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 Q9JLV2

Entry ID Method Resolution Chain Position Source
AF-Q9JLV2-F1 Predicted AlphaFoldDB

30 variants for Q9JLV2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388601179 58 T>VSDG* No EVA
rs3388601660 60 T>I No EVA
rs3388605229 98 L>H No EVA
rs3388605316 162 M>L No EVA
rs3388606594 170 L>M No EVA
rs3388605563 216 G>VSDG* No EVA
rs3388607468 218 K>E No EVA
rs3388596970 253 I>F No EVA
rs3388596980 276 S>N No EVA
rs3388601652 310 S>* No EVA
rs250781560 347 E>D No EVA
rs3388601152 421 N>D No EVA
rs13466894 421 N>K No EVA
rs3388601150 448 C>Y No EVA
rs3388601625 455 K>R No EVA
rs3392498661 459 L>V No EVA
rs3388601144 481 L>P No EVA
rs3388601165 560 L>P No EVA
rs3388605599 591 K>R No EVA
rs3388602956 601 N>S No EVA
rs3388598651 632 T>I No EVA
rs3388595553 636 D>Y No EVA
rs3388603025 652 E>D No EVA
rs3388605518 662 V>M No EVA
rs3388605552 674 N>K No EVA
rs3388605603 674 N>Y No EVA
rs3388605724 681 L>Q No EVA
rs3388607458 720 K>N No EVA
rs3388605299 726 L>F No EVA
rs3388601119 788 M>K No EVA

No associated diseases with Q9JLV2

No regional properties for Q9JLV2

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9JLV2

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, perinuclear region
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
Cul4-RING E3 ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul4 family and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
Cul4A-RING E3 ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.

2 GO annotations of molecular function

Name Definition
phosphatase binding Binding to a phosphatase.
ubiquitin ligase-substrate adaptor activity The binding activity of a molecule that brings together a ubiquitin ligase and its substrate. Usually mediated by F-box BTB/POZ domain proteins.

4 GO annotations of biological process

Name Definition
hair follicle maturation A developmental process, independent of morphogenetic (shape) change, that is required for a hair follicle to attain its fully functional state.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
ubiquitin-dependent protein catabolic process via the C-end degron rule pathway The chemical reactions and pathways resulting in the breakdown of a protein or peptide covalently tagged with ubiquitin, via the DesCEND (destruction via C-end degron) pathway. In the DesCEND pathway, C-terminal residues (C-end degrons) in substrates are recognized by Cul2-RING and Cul4-RING E3 ligases, whereupon the substrates are linked to ubiquitin and then delivered to the proteasome for degradation. C-end degrons can be present in full-length proteins, truncated proteins or proteolytically cleaved forms.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAAAPAAAGA GASRGRRLAA TAAAWGGWGG RPRPGNILLQ LRQGQLTGRG LVRAVQFTET
70 80 90 100 110 120
FLTERDKLSK WSGIPQLLLK LYATSHLHSD FVECQSILKE ISPLLSMEAM AFVTEDRKFT
130 140 150 160 170 180
QEATYPNTYI FDLFGGVDLL VEILMRPTIS IRGQKLKISD EMSKDCLSIL YNTCVCTEGV
190 200 210 220 230 240
TKRLAEKNDF VIFLFTLMTS KKTFLQTATL IEDILGVKKE MIRLDEVPNL SSLVSNFDQQ
250 260 270 280 290 300
QLANFCRILA VTISEMDTGN DDKHTLLAKN AQQKKSLSLG PSAAEINQAA LLSIPGFVER
310 320 330 340 350 360
LCKLATRKVS ESTGTASFLQ ELEEWYTWLD NALVLDALMR VANEESEHNQ APTVFPSLGT
370 380 390 400 410 420
SEEGGLPHTS ARAQLPQSMK IMHEIMYKLE VLYVLCVLLM GRQRNQVHRM IAEFKLIPGL
430 440 450 460 470 480
NNLFDKLIWR KHSASALVLH GHNQNCDCSP DITLKIQFLR LLQSFSDHHE NKYLLLNNQE
490 500 510 520 530 540
LNELSAISLK ANIPEVEAVL NTDRSLVCDG KRGLLTRLLQ VMKKEPAESS FRFWQARAVE
550 560 570 580 590 600
SFLRGTTSYA DQMFLLKRGL LEHILYCIVD SECKSRDVLQ SYFDLLGELM KFNVDAFKRF
610 620 630 640 650 660
NKYINTDAKF QVFLKQINSS LVDSNMLVRC VTLSLDRFEN QVDMKVAEVL SECRLLAYIS
670 680 690 700 710 720
QVPTQMSFLF RLINIIHVQT LTQENVSCLN TSLVILMLAR RKERLPLYLR LLQRMEHSKK
730 740 750 760 770 780
YPGFLLNNFH NLLRFWQQHY LHKDKDSTCL ENSSCISFSY WKETVSILLN PDRQSPSALV
790
SYIEEPYMDI DRDFTEE