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Protein

Rac GTPase-activating protein 1

Gene

Racgap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri287 – 33650Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, GTPase activation

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Ion transport, Spermatogenesis, Transport

Keywords - Ligandi

Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-MMU-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Rac GTPase-activating protein 1
Alternative name(s):
Male germ cell RacGap
Short name:
MgcRacGAP
Gene namesi
Name:Racgap1Imported
Synonyms:Mgcracgap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1349423. Racgap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 628628Rac GTPase-activating protein 1PRO_0000228809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei150 – 1501Phosphoserine; by PLK1By similarity
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei158 – 1581Phosphoserine; by PLK1By similarity
Modified residuei162 – 1621PhosphothreonineBy similarity
Modified residuei165 – 1651Phosphoserine; by PLK1By similarity
Modified residuei171 – 1711Phosphoserine; by PLK1By similarity
Modified residuei204 – 2041PhosphoserineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei258 – 2581PhosphoserineBy similarity
Modified residuei343 – 3431PhosphothreonineBy similarity
Modified residuei388 – 3881Phosphoserine; by AURKBBy similarity
Modified residuei411 – 4111Phosphoserine; by AURKBBy similarity
Modified residuei564 – 5641PhosphothreonineCombined sources
Modified residuei577 – 5771PhosphothreonineCombined sources
Modified residuei585 – 5851PhosphothreonineCombined sources
Modified residuei602 – 6021PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated at multiple sites in the midbody during cytokinesis. Phosphorylation by AURKB on Ser-388 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA. Phosphorylation on multiple serine residues by PLK1 enhances its association with ECT2 and is critical for cleavage furrow formation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9WVM1.
MaxQBiQ9WVM1.
PaxDbiQ9WVM1.
PRIDEiQ9WVM1.

PTM databases

iPTMnetiQ9WVM1.
PhosphoSiteiQ9WVM1.

Expressioni

Tissue specificityi

Highly expressed in testis, thymus and spleen and weakly expressed in brain, heart, skeletal muscle and kidney. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Not detected in adult liver. Also expressed in fetal liver and in several hematopoietic cell lines.3 Publications

Developmental stagei

At E6.5 expressed in primitive endoderm, embryonic ectoderm, extraembryonic ectoderm and the ectoplacental cone. By E7.5, a widespread expression was observed in all intra- and extraembryonic tissues and also in the giant cells lining the inner boundary of the deciduum. At E9.5, expression was elevated in the neuroepithelium of the brain ventricles and the neural tube. By E12.5, expression remains widespread and in the brain higher levels were observed in the ventricular zone of the two telencephalic lobes, and in the mesencephalon and diencephalon, with the exception of the median sulcus. In adult brain, highest levels of expression were detected in cerebellum, specifically the Purkinje cell layer extending into the molecular layer.1 Publication

Inductioni

Expression is down-regulated during macrophage differentiation of M1 cells.1 Publication

Gene expression databases

BgeeiQ9WVM1.
CleanExiMM_RACGAP1.
ExpressionAtlasiQ9WVM1. baseline and differential.
GenevisibleiQ9WVM1. MM.

Interactioni

Subunit structurei

Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Interacts with SLC26A8 via its N-terminus. Interacts with RAB11FIP3. Interacts with ECT2; the interaction is direct, occurs at anaphase and during cytokinesis in a microtubule-dependent manner and is enhanced by phosphorylation by PLK1. Interacts with KIF23; the interaction is direct (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi205072. 41 interactions.
DIPiDIP-42340N.
IntActiQ9WVM1. 44 interactions.
MINTiMINT-1202825.
STRINGi10090.ENSMUSP00000023756.

Structurei

3D structure databases

ProteinModelPortaliQ9WVM1.
SMRiQ9WVM1. Positions 283-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini350 – 540191Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 286180Interaction with SLC26A8By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili33 – 11078Sequence analysisAdd
BLAST

Domaini

The coiled coil region is indispensible for localization to the midbody during cytokinesis.By similarity
The phorbol-ester/DAG-type zinc finger domain mediates interaction with membranes enriched in phosphatidylinositol 3,4,5-trisphosphate and is required during mitotic cytokinesis for normal attachment of the midbody to the cell membrane.By similarity

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri287 – 33650Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG3564. Eukaryota.
ENOG410XPK0. LUCA.
GeneTreeiENSGT00840000129703.
HOGENOMiHOG000230702.
HOVERGENiHBG062009.
InParanoidiQ9WVM1.
KOiK16733.
OMAiIRELLMC.
OrthoDBiEOG7K0ZBT.
PhylomeDBiQ9WVM1.
TreeFamiTF318102.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WVM1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTTMVNLWT LFEQLVRRME IINEGNESIE FIQVVKDFED FRKKYQRTNQ
60 70 80 90 100
ELEKFKDLLL KAETGRSALD VKLKHARNQV DVEIKRRQRA EAECAKLEQQ
110 120 130 140 150
IQLIRDILMC DTSGSIQLSE EQKSALAFLN RGQASSGHAG NNRLSTIDES
160 170 180 190 200
GSILSDISFD KTDESLDWDS SLVKNFKMKK REKRRSNSRQ FIDGPPGPVK
210 220 230 240 250
KTCSIGSTVD QANESIVAKT TVTVPSDGGP IEAVSTIETL PSWTRSRGKS
260 270 280 290 300
GPLQPVNSDS ALNSRPLEPR TDTDNLGTPQ NTGGMRLHDF VSKTVIKPES
310 320 330 340 350
CVPCGKRIKF GKLSLKCRDC RLVSHPECRD RCPLPCIPPL VGTPVKIGEG
360 370 380 390 400
MLADFVSQAS PMIPAIVVSC VNEIEQRGLT EAGLYRISGC DRTVKELKEK
410 420 430 440 450
FLKVKTVPLL SKVDDIHVIC SLLKDFLRNL KEPLLTFWLS KAFMEAAEIT
460 470 480 490 500
DEDNSTAAMY QAVSELPQAN RDTLAFLMIH LQRVSQSPDT KMDIANLAKV
510 520 530 540 550
FGPTIVAHTV PNPDPVTMFQ DIKRQLKVVE RLLSLPLEYW NQFMMVDQEN
560 570 580 590 600
IDSQRGNGNS TPRTPDVKVS LLGPVTTPEF QLVKTPLSSS LSQRLYNLSK
610 620
STPRFGNKSK SATNLGQQGK FFPAPYLK
Length:628
Mass (Da):70,158
Last modified:November 1, 1999 - v1
Checksum:i8D1B9DEC3CE057BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 313IEF → MES in BAE38561 (PubMed:16141072).Curated
Sequence conflicti100 – 1001Q → E in BAE40131 (PubMed:16141072).Curated
Sequence conflicti100 – 1001Q → E in BAE40010 (PubMed:16141072).Curated
Sequence conflicti398 – 3981K → E in BAE40005 (PubMed:16141072).Curated
Sequence conflicti623 – 6231P → T in BAE40005 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079974 mRNA. Translation: AAD40487.1.
AB030252 mRNA. Translation: BAA90248.1.
AF212320 mRNA. Translation: AAG43539.1.
AF212321 mRNA. Translation: AAG43540.1.
AK144608 mRNA. Translation: BAE25967.1.
AK154929 mRNA. Translation: BAE32931.1.
AK165897 mRNA. Translation: BAE38446.1.
AK166084 mRNA. Translation: BAE38561.1.
AK168020 mRNA. Translation: BAE40005.1.
AK168025 mRNA. Translation: BAE40010.1.
AK168170 mRNA. Translation: BAE40131.1.
AK168679 mRNA. Translation: BAE40528.1.
BC010715 mRNA. Translation: AAH10715.1.
CCDSiCCDS27825.1.
RefSeqiNP_001240737.1. NM_001253808.1.
NP_001240738.1. NM_001253809.1.
NP_036155.1. NM_012025.7.
XP_011243948.1. XM_011245646.1.
UniGeneiMm.273804.

Genome annotation databases

EnsembliENSMUST00000023756; ENSMUSP00000023756; ENSMUSG00000023015.
ENSMUST00000171702; ENSMUSP00000126417; ENSMUSG00000023015.
GeneIDi26934.
KEGGimmu:26934.
UCSCiuc007xpx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079974 mRNA. Translation: AAD40487.1.
AB030252 mRNA. Translation: BAA90248.1.
AF212320 mRNA. Translation: AAG43539.1.
AF212321 mRNA. Translation: AAG43540.1.
AK144608 mRNA. Translation: BAE25967.1.
AK154929 mRNA. Translation: BAE32931.1.
AK165897 mRNA. Translation: BAE38446.1.
AK166084 mRNA. Translation: BAE38561.1.
AK168020 mRNA. Translation: BAE40005.1.
AK168025 mRNA. Translation: BAE40010.1.
AK168170 mRNA. Translation: BAE40131.1.
AK168679 mRNA. Translation: BAE40528.1.
BC010715 mRNA. Translation: AAH10715.1.
CCDSiCCDS27825.1.
RefSeqiNP_001240737.1. NM_001253808.1.
NP_001240738.1. NM_001253809.1.
NP_036155.1. NM_012025.7.
XP_011243948.1. XM_011245646.1.
UniGeneiMm.273804.

3D structure databases

ProteinModelPortaliQ9WVM1.
SMRiQ9WVM1. Positions 283-546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205072. 41 interactions.
DIPiDIP-42340N.
IntActiQ9WVM1. 44 interactions.
MINTiMINT-1202825.
STRINGi10090.ENSMUSP00000023756.

PTM databases

iPTMnetiQ9WVM1.
PhosphoSiteiQ9WVM1.

Proteomic databases

EPDiQ9WVM1.
MaxQBiQ9WVM1.
PaxDbiQ9WVM1.
PRIDEiQ9WVM1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023756; ENSMUSP00000023756; ENSMUSG00000023015.
ENSMUST00000171702; ENSMUSP00000126417; ENSMUSG00000023015.
GeneIDi26934.
KEGGimmu:26934.
UCSCiuc007xpx.2. mouse.

Organism-specific databases

CTDi29127.
MGIiMGI:1349423. Racgap1.

Phylogenomic databases

eggNOGiKOG3564. Eukaryota.
ENOG410XPK0. LUCA.
GeneTreeiENSGT00840000129703.
HOGENOMiHOG000230702.
HOVERGENiHBG062009.
InParanoidiQ9WVM1.
KOiK16733.
OMAiIRELLMC.
OrthoDBiEOG7K0ZBT.
PhylomeDBiQ9WVM1.
TreeFamiTF318102.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-MMU-983189. Kinesins.

Miscellaneous databases

ChiTaRSiRacgap1. mouse.
PROiQ9WVM1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVM1.
CleanExiMM_RACGAP1.
ExpressionAtlasiQ9WVM1. baseline and differential.
GenevisibleiQ9WVM1. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a transcript for a novel Rac GTPase-activating protein in terminally differentiating 3T3-L1 adipocytes."
    Wooltorton E.J., Haliotis T., Mueller C.R.
    DNA Cell Biol. 18:265-273(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Erythroleukemia1 Publication.
  2. "MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells."
    Kawashima T., Hirose K., Satoh T., Kaneko A., Ikeda Y., Kaziro Y., Nosaka T., Kitamura T.
    Blood 96:2116-2124(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  3. "Mice with a homozygous gene trap vector insertion in mgcRacGAP die during pre-implantation development."
    Van de Putte T., Zwijsen A., Lonnoy O., Rybin V., Cozijnsen M., Francis A., Baekelandt V., Kozak C.A., Zerial M., Huylebroeck D.
    Mech. Dev. 102:33-44(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: CD-1Imported.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported, DBA/2JImported and NODImported.
    Tissue: HeartImported and LungImported.
  5. "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].
    Strain: FVB/NImported.
    Tissue: Mammary glandImported.
  6. "Structure and expression of murine mgcRacGAP: its developmental regulation suggests a role for the Rac/MgcRacGAP signalling pathway in neurogenesis."
    Arar C., Ott M.-O., Toure A., Gacon G.
    Biochem. J. 343:225-230(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells."
    Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D., Chardin P., Gacon G.
    Biochem. J. 372:105-112(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564; THR-577 AND THR-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiRGAP1_MOUSE
AccessioniPrimary (citable) accession number: Q9WVM1
Secondary accession number(s): Q3THR5, Q3TI41, Q3TM81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.