Overview
| Uniprot ID | Q9NRY4 |
| Protein Name | Rho GTPase-activating protein 35 |
| Gene Name | ARHGAP35 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 1115 |
PHDSTQGKIITIRNI |
| 587 |
RPSDRNQKNSLSDPN |
Function
Rho GTPase-activating protein (GAP) (PubMed:19673492, PubMed:28894085). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:19673492). This binding is inhibited by phosphorylation by PRKCA (PubMed:19673492). Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis (By similarity). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (By similarity). Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (By similarity). Modulates Rho GTPase-dependent F-actin polymerization, organization and assembly, is involved in polarized cell migration and in the positive regulation of ciliogenesis and cilia elongation (By similarity). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (By similarity). Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however unclear and would need additional experimental evidences (PubMed:1894621)
Protein Sequence
10
MMMARKQDVR
20
IPTYNISVVG
30
LSGTEKEKGQ
40
CGIGKSCLCN
50
RFVRPSADEF
60
HLDHTSVLST
70
SDFGGRVVNN
80
DHFLYWGEVS
90
RSLEDCVECK
100
MHIVEQTEFI
110
DDQTFQPHRS
120
TALQPYIKRA
130
AATKLASAEK
140
LMYFCTDQLG
150
LEQDFEQKQM
160
PDGKLLVDGF
170
LLGIDVSRGM
180
NRNFDDQLKF
190
VSNLYNQLAK
200
TKKPIVVVLT
210
KCDEGVERYI
220
RDAHTFALSK
230
KNLQVVETSA
240
RSNVNVDLAF
250
STLVQLIDKS
260
RGKTKIIPYF
270
EALKQQSQQI
280
ATAKDKYEWL
290
VSRIVKNHNE
300
NWLSVSRKMQ
310
ASPEYQDYVY
320
LEGTQKAKKL
330
FLQHIHRLKH
340
EHIERRRKLY
350
LAALPLAFEA
360
LIPNLDEIDH
370
LSCIKAKKLL
380
ETKPEFLKWF
390
VVLEETPWDA
400
TSHIDNMENE
410
RIPFDLMDTV
420
PAEQLYEAHL
430
EKLRNERKRV
440
EMRRAFKENL
450
ETSPFITPGK
460
PWEEARSFIM
470
NEDFYQWLEE
480
SVYMDIYGKH
490
QKQIIDKAKE
500
EFQELLLEYS
510
ELFYELELDA
520
KPSKEKMGVI
530
QDVLGEEQRF
540
KALQKLQAER
550
DALILKHIHF
560
VYHPTKETCP
570
SCPACVDAKI
580
EHLISSRFIR
590
PSDRNQKNSL
600
SDPNIDRINL
610
VILGKDGLAR
620
ELANEIRALC
630
TNDDKYVIDG
640
KMYELSLRPI
650
EGNVRLPVNS
660
FQTPTFQPHG
670
CLCLYNSKES
680
LSYVVESIEK
690
SRESTLGRRD
700
NHLVHLPLTL
710
ILVNKRGDTS
720
GETLHSLIQQ
730
GQQIASKLQC
740
VFLDPASAGI
750
GYGRNINEKQ
760
ISQVLKGLLD
770
SKRNLNLVSS
780
TASIKDLADV
790
DLRIVMCLMC
800
GDPFSADDIL
810
FPVLQSQTCK
820
SSHCGSNNSV
830
LLELPIGLHK
840
KRIELSVLSY
850
HSSFSIRKSR
860
LVHGYIVFYS
870
AKRKASLAML
880
RAFLCEVQDI
890
IPIQLVALTD
900
GAVDVLDNDL
910
SREQLTEGEE
920
IAQEIDGRFT
930
SIPCSQPQHK
940
LEIFHPFFKD
950
VVEKKNIIEA
960
THMYDNAAEA
970
CSTTEEVFNS
980
PRAGSPLCNS
990
NLQDSEEDIE
1000
PSYSLFREDT
1010
SLPSLSKDHS
1020
KLSMELEGND
1030
GLSFIMSNFE
1040
SKLNNKVPPP
1050
VKPKPPVHFE
1060
ITKGDLSYLD
1070
QGHRDGQRKS
1080
VSSSPWLPQD
1090
GFDPSDYAEP
1100
MDAVVKPRNE
1110
EENIYSVPHD
1120
STQGKIITIR
1130
NINKAQSNGS
1140
GNGSDSEMDT
1150
SSLERGRKVS
1160
IVSKPVLYRT
1170
RCTRLGRFAS
1180
YRTSFSVGSD
1190
DELGPIRKKE
1200
EDQASQGYKG
1210
DNAVIPYETD
1220
EDPRRRNILR
1230
SLRRNTKKPK
1240
PKPRPSITKA
1250
TWESNYFGVP
1260
LTTVVTPEKP
1270
IPIFIERCIE
1280
YIEATGLSTE
1290
GIYRVSGNKS
1300
EMESLQRQFD
1310
QDHNLDLAEK
1320
DFTVNTVAGA
1330
MKSFFSELPD
1340
PLVPYNMQID
1350
LVEAHKINDR
1360
EQKLHALKEV
1370
LKKFPKENHE
1380
VFKYVISHLN
1390
KVSHNNKVNL
1400
MTSENLSICF
1410
WPTLMRPDFS
1420
TMDALTATRT
1430
YQTIIELFIQ
1440
QCPFFFYNRP
1450
ITEPPGARPS
1460
SPSAVASTVP
1470
FLTSTPVTSQ
1480
PSPPQSPPPT
1490
PQSPMQPLLP
SQLQAEHTL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0015629 |
actin cytoskeleton |
| Cellular Component |
GO:0036064 |
ciliary basal body |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0005525 |
GTP binding |
| Molecular Function |
GO:0005096 |
GTPase activator activity |
| Molecular Function |
GO:0003924 |
GTPase activity |
| Molecular Function |
GO:0005543 |
phospholipid binding |
| Biological Process |
GO:0007411 |
axon guidance |
| Biological Process |
GO:0007413 |
axonal fasciculation |
| Biological Process |
GO:0016477 |
cell migration |
| Biological Process |
GO:0021955 |
central nervous system neuron axonogenesis |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0030950 |
establishment or maintenance of actin cytoskeleton polarity |
| Biological Process |
GO:0030879 |
mammary gland development |
| Biological Process |
GO:0035024 |
negative regulation of Rho protein signal transduction |
| Biological Process |
GO:0097485 |
neuron projection guidance |
| Biological Process |
GO:0045724 |
positive regulation of cilium assembly |
| Biological Process |
GO:0010976 |
positive regulation of neuron projection development |
| Biological Process |
GO:0032956 |
regulation of actin cytoskeleton organization |
| Biological Process |
GO:0008064 |
regulation of actin polymerization or depolymerization |
| Biological Process |
GO:0050770 |
regulation of axonogenesis |
| Biological Process |
GO:0008361 |
regulation of cell size |
| Biological Process |
GO:0051056 |
regulation of small GTPase mediated signal transduction |
| Biological Process |
GO:0007266 |
Rho protein signal transduction |
| Biological Process |
GO:0044319 |
wound healing, spreading of cells |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.