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

3 structures for P36102

Entry ID Method Resolution Chain Position Source
4CYK NMR - A 1-41 PDB
4XR7 X-ray 380 A B/C/E/F/H/I/K/L 226-679 PDB
AF-P36102-F1 Predicted AlphaFoldDB

14 variants for P36102

Variant ID(s) Position Change Description Diseaes Association Provenance
s11-391743 60 M>I No SGRP
s11-391636 96 N>I No SGRP
s11-391614 103 M>I No SGRP
s11-391594 110 A>D No SGRP
s11-391595 110 A>T No SGRP
s11-391592 111 S>A No SGRP
s11-391528 132 N>S No SGRP
s11-391353 190 D>E No SGRP
s11-391355 190 D>N No SGRP
s11-390565 453 F>S No SGRP
s11-390381 514 D>E No SGRP
s11-390322 534 G>V No SGRP
s11-390307 539 S>N No SGRP
s11-390179 582 V>I No SGRP

No associated diseases with P36102

3 regional properties for P36102

Type Name Position InterPro Accession
domain Zinc finger, CCCH-type 8 - 37 IPR000571
domain Protein kinase domain 299 - 549 IPR000719
domain Pan3 pseudokinase domain 540 - 676 IPR041332

Functions

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

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
P-body A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing.
PAN complex A complex that possesses poly(A)-specific ribonuclease activity; catalyzes the message-specific shortening of mRNA poly(A) tails. Contains at least two subunits, known as Pan2p and Pan3p in Saccharomyces.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
poly(A) binding Binding to a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
RNA binding Binding to an RNA molecule or a portion thereof.

5 GO annotations of biological process

Name Definition
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
mRNA processing Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
nuclear-transcribed mRNA poly(A) tail shortening Shortening of the poly(A) tail of a nuclear-transcribed mRNA from full length to an oligo(A) length.
postreplication repair The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication. Includes pathways that remove replication-blocking lesions in conjunction with DNA replication.
protein phosphorylation The process of introducing a phosphate group on to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDKINPDWAK DIPCRNITIY GYCKKEKEGC PFKHSDNTTA TTINDVPPPI DVGEATTPTM
70 80 90 100 110 120
TSVPKFNAKV SASFTPMTVG SDSLTTVTNT TSAATNATGN IAMAATSATA STVNPMINPI
130 140 150 160 170 180
VNSSLVNNNN NNSNISISIP TTASSSNYDP FNAPIFTPSS TSSIHTNANA HSFPFPSIAN
190 200 210 220 230 240
SGGININATD DNSNNMSMAN NVPPPMQPPP IESSNLKYPR IYPPPHSLLQ YHLYAPEQPS
250 260 270 280 290 300
SLKSLLKPNE RSADQLFIPN NIREDLTKKN LSILQVFPSS GKVIPSIVQD YFNLVPLNFN
310 320 330 340 350 360
NNDFLNKTTL FKVFSNYDGK AYVLKRLPNI DKSMNPNKIS KIYQIWSKIN CTNLIKFRDI
370 380 390 400 410 420
FQTTKFGDLS ICLVFDYYPN SLSLYDYHFV NFPKFPITNN YLWIYLVQLT NVINSIHSQN
430 440 450 460 470 480
LSIGNTLNWR KVLITGDPGR IKLSHCNFMD LLFNDDTDTV VSSGGSTIEG QQQLDYKYLG
490 500 510 520 530 540
ELLFNLSINI ENSNNNTAPK EYRLEEITPQ SIDDMRQIDD KFKDVLKYLI SDNGDSKKSI
550 560 570 580 590 600
HDLTSHFYDK MFMVLESSQT YTEYMESVLS RELENGRLFR LVNKLNCIFG RIESRIDINW
610 620 630 640 650 660
SESGTKFPII LFYDYVFHQV DSNGKPIMDL THVLRCLNKL DAGIQEKLML VTPDELNCII
670
ISYKELKDLI ESTFRSITQ