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Protein

Rho GTPase-activating protein 17

Gene

ARHGAP17

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

Functioni

Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca2+-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1.2 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW

GO - Biological processi

  1. regulation of small GTPase mediated signal transduction Source: Reactome
  2. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 17
Alternative name(s):
Rho-type GTPase-activating protein 17
RhoGAP interacting with CIP4 homologs protein 1
Short name:
RICH-1
Gene namesi
Name:ARHGAP17
Synonyms:RICH1
ORF Names:MSTP066, MSTP110
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:18239. ARHGAP17.

Subcellular locationi

Membrane; Peripheral membrane protein. Cytoplasm. Cell junctiontight junction
Note: Associates with membranes and concentrates at sites of cell-cell contact.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. plasma membrane Source: Ensembl
  3. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi288 – 2881R → A: Loss of function; leading to defects in tight junction maintenance. 1 Publication

Organism-specific databases

PharmGKBiPA134908575.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 881881Rho GTPase-activating protein 17PRO_0000280462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei575 – 5751Phosphoserine2 Publications
Modified residuei679 – 6791Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ68EM7.
PaxDbiQ68EM7.
PRIDEiQ68EM7.

PTM databases

PhosphoSiteiQ68EM7.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed at higher level in heart and placenta.1 Publication

Gene expression databases

BgeeiQ68EM7.
ExpressionAtlasiQ68EM7. baseline and differential.
GenevestigatoriQ68EM7.

Organism-specific databases

HPAiHPA041703.

Interactioni

Subunit structurei

Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMOTQ4VCS52EBI-1642807,EBI-2511319
AMOTQ4VCS5-24EBI-1642807,EBI-3891843

Protein-protein interaction databases

BioGridi120424. 30 interactions.
IntActiQ68EM7. 7 interactions.
MINTiMINT-195688.

Structurei

3D structure databases

ProteinModelPortaliQ68EM7.
SMRiQ68EM7. Positions 25-232, 246-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 246233BARPROSITE-ProRule annotationAdd
BLAST
Domaini252 – 442191Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi753 – 76614SH3-bindingSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi521 – 816296Pro-richAdd
BLAST

Domaini

The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions.1 Publication

Sequence similaritiesi

Contains 1 BAR domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiNOG329716.
GeneTreeiENSGT00760000118863.
HOVERGENiHBG000015.
InParanoidiQ68EM7.
OMAiSICHHSH.
OrthoDBiEOG7MKW5G.
PhylomeDBiQ68EM7.
TreeFamiTF350627.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00721. BAR. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q68EM7-1) [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
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL
60 70 80 90 100
VACFQGQHGT DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA
110 120 130 140 150
ENQLALELSQ HEVFVEKEIV DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS
160 170 180 190 200
VRARWNQAHK SSGTNFQGLP SKIDTLKEEM DEAGNKVEQC KDQLAADMYN
210 220 230 240 250
FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH QDKWAEKPAF
260 270 280 290 300
GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK
310 320 330 340 350
AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV
360 370 380 390 400
QDQDKKLQDL WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA
410 420 430 440 450
IVLGPNLLWA RNEGTLAEMA AATSVHVVAV IEPIIQHADW FFPEEVEFNV
460 470 480 490 500
SEAFVPLTTP SSNHSFHTGN DSDSGTLERK RPASMAVMEG DLVKKESFGV
510 520 530 540 550
KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP EPPPQSSRAE
560 570 580 590 600
SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG
610 620 630 640 650
QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH
660 670 680 690 700
PGGQSSSGTS QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR
710 720 730 740 750
YSSSLSPIQA PNHPPPQPPT QATPLMHTKP NSQGPPNPMA LPSEHGLEQP
760 770 780 790 800
SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA GGNPETAQPH AGTLPRPRPV
810 820 830 840 850
PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDS NSRVSEPHRS
860 870 880
IFPEMHSDSA SKDVPGRILL DIDNDTESTA L
Length:881
Mass (Da):95,437
Last modified:October 11, 2004 - v1
Checksum:i92029DBFFEAD1001
GO
Isoform 2 (identifier: Q68EM7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     497-574: Missing.

Show »
Length:803
Mass (Da):87,609
Checksum:i9F42C390ACBAFADA
GO
Isoform 3 (identifier: Q68EM7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-273: Missing.

Note: No experimental confirmation available.

Show »
Length:608
Mass (Da):64,267
Checksum:i8060364C667A5535
GO
Isoform 4 (identifier: Q68EM7-4) [UniParc]FASTAAdd to Basket

Also known as: RICH1B

The sequence of this isoform differs from the canonical sequence as follows:
     215-226: LLEAQADYHRKA → ISGRKNQPLGLP
     227-881: Missing.

Show »
Length:226
Mass (Da):25,760
Checksum:iC849839D16E68AE1
GO
Isoform 5 (identifier: Q68EM7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     839-881: DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → GFQNRIAASFLKCTQTQPAKTCLAASCWI

Note: No experimental confirmation available.

Show »
Length:867
Mass (Da):93,855
Checksum:iB2797018F447B1FF
GO
Isoform 6 (identifier: Q68EM7-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     840-881: SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → V

Show »
Length:840
Mass (Da):90,929
Checksum:i333F5437A7222C79
GO
Isoform 7 (identifier: Q68EM7-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-467: Missing.
     468-496: TGNDSDSGTLERKRPASMAVMEGDLVKKE → MCGFNTCGPMGFCLSSLLAWCVDCFFSLC

Note: No experimental confirmation available.

Show »
Length:414
Mass (Da):42,512
Checksum:iB20A13496205E5A8
GO

Sequence cautioni

The sequence AAH01241.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAQ13586.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAQ13632.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391K → E in BAB55203. (PubMed:14702039)Curated
Sequence conflicti167 – 1671Q → R in CAC37948. (PubMed:11431473)Curated
Sequence conflicti186 – 1861K → R in CAC37948. (PubMed:11431473)Curated
Sequence conflicti255 – 2551E → A in BAB14506. (PubMed:14702039)Curated
Sequence conflicti404 – 4041G → A in BAB55203. (PubMed:14702039)Curated
Sequence conflicti575 – 5751S → C in BAC86144. (PubMed:14702039)Curated
Sequence conflicti855 – 8551M → V in BAB55203. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 467467Missing in isoform 7. 1 PublicationVSP_023682Add
BLAST
Alternative sequencei1 – 273273Missing in isoform 3. 1 PublicationVSP_023683Add
BLAST
Alternative sequencei215 – 22612LLEAQ…YHRKA → ISGRKNQPLGLP in isoform 4. 1 PublicationVSP_023684Add
BLAST
Alternative sequencei227 – 881655Missing in isoform 4. 1 PublicationVSP_023685Add
BLAST
Alternative sequencei468 – 49629TGNDS…LVKKE → MCGFNTCGPMGFCLSSLLAW CVDCFFSLC in isoform 7. 1 PublicationVSP_023686Add
BLAST
Alternative sequencei497 – 57478Missing in isoform 2. 2 PublicationsVSP_023687Add
BLAST
Alternative sequencei839 – 88143DSNSR…ESTAL → GFQNRIAASFLKCTQTQPAK TCLAASCWI in isoform 5. 1 PublicationVSP_023688Add
BLAST
Alternative sequencei840 – 88142SNSRV…ESTAL → V in isoform 6. 1 PublicationVSP_023689Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ306731 mRNA. Translation: CAC37948.1.
AJ306732 mRNA. Translation: CAC37949.1.
AK001170 mRNA. No translation available.
AK023281 mRNA. Translation: BAB14506.1.
AK027567 mRNA. Translation: BAB55203.1.
AK125358 mRNA. Translation: BAC86144.1.
AK291691 mRNA. Translation: BAF84380.1.
AL833975 mRNA. Translation: CAD38819.1.
BC001241 mRNA. Translation: AAH01241.1. Different initiation.
BC080195 mRNA. Translation: AAH80195.1.
AF163257 mRNA. Translation: AAQ13586.1. Different initiation.
AF173885 mRNA. Translation: AAQ13632.1. Different initiation.
CCDSiCCDS32408.1. [Q68EM7-2]
CCDS32409.1. [Q68EM7-1]
PIRiF59433.
RefSeqiNP_001006635.1. NM_001006634.2. [Q68EM7-1]
NP_060524.4. NM_018054.5. [Q68EM7-2]
XP_005255471.1. XM_005255414.1. [Q68EM7-6]
UniGeneiHs.373793.

Genome annotation databases

EnsembliENST00000289968; ENSP00000289968; ENSG00000140750. [Q68EM7-1]
ENST00000303665; ENSP00000303130; ENSG00000140750. [Q68EM7-2]
GeneIDi55114.
KEGGihsa:55114.
UCSCiuc002dmy.3. human. [Q68EM7-7]
uc002dna.3. human. [Q68EM7-1]
uc002dnc.3. human. [Q68EM7-2]
uc002dng.1. human. [Q68EM7-4]

Polymorphism databases

DMDMi74736331.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ306731 mRNA. Translation: CAC37948.1.
AJ306732 mRNA. Translation: CAC37949.1.
AK001170 mRNA. No translation available.
AK023281 mRNA. Translation: BAB14506.1.
AK027567 mRNA. Translation: BAB55203.1.
AK125358 mRNA. Translation: BAC86144.1.
AK291691 mRNA. Translation: BAF84380.1.
AL833975 mRNA. Translation: CAD38819.1.
BC001241 mRNA. Translation: AAH01241.1. Different initiation.
BC080195 mRNA. Translation: AAH80195.1.
AF163257 mRNA. Translation: AAQ13586.1. Different initiation.
AF173885 mRNA. Translation: AAQ13632.1. Different initiation.
CCDSiCCDS32408.1. [Q68EM7-2]
CCDS32409.1. [Q68EM7-1]
PIRiF59433.
RefSeqiNP_001006635.1. NM_001006634.2. [Q68EM7-1]
NP_060524.4. NM_018054.5. [Q68EM7-2]
XP_005255471.1. XM_005255414.1. [Q68EM7-6]
UniGeneiHs.373793.

3D structure databases

ProteinModelPortaliQ68EM7.
SMRiQ68EM7. Positions 25-232, 246-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120424. 30 interactions.
IntActiQ68EM7. 7 interactions.
MINTiMINT-195688.

PTM databases

PhosphoSiteiQ68EM7.

Polymorphism databases

DMDMi74736331.

Proteomic databases

MaxQBiQ68EM7.
PaxDbiQ68EM7.
PRIDEiQ68EM7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000289968; ENSP00000289968; ENSG00000140750. [Q68EM7-1]
ENST00000303665; ENSP00000303130; ENSG00000140750. [Q68EM7-2]
GeneIDi55114.
KEGGihsa:55114.
UCSCiuc002dmy.3. human. [Q68EM7-7]
uc002dna.3. human. [Q68EM7-1]
uc002dnc.3. human. [Q68EM7-2]
uc002dng.1. human. [Q68EM7-4]

Organism-specific databases

CTDi55114.
GeneCardsiGC16M024931.
HGNCiHGNC:18239. ARHGAP17.
HPAiHPA041703.
MIMi608293. gene.
neXtProtiNX_Q68EM7.
PharmGKBiPA134908575.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG329716.
GeneTreeiENSGT00760000118863.
HOVERGENiHBG000015.
InParanoidiQ68EM7.
OMAiSICHHSH.
OrthoDBiEOG7MKW5G.
PhylomeDBiQ68EM7.
TreeFamiTF350627.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiARHGAP17. human.
GenomeRNAii55114.
NextBioi58744.
PROiQ68EM7.
SOURCEiSearch...

Gene expression databases

BgeeiQ68EM7.
ExpressionAtlasiQ68EM7. baseline and differential.
GenevestigatoriQ68EM7.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00721. BAR. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1."
    Richnau N., Aspenstroem P.
    J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FNBP1 AND TRIP10, MUTAGENESIS OF ARG-288.
  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] (ISOFORMS 1; 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 634-881 (ISOFORM 5).
    Tissue: Placenta and Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    Tissue: Brain.
  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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-881 (ISOFORM 6).
    Tissue: Cervix and Eye.
  5. Liu Y.Q., Zhao B., Xu Y.Y., Wang X.Y., Liu B., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-881.
    Tissue: Aorta.
  6. "Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP."
    Reczek D., Bretscher A.
    J. Cell Biol. 153:191-206(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A3R1.
  7. "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
    Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
    Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAR, INTERACTION WITH AMOT; MPP5; INADL; PARD3; CAPZA; CAPZB; CD2AP AND SH3KBP1.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRHG17_HUMAN
AccessioniPrimary (citable) accession number: Q68EM7
Secondary accession number(s): A8K6M6
, Q6ZUS4, Q7Z2F2, Q8NDG2, Q96KS2, Q96KS3, Q96SS8, Q9BVF6, Q9H8U5, Q9NW54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2004
Last modified: January 7, 2015
This is version 101 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.