Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6INP9

Entry ID Method Resolution Chain Position Source
AF-Q6INP9-F1 Predicted AlphaFoldDB

No variants for Q6INP9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6INP9

No associated diseases with Q6INP9

3 regional properties for Q6INP9

Type Name Position InterPro Accession
domain SH2 domain 150 - 251 IPR000980
domain Ras guanine-nucleotide exchange factors catalytic domain 534 - 806 IPR001895
domain SHEP1/BCAR3/NSP1, SH2 domain 145 - 280 IPR044102

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
phosphotyrosine residue binding Binding to a phosphorylated tyrosine residue within a protein.

1 GO annotations of biological process

Name Definition
small GTPase mediated signal transduction The series of molecular signals in which a small monomeric GTPase relays a signal.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAAGKFASYH RNVQMNHPLV SSMDLLGSKS ALGERRSDAF KNVCIHGTLP RKKKERVPIR
70 80 90 100 110 120
SSDMFCHMGT LPHTKSHRLP NPLMQDIKED YPFQERRTGI FNMREHYLDP AMEYVKFSKD
130 140 150 160 170 180
RYIMDGGTPD KLKKELEEEL KLNSEDLRSH AWYHGRIPRQ VSESLVKRDG DFLIRDSLSS
190 200 210 220 230 240
PGNLVLTCQW KNLSQHFKIN KVVIRLNEAY CRIQYQLEHE SFDSIPALVR FYVGNRKAVS
250 260 270 280 290 300
QQSGAIIFQP INRTVPLRCI EEKYGTSPVR RLELGIMEVK SEPTKRLSLN FGQGISQEQS
310 320 330 340 350 360
LVRGNLLRNK EKSGSQPACL DNMREKRRPL KAHQSESYLP LGSRQPCLSQ GMDMKTSPKP
370 380 390 400 410 420
HVFRTGSEPT LSPTEIRRFN HEVHPVEALR GSDSQLCPRP PPKPTKAPSI KQSQSPLVWQ
430 440 450 460 470 480
SSEANYCEFH PTPPEDCAWS DSHSSHNSYI EDQRTDEIET LSFSNSELSF PALDDSISQC
490 500 510 520 530 540
SATDFCGNVE DDEFIRPVYE TVSSFCPNDF QSVLLTAENK PLETSLLRRA KELFTNNDPR
550 560 570 580 590 600
TIAKHILRMD CKVARILDVT PEVERMMGVS SGLELIILPY GHQLRLDLME RHSTMAIGIA
610 620 630 640 650 660
VDILGCTGNL EERVATLHKI IQLAVEVKTL GDYFAFSAIM KALDMPQITR LEQTWTMLRH
670 680 690 700 710 720
QYTQTAITYE KQLKPFSKYL HEGEALDAQE DVTVPLVMPL VTLLERQSVL FEGMDFWENN
730 740 750 760 770 780
DRGCEILFNH LQTARQVAHN ATVYKKNAQR ILEGFKPDEL MSEIFKTEFQ MRLLWGSKGA
790 800
LLKQSERYHK FGQILTALSR KLEPPS