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Protein

Rho GTPase-activating protein 44

Gene

ARHGAP44

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

Functioni

GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP-bound states. May act as a GAP for CDC42 and RAC1. Endosomal recycling protein which, in association with SHANK3, is involved in synaptic plasticity. Promotes GRIA1 exocytosis from recycling endosomes and spine morphological changes associated to long-term potentiation.1 Publication

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • phospholipid binding Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Exocytosis

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 44
Alternative name(s):
NPC-A-10
Rho-type GTPase-activating protein RICH2
RhoGAP interacting with CIP4 homologs protein 2
Short name:
RICH-2
Gene namesi
Name:ARHGAP44
Synonyms:KIAA0672, RICH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:29096. ARHGAP44.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: Reactome
  • dendritic spine Source: UniProtKB-SubCell
  • leading edge membrane Source: FlyBase
  • recycling endosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Endosome, Synapse

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiARHGAP44.
DMDMi121948837.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 818818Rho GTPase-activating protein 44PRO_0000280480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei493 – 4931PhosphoserineBy similarity
Modified residuei809 – 8091PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ17R89.
MaxQBiQ17R89.
PaxDbiQ17R89.
PRIDEiQ17R89.

PTM databases

PhosphoSiteiQ17R89.

Expressioni

Tissue specificityi

Highly expressed in brain. Expressed at weak level in other tissues.1 Publication

Gene expression databases

BgeeiQ17R89.
ExpressionAtlasiQ17R89. baseline and differential.
GenevisibleiQ17R89. HS.

Organism-specific databases

HPAiHPA038814.

Interactioni

Subunit structurei

Interacts with BST2 (via cytoplasmic domain). Interacts (probably via PDZ-binding motif) with SHANK3 (via PDZ domain); the interaction takes place in dendritic spines and promotes GRIA1 exocytosis.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TRIP10Q156423EBI-10238335,EBI-739936

Protein-protein interaction databases

BioGridi115241. 14 interactions.
IntActiQ17R89. 2 interactions.
MINTiMINT-1390982.
STRINGi9606.ENSP00000368994.

Structurei

3D structure databases

ProteinModelPortaliQ17R89.
SMRiQ17R89. Positions 4-236, 253-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 249236BARPROSITE-ProRule annotationAdd
BLAST
Domaini255 – 445191Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni731 – 81888Interaction with BST2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi815 – 8184PDZ-bindingCurated

Domaini

Rho-GAP domain is required to promote GRIA1 exocytosis from recycling endosomes. Rho-GAP and BAR domains are necessary for the control of long-term potentiation in hippocampal neurons (By similarity).By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG4270. Eukaryota.
ENOG410XRR2. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000179193.
HOVERGENiHBG000015.
InParanoidiQ17R89.
OMAiYANYFQM.
OrthoDBiEOG7MKW5G.
PhylomeDBiQ17R89.
TreeFamiTF316514.

