wanglab/gogpt-training-data huggingface dataset:
Protein: Chromatin structure-remodeling complex subunit rsc4 (Bromodomain-containing protein brd1) (RSC complex subunit rsc4) (Q09948)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Chromatin structure-remodeling complex subunit rsc7
- Chromatin structure-remodeling complex subunit rsc9
- Chromatin structure-remodeling complex subunit sfh1
- Chromatin structure-remodeling complex subunit rsc58
- Chromatin structure-remodeling complex subunit rsc1
- SWI/SNF and RSC complexes subunit arp9
- SWI/SNF and RSC complexes subunit arp42
- SWI/SNF and RSC complexes subunit ssr3
- SWI/SNF and RSC complexes subunit ssr2
- SWI/SNF and RSC complexes subunit ssr1
Sequence:
MVDDSHNAPFDKTKFDEVLEALVGLKDNEGNPFDDIFEELPSKRYFPDYYQIIQKPICYKMMRNKAKTGKYLSMGDFYDDIRLMVSNAQTYNMPGSLVYECSVLIANTANSLESKDGTLNEEENEEMESSINEEHKPGTNEIDVPKVIQNILDALHEEKDEQGRFLIDIFIDLPSKRLYPDYYEIIKSPMTIKMLEKRFKKGEYTTLESFVKDLNQMFINAKTYNAPGSFVYEDAEKLSQLSSSLISSFSEQPKEHSPATSKHEPEETPASPTPSVSASTSRERSTSVAPSFITSDQAATPDVLKSEEAHVESFSKESEKDQTPIPEDVPSPMDTLSQANYGAFALIKSFPSTPVPDFLNFSHKSVMGRSTFNMPNFPEPKFFEDIPNTERCILSAFICSPPQLPLPNPLRMYLPCPSLNSTEVSVITLAPQHSFLNIVINLNPALALKSYTIITLLNGKRLGAGVSTPPSTLYALEGIKHTEEPIRTVYEAKLSVGLNCLEFVLGