Protein Help

NIP100 / YPL174C Protein

Protein abundance data, domains, shared domains with other proteins, protein sequence retrieval for various strains, sequence-based physico-chemical properties, protein modification sites, and external identifiers for the protein.


Aliases
PAC13 3
Feature Type
ORF , Verified

AlphaFold Protein Structure

AlphaFold, developed by DeepMind, is an AI program that accurately predicts protein structures from amino acid sequences, enabling visualization of protein conformations. The predicted structures can be accessed through the Protein Data Bank (PDB) and AlphaFold Protein Structure Database.


Parsing response... [0/0]

Model Confidence

Very high
Confident
Low
Very low

Experimental Data

Contains experimentally-derived protein half-life data obtained using stable isotope labeling by amino acids (SILAC) coupled with mass spectrometry. This section also contains protein abundance data for both untreated and treated cells obtained from over 20 studies. These data have been normalized and converted to a common unit of molecules per cell.


Protein Half Life

No half-life data available for NIP100.

Protein Abundance

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
1202SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
238YEPDuntreatedqualitative western immunoblotting evidenceS288CGhaemmaghami S, et al. (2003)Ho B, et al. (2018)
30YEPDuntreatedquantitative mass spectrometry evidenceS288CKulak NA, et al. (2014)Ho B, et al. (2018)
297YEPDuntreatedquantitative mass spectrometry evidenceS288CWebb KJ, et al. (2013)Ho B, et al. (2018)
Showing 1 to 4 of 4 entries

Domains and Classification - S288C

Collection of computationally identified domains and motifs, as determined by InterProScan analysis; includes protein coordinates for the domain, a domain Description, a Source and corresponding accession ID, and the number of S. cerevisiae genes that share the same domain.


Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Gene Protein Coordinates Accession ID Description Source No. of Genes with Domain

Domain Locations

Visual representation of the locations of the domains within the protein, as listed in the Domains and Classification table. Each row displays the domain(s) derived from a different Source, with domains color-coded according to this Source.

Scroll over a domain to view its exact coordinates and its Description.

Shared Domains

This diagram displays domains (colored squares) shared between the given protein (yellow circle) and other proteins (gray circles); the domains are color-coded according to their source, as displayed in the Domain Locations table, above.

Reset

Click on a gene or domain name to go to its specific page within SGD; drag any of the gene or domain objects around within the visualization for easier viewing; click “Reset” to automatically redraw the diagram.

Alleles

Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.


nip100-Δ

View all NIP100 alleles in SGD search

Sequence

Protein sequence for the given gene in S288C and other strains, when available. Use the pull-down menu under "Strain" to select the sequence for a specific strain. The displayed sequence can be downloaded in FASTA format as a .txt file. Amino acids displayed in blue represent modification sites. More detailed evidence for these modification sites is presented in the Post-translational Modifications table, located just below the protein sequence.


1 MRNAGVQVDT NMQKISLQDT VLVNEMKGRV KFIGETQFAK GIWYGIELDK PLGKNDGSAN
61 GIRYFDIDLK KANSNGGYYG LFCKKDTLQF YKPDDDEHSL LNGNAAQETI KNLQVKCESL
121 ASKLNKIKIE NHELKTSVEK LSTNETVLLS KISRLDKLVK ELKVENGNMK THLDNFNHLL
181 DASDSVMAPD LDKGTLLERS HLLQGLLDQT KLSYDKAMKV QEDLLEENTQ LLEENAVLSK
241 KISDLGLQLQ QTNNTIGDLA LQIEAQSKSS NIVDKLTNDN ILLTSNIKAL NNELEELQAK
301 EKLDENLRIT YEQLEQELRL QLSNLQSALE NEKEIAGTYI EENSRLKATL ESIEAKTSHK
361 FQSLELKVNT LQEELYQNKL LKKFYQIYEP FAQPHLAALS SQLQYLAEVI ESENFGKLEN
421 IEIHIILKVL SSISYALHIY TIKNTPDHLE TTLQCFKVNI APISMWLSEF LQRKFSSKQE
481 TAFSICQFLE DNKFLDKDVT LILKILHPIL ETTVPKLLAF LRTNSNFNDN DTLCLIGSLY
541 ERSLSLIARI DKLIGKEEIS KQDNRLFLYP SCDITLSSIL TILFSDALFL RQDYKRISSL
601 KKLEVFFQGI ESLLENITIF PEQPSQQTSD SESQCNIKEG NFSNSLLSDR LNEENIRLKE
661 VLVQKENMLT ELETKIKIII GRDLERKTLE ENIKTLKVEL NNKNEENCGK TEILNKLKEE
721 NFNLVNRLKN MELKLYQIKD NNTLNKIYLD REKVDRVNLV SEIMELRETI RRQIKEQKRV
781 SIDFSWLDEL PAVENKQPFK EHINHSLDTL GIEMFNFVST SRILDLKLDQ PLAEDELWHE
841 RDHSYISYLK RKRKNIRLKS QNVVTYYK*

* Blue amino acids indicate modification sites. More information below.

Post-translational Modifications - S288C

Modification sites for the protein in the selected strain, based on the presence of a residue in the specific strain, as inferred from experimental evidence.

2 entries for 2 sites

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

SiteModificationModifierReference
S598phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S599phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
Showing 1 to 2 of 2 entries

Sequence-Based Physico-chemical Properties - S288C

Calculated protein properties, including amino acid composition, length, coding region calculations, and atomic composition.

Amino Acid Composition

Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.

Amino AcidFrequencyPercentage
A313.57
C80.92
D485.53
E859.79
F303.46
G263.00
H151.73
I667.60
K859.79
L13215.21
M111.27
N697.95
P151.73
Q465.30
R313.57
S657.49
T455.18
V333.80
W40.46
Y232.65

Physical Details

Length (a.a): 868
Molecular Weight (Da): 100273.5
Isoelectric Point (pl): 5.59
Formula: C4457H7208N1195O1383S19
Aliphatic Index: 98.8
Instability Index: 43.48

Coding Region Translation Calculations

Codon Bias: -0.03
Codon Adaptation Index: 0.12
Frequence of Optimal Codons: 0.42
Hydropathicity of Protein: -0.48
Aromaticity Score: 0.07

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 56770.0
NO Cys residues appear as half cystines: 56270.0

Atomic Composition

Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.

Atom Frequency Percentage

Data not found or not available for  S288C

External Identifiers

List of external identifiers for the protein from various database sources.

19 entries for 9 sources


Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

External IDSource
orf19.486CGD
1473DIP
CAA51030.1GenBank/EMBL/DDBJ
Z73530GenBank/EMBL/DDBJ
X72227GenBank/EMBL/DDBJ
6325083GenBank/EMBL/DDBJ
CAA97881.1GenBank/EMBL/DDBJ
2506257GenBank/EMBL/DDBJ
1370367GenBank/EMBL/DDBJ
2058360GenBank/EMBL/DDBJ
Showing 1 to 10 of 19 entries

Resources