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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q17R89-1) [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
MKKQFNRMRQ LANQTVGRAE KTEVLSEDLL QVEKRLELVK QVSHSTHKKL
60 70 80 90 100
TACLQGQQGA EADKRSKKLP LTTLAQCLME GSAILGDDTL LGKMLKLCGE
110 120 130 140 150
TEDKLAQELI HFELQVERDV IEPLFLLAEV EIPNIQKQRK HLAKLVLDMD
160 170 180 190 200
SSRTRWQQTS KSSGLSSSLQ PAGAKADALR EEMEEAANRV EICRDQLSAD
210 220 230 240 250
MYSFVAKEID YANYFQTLIE VQAEYHRKSL TLLQAVLPQI KAQQEAWVEK
260 270 280 290 300
PSFGKPLEEH LTISGREIAF PIEACVTMLL ECGMQEEGLF RVAPSASKLK
310 320 330 340 350
KLKAALDCCV VDVQEYSADP HAIAGALKSY LRELPEPLMT FELYDEWIQA
360 370 380 390 400
SNVQEQDKKL QALWNACEKL PKANHNNIRY LIKFLSKLSE YQDVNKMTPS
410 420 430 440 450
NMAIVLGPNL LWPQAEGNIT EMMTTVSLQI VGIIEPIIQH ADWFFPGEIE
460 470 480 490 500
FNITGNYGSP VHVNHNANYS SMPSPDMDPA DRRQPEQARR PLSVATDNMM
510 520 530 540 550
LEFYKKDGLR KIQSMGVRVM DTNWVARRGS SAGRKVSCAP PSMQPPAPPA
560 570 580 590 600
ELAAPLPSPL PEQPLDSPAA PALSPSGLGL QPGPERTSTT KSKELSPGSA
610 620 630 640 650
QKGSPGSSQG TACAGTQPGA QPGAQPGASP SPSQPPADQS PHTLRKVSKK
660 670 680 690 700
LAPIPPKVPF GQPGAMADQS AGQPSPVSLS PTPPSTPSPY GLSYPQGYSL
710 720 730 740 750
ASGQLSPAAA PPLASPSVFT STLSKSRPTP KPRQRPTLPP PQPPTVNLSA
760 770 780 790 800
SSPQSTEAPM LDGMSPGESM STDLVHFDIP SIHIELGSTL RLSPLEHMRR
810
HSVTDKRDSE EESESTAL
Length:818
Mass (Da):89,247
Last modified:July 25, 2006 - v1
Checksum:iFCAC06CEDB522C09
GO
Isoform 2 (identifier: Q17R89-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     509-514: Missing.
     773-774: DL → AV
     775-818: Missing.

Note: Contains a PDZ-binding motif at positions 764-767.
Show »
Length:768
Mass (Da):83,424
Checksum:i04E6F2DEE6094D5D
GO
Isoform 3 (identifier: Q17R89-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     509-514: Missing.

Note: No experimental confirmation available.
Show »
Length:812
Mass (Da):88,521
Checksum:i9E574C0C808B357F
GO

Sequence cautioni

The sequence AAP73805.1 differs from that shown. Reason: Frameshift at position 385. Curated
The sequence AAP73805.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA31647.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461E → G in AAP73805 (Ref. 5) Curated
Sequence conflicti518 – 5181R → M in CAB46376 (PubMed:17974005).Curated
Sequence conflicti674 – 6741P → L in BAA31647 (PubMed:9734811).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti463 – 4631V → M.
Corresponds to variant rs3213688 [ dbSNP | Ensembl ].
VAR_031159

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei509 – 5146Missing in isoform 2 and isoform 3. 3 PublicationsVSP_053616
Alternative sequencei773 – 7742DL → AV in isoform 2. 1 PublicationVSP_053617
Alternative sequencei775 – 81844Missing in isoform 2. 1 PublicationVSP_053618Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014572 mRNA. Translation: BAA31647.2. Different initiation.
AK294538 mRNA. Translation: BAG57745.1.
AC005274 Genomic DNA. No translation available.
AC005277 Genomic DNA. No translation available.
BC117412 mRNA. Translation: AAI17413.1.
BC117416 mRNA. Translation: AAI17417.1.
BC143853 mRNA. Translation: AAI43854.1.
AY320403 mRNA. Translation: AAP73805.1. Sequence problems.
AL096728 mRNA. Translation: CAB46376.1.
CCDSiCCDS45616.1. [Q17R89-1]
PIRiA59433.
RefSeqiNP_055674.4. NM_014859.5. [Q17R89-1]
XP_005256945.1. XM_005256888.1. [Q17R89-3]
XP_005256947.1. XM_005256890.1. [Q17R89-2]
UniGeneiHs.499758.

