Last modified:May 18, 2010 - v3
Checksum:iD986A1F85D48EE24
GO
Isoform 2 (identifier: Q6ZSZ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.

Show »
Length:1,015
Mass (Da):114,077
Checksum:i03BD1D9224E422BD
GO

Sequence cautioni

The sequence AAH77721.1 differs from that shown.Aberrant splicing.Curated
The sequence BAA25447.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031V → M in BAC86801 (PubMed:14702039).Curated
Sequence conflicti183 – 1831I → V in BAC86801 (PubMed:14702039).Curated
Sequence conflicti1107 – 11071P → S in BAC86801 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti701 – 7011Q → R.2 Publications
Corresponds to variant rs2287918 [ dbSNP | Ensembl ].
VAR_044066
Natural varianti752 – 7521R → Q.
Corresponds to variant rs2287920 [ dbSNP | Ensembl ].
VAR_044067
Natural varianti1019 – 10191N → S.2 Publications
Corresponds to variant rs9329368 [ dbSNP | Ensembl ].
VAR_063099

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 158158Missing in isoform 2. 2 PublicationsVSP_034315Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011093 mRNA. Translation: BAA25447.1. Different initiation.
AK127045 mRNA. Translation: BAC86801.1.
AC008878 Genomic DNA. No translation available.
AC119396 Genomic DNA. No translation available.
BC077721 mRNA. Translation: AAH77721.1. Sequence problems.
CCDSiCCDS12177.1. [Q6ZSZ5-2]
CCDS45946.1. [Q6ZSZ5-1]
RefSeqiNP_001124427.1. NM_001130955.1. [Q6ZSZ5-1]
NP_056133.2. NM_015318.3. [Q6ZSZ5-2]
XP_006722771.1. XM_006722708.2. [Q6ZSZ5-2]
XP_006722772.1. XM_006722709.2. [Q6ZSZ5-2]
UniGeneiHs.465761.
Hs.736818.

Genome annotation databases

EnsembliENST00000319670; ENSP00000319200; ENSG00000104880. [Q6ZSZ5-2]
ENST00000359920; ENSP00000352995; ENSG00000104880. [Q6ZSZ5-1]
GeneIDi23370.
KEGGihsa:23370.
UCSCiuc002mgh.3. human. [Q6ZSZ5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011093 mRNA. Translation: BAA25447.1. Different initiation.
AK127045 mRNA. Translation: BAC86801.1.
AC008878 Genomic DNA. No translation available.
AC119396 Genomic DNA. No translation available.
BC077721 mRNA. Translation: AAH77721.1. Sequence problems.
CCDSiCCDS12177.1. [Q6ZSZ5-2]
CCDS45946.1. [Q6ZSZ5-1]
RefSeqiNP_001124427.1. NM_001130955.1. [Q6ZSZ5-1]
NP_056133.2. NM_015318.3. [Q6ZSZ5-2]
XP_006722771.1. XM_006722708.2. [Q6ZSZ5-2]
XP_006722772.1. XM_006722709.2. [Q6ZSZ5-2]
UniGeneiHs.465761.
Hs.736818.

3D structure databases

ProteinModelPortaliQ6ZSZ5.
SMRiQ6ZSZ5. Positions 220-599.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116950. 6 interactions.
IntActiQ6ZSZ5. 1 interaction.
STRINGi9606.ENSP00000352995.

PTM databases

PhosphoSiteiQ6ZSZ5.

Polymorphism and mutation databases

BioMutaiARHGEF18.
DMDMi296439444.

Proteomic databases

MaxQBiQ6ZSZ5.
PaxDbiQ6ZSZ5.
PRIDEiQ6ZSZ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319670; ENSP00000319200; ENSG00000104880. [Q6ZSZ5-2]
ENST00000359920; ENSP00000352995; ENSG00000104880. [Q6ZSZ5-1]
GeneIDi23370.
KEGGihsa:23370.
UCSCiuc002mgh.3. human. [Q6ZSZ5-1]

Organism-specific databases

CTDi23370.
GeneCardsiGC19P007459.
HGNCiHGNC:17090. ARHGEF18.
HPAiHPA042689.
neXtProtiNX_Q6ZSZ5.
PharmGKBiPA128394630.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG243163.
GeneTreeiENSGT00760000119193.
HOGENOMiHOG000236361.
HOVERGENiHBG104846.
InParanoidiQ6ZSZ5.
OMAiPRKWSEN.
OrthoDBiEOG7JDQWP.
PhylomeDBiQ6ZSZ5.
TreeFamiTF325887.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSiARHGEF18. human.
GenomeRNAii23370.
NextBioi45444.
PROiQ6ZSZ5.

Gene expression databases

BgeeiQ6ZSZ5.
CleanExiHS_ARHGEF18.
ExpressionAtlasiQ6ZSZ5. baseline.
GenevisibleiQ6ZSZ5. HS.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERiPTHR22825. PTHR22825. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ARG-701 AND SER-1019.
    Tissue: Brain.
  2. "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] (ISOFORM 1).
    Tissue: Brain.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1156 (ISOFORM 2), VARIANTS ARG-701 AND SER-1019.
    Tissue: Lymph.
  5. "Identification and characterization of a novel Rho-specific guanine nucleotide exchange factor."
    Blomquist A., Schwoerer G., Schablowski H., Psoma A., Lehnen M., Jakobs K.H., Ruemenapp U.
    Biochem. J. 352:319-325(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. Cited for: IDENTIFICATION.
  7. "G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide exchange factor for RhoA and Rac1: regulation of cell shape and reactive oxygen species production."
    Niu J., Profirovic J., Pan H., Vaiskunaite R., Voyno-Yasenetskaya T.
    Circ. Res. 93:848-856(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH GNB1 AND GNG2.
  8. "Cytoskeletal modification of Rho guanine nucleotide exchange factor activity: identification of a Rho guanine nucleotide exchange factor as a binding partner for Sept9b, a mammalian septin."
    Nagata K., Inagaki M.
    Oncogene 24:65-76(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SEPT9.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARHGI_HUMAN
AccessioniPrimary (citable) accession number: Q6ZSZ5
Secondary accession number(s): A8MV62
, B5ME81, O60274, Q6DD92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 18, 2010
Last modified: June 24, 2015
This is version 106 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.