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 Q95216

Entry ID Method Resolution Chain Position Source
AF-Q95216-F1 Predicted AlphaFoldDB

No variants for Q95216

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q95216

No associated diseases with Q95216

2 regional properties for Q95216

Type Name Position InterPro Accession
domain Glycoside hydrolase family 20, catalytic domain 174 - 490 IPR015883
domain Beta-hexosaminidase, eukaryotic type, N-terminal 32 - 152 IPR029019

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm
  • Nucleus, nucleolus
  • Nucleus, nucleoplasm
  • Cytoplasmic and nuclear localization in the presence of prolactin
  • Nuclear localization is stimulated by progesterone
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.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

7 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP-dependent chromatin remodeler activity An activity, driven by ATP hydrolysis, that modulates the contacts between histones and DNA, resulting in a change in chromosome architecture within the nucleosomal array, leading to chromatin remodeling.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
helicase activity Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Catalysis of the hydrolysis of any acid anhydride which contains phosphorus.
transferase activity Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
protein ubiquitination The process in which one or more ubiquitin groups are added 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
MSWMFKRDPV WKYLQTVQYG VHGNFSRLSY PTFFPRFEFQ DIIPPDDFLT SDEELDSVLF
70 80 90 100 110 120
GTLRGHVVGL RYYTGVVNNN EMVALQREPN NPYDKNAIKV NNVNGNQVGY LKKELAAALA
130 140 150 160 170 180
YIMDNKLAQI EGVVPYGANN AFTMPLQMTF WGKEENRKAV LDQLKKHGFK LGPAPKTLGF
190 200 210 220 230 240
SLESGWGSGR AGPSYSMPVH AAIQMTTEQL KTEFDKLFED LKEDDKTQEM EPAEAVETPL
250 260 270 280 290 300
LPHQKQALAW MVSRENSREL PPFWELRNDL YYNTITNFSE KDQPENVHGG ILADDMGLGK
310 320 330 340 350 360
TLTAIAVILT NFHDGKPLPV ERMKKNQVKK ECNSSESDKP GRKDTIKKTD GLSKEGSRYS
370 380 390 400 410 420
EEPSISDVKK NKYSMSELSS SQPKRKKIAV QYIESSDSEE IEISELPQKM KGKLKNVQSE
430 440 450 460 470 480
TKRVKVGPSK IKEDTAFACA LTSSASTTTK KILKKGASAQ RVQRKLMFEE RPRTTLIICP
490 500 510 520 530 540
LSVLSNWIDQ FGQHIKSDVH LNFYVYYGPD RIRDPALLSK QDIVLTTYNI LTHDYGTKGD
550 560 570 580 590 600
SPLHSIRWLR VILDEGHAIR NPNAQQTKAV LDLEAERRWV LTGTPIQNSL KDLWSLLSFL
610 620 630 640 650 660
KLKPFVDREW WHRTIQRPVT MGDEGGLRRL QSLIKNITLR RTKTSKIKGK PVLELPERPV
670 680 690 700 710 720
FIQHITLSDE ERKIYQSVKS EGKATIGRYF NEGTVLAHYA DVLGLLLRLR QICCHTHLLT
730 740 750 760 770 780
NTVSSSGPSG NDTPEELRKK LIKKMKLILS SGSDEECAIC LDSLTVPVIT HCAHVFCKPC
790 800 810 820 830 840
ICQCIQNEQP HAKCPLCRND IHGDNLLECP PEELACDSEK KSNMEWTSSS KINALMHALI
850 860 870 880 890 900
DLRTKNPNIK SLVVSQFTTF LSLIETPLKA SGFVFTRLDG SMAQKKRVES IQCFQNTEAG
910 920 930 940 950 960
SPTIMLLSLK AGGVGLNLCA ASRVFLMDPA WNPAAEDQRF DRCHRLGQKQ EVIITKFIVK
970 980 990 1000
DSVEENMLKI QNTKRELAAG AFGTKKNANE MKQAKINEIR TLIDL