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Protein

Ras-related protein Rap-2c

Gene

RAP2C

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

Functioni

Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May play a role in SRE-mediated gene transcription.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi116 – 1194GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTP binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rap-2c
Gene namesi
Name:RAP2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:21165. RAP2C.

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • cell-cell contact zone Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134899238.

Polymorphism and mutation databases

DMDMi47117343.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Ras-related protein Rap-2cPRO_0000030221Add
BLAST
Propeptidei181 – 1833Removed in mature formBy similarityPRO_0000030222

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi176 – 1761S-palmitoyl cysteineBy similarity
Lipidationi177 – 1771S-palmitoyl cysteineBy similarity
Modified residuei180 – 1801Cysteine methyl esterBy similarity
Lipidationi180 – 1801S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Palmitate, Prenylation

Proteomic databases

EPDiQ9Y3L5.
MaxQBiQ9Y3L5.
PaxDbiQ9Y3L5.
PeptideAtlasiQ9Y3L5.
PRIDEiQ9Y3L5.

PTM databases

iPTMnetiQ9Y3L5.
PhosphoSiteiQ9Y3L5.
SwissPalmiQ9Y3L5.

Expressioni

Tissue specificityi

Expressed in liver, skeletal muscle, prostate, uterus, rectum, stomach, and bladder and to a lower extent in brain, kidney, pancreas, and bone marrow. Expressed in mononuclear leukocytes and megakaryocytes.2 Publications

Gene expression databases

BgeeiQ9Y3L5.
CleanExiHS_RAP2C.
ExpressionAtlasiQ9Y3L5. baseline and differential.
GenevisibleiQ9Y3L5. HS.

Interactioni

Protein-protein interaction databases

BioGridi121785. 20 interactions.
IntActiQ9Y3L5. 3 interactions.
STRINGi9606.ENSP00000340274.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3L5.
SMRiQ9Y3L5. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionCurated

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiQ9Y3L5.
KOiK07839.
OMAiKEKKSYC.
OrthoDBiEOG7QVM41.
PhylomeDBiQ9Y3L5.
TreeFamiTF313014.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y3L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP
60 70 80 90 100
SVLEILDTAG TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI
110 120 130 140 150
VRVKRYEKVP LILVGNKVDL EPEREVMSSE GRALAQEWGC PFMETSAKSK
160 170 180
SMVDELFAEI VRQMNYSSLP EKQDQCCTTC VVQ
Length:183
Mass (Da):20,745
Last modified:November 1, 1999 - v1
Checksum:i6763385F76638324
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351A → V in AAH03403 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY298955 mRNA. Translation: AAP55684.1.
AL049685 mRNA. Translation: CAB41256.1.
AK124801 mRNA. Translation: BAG54098.1.
Z78022 Genomic DNA. Translation: CAI42719.1.
CH471107 Genomic DNA. Translation: EAX11782.1.
BC003403 mRNA. Translation: AAH03403.1.
CCDSiCCDS14632.1.
RefSeqiNP_001258115.1. NM_001271186.1.
NP_001258116.1. NM_001271187.1.
NP_067006.3. NM_021183.4.
XP_011529678.1. XM_011531376.1.
UniGeneiHs.119889.
Hs.743556.

Genome annotation databases

EnsembliENST00000342983; ENSP00000340274; ENSG00000123728.
ENST00000370874; ENSP00000359911; ENSG00000123728.
GeneIDi57826.
KEGGihsa:57826.
UCSCiuc004ewp.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY298955 mRNA. Translation: AAP55684.1.
AL049685 mRNA. Translation: CAB41256.1.
AK124801 mRNA. Translation: BAG54098.1.
Z78022 Genomic DNA. Translation: CAI42719.1.
CH471107 Genomic DNA. Translation: EAX11782.1.
BC003403 mRNA. Translation: AAH03403.1.
CCDSiCCDS14632.1.
RefSeqiNP_001258115.1. NM_001271186.1.
NP_001258116.1. NM_001271187.1.
NP_067006.3. NM_021183.4.
XP_011529678.1. XM_011531376.1.
UniGeneiHs.119889.
Hs.743556.

3D structure databases

ProteinModelPortaliQ9Y3L5.
SMRiQ9Y3L5. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121785. 20 interactions.
IntActiQ9Y3L5. 3 interactions.
STRINGi9606.ENSP00000340274.

PTM databases

iPTMnetiQ9Y3L5.
PhosphoSiteiQ9Y3L5.
SwissPalmiQ9Y3L5.

Polymorphism and mutation databases

DMDMi47117343.

Proteomic databases

EPDiQ9Y3L5.
MaxQBiQ9Y3L5.
PaxDbiQ9Y3L5.
PeptideAtlasiQ9Y3L5.
PRIDEiQ9Y3L5.

Protocols and materials databases

DNASUi57826.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342983; ENSP00000340274; ENSG00000123728.
ENST00000370874; ENSP00000359911; ENSG00000123728.
GeneIDi57826.
KEGGihsa:57826.
UCSCiuc004ewp.5. human.

Organism-specific databases

CTDi57826.
GeneCardsiRAP2C.
HGNCiHGNC:21165. RAP2C.
neXtProtiNX_Q9Y3L5.
PharmGKBiPA134899238.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiQ9Y3L5.
KOiK07839.
OMAiKEKKSYC.
OrthoDBiEOG7QVM41.
PhylomeDBiQ9Y3L5.
TreeFamiTF313014.

Miscellaneous databases

ChiTaRSiRAP2C. human.
GenomeRNAii57826.
PROiQ9Y3L5.

Gene expression databases

BgeeiQ9Y3L5.
CleanExiHS_RAP2C.
ExpressionAtlasiQ9Y3L5. baseline and differential.
GenevisibleiQ9Y3L5. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the human gene RAP2C, a novel member of Ras family, which activates transcriptional activities of SRE."
    Guo Z., Yuan J., Tang W., Chen X., Gu X., Luo K., Wang Y., Wan B., Yu L.
    Mol. Biol. Rep. 34:137-144(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. Rhodes S., Huckle E.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
    Tissue: Caudate nucleus.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Placenta.
  7. "Identification and biochemical characterization of Rap2C, a new member of the Rap family of small GTP-binding proteins."
    Paganini S., Guidetti G.F., Catricala S., Trionfini P., Panelli S., Balduini C., Torti M.
    Biochimie 88:285-295(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GTP-BINDING, TISSUE SPECIFICITY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAP2C_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3L5
Secondary accession number(s): B3KWD6, Q5H9H9, Q9BTS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
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
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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  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.