Genome annotation databases

EnsembliENST00000340825; ENSP00000342566; ENSG00000006740. [Q17R89-3]
ENST00000379672; ENSP00000368994; ENSG00000006740. [Q17R89-1]
GeneIDi9912.
KEGGihsa:9912.
UCSCiuc002gnr.5. human. [Q17R89-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014572 mRNA. Translation: BAA31647.2. Different initiation.
AK294538 mRNA. Translation: BAG57745.1.
AC005274 Genomic DNA. No translation available.
AC005277 Genomic DNA. No translation available.
BC117412 mRNA. Translation: AAI17413.1.
BC117416 mRNA. Translation: AAI17417.1.
BC143853 mRNA. Translation: AAI43854.1.
AY320403 mRNA. Translation: AAP73805.1. Sequence problems.
AL096728 mRNA. Translation: CAB46376.1.
CCDSiCCDS45616.1. [Q17R89-1]
PIRiA59433.
RefSeqiNP_055674.4. NM_014859.5. [Q17R89-1]
XP_005256945.1. XM_005256888.1. [Q17R89-3]
XP_005256947.1. XM_005256890.1. [Q17R89-2]
UniGeneiHs.499758.

3D structure databases

ProteinModelPortaliQ17R89.
SMRiQ17R89. Positions 4-236, 253-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115241. 14 interactions.
IntActiQ17R89. 2 interactions.
MINTiMINT-1390982.
STRINGi9606.ENSP00000368994.

PTM databases

PhosphoSiteiQ17R89.

Polymorphism and mutation databases

BioMutaiARHGAP44.
DMDMi121948837.

Proteomic databases

EPDiQ17R89.
MaxQBiQ17R89.
PaxDbiQ17R89.
PRIDEiQ17R89.

Protocols and materials databases

DNASUi9912.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340825; ENSP00000342566; ENSG00000006740. [Q17R89-3]
ENST00000379672; ENSP00000368994; ENSG00000006740. [Q17R89-1]
GeneIDi9912.
KEGGihsa:9912.
UCSCiuc002gnr.5. human. [Q17R89-1]

Organism-specific databases

CTDi9912.
GeneCardsiARHGAP44.
HGNCiHGNC:29096. ARHGAP44.
HPAiHPA038814.
neXtProtiNX_Q17R89.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4270. Eukaryota.
ENOG410XRR2. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000179193.
HOVERGENiHBG000015.
InParanoidiQ17R89.
OMAiYANYFQM.
OrthoDBiEOG7MKW5G.
PhylomeDBiQ17R89.
TreeFamiTF316514.

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiARHGAP44. human.
GenomeRNAii9912.
NextBioi35462455.
PROiQ17R89.

Gene expression databases

BgeeiQ17R89.
ExpressionAtlasiQ17R89. baseline and differential.
GenevisibleiQ17R89. HS.

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. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 3).
    Tissue: Amygdala.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [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] (ISOFORMS 1 AND 3).
    Tissue: Brain.
  5. "Construction of cDNA expression library from nasopharyngeal carcinoma tissue and screening of antigenic genes."
    Shu J., Li G., He X.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-508 (ISOFORM 1/2).
    Tissue: Nasopharyngeal carcinoma.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 356-758 (ISOFORM 2).
    Tissue: Testis.
  7. "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: FUNCTION AS A GTPASE-ACTIVATING PROTEIN, TISSUE SPECIFICITY.
  8. "A CD317/tetherin-RICH2 complex plays a critical role in the organization of the subapical actin cytoskeleton in polarized epithelial cells."
    Rollason R., Korolchuk V., Hamilton C., Jepson M., Banting G.
    J. Cell Biol. 184:721-736(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BST2.

Entry informationi

Entry nameiRHG44_HUMAN
AccessioniPrimary (citable) accession number: Q17R89
Secondary accession number(s): A6NCP5
, A8MQB2, O75160, Q7Z5Z7, Q9Y4Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 25, 2006
Last modified: May 11, 2016
This is version 87 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 17
    Human chromosome 17: 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

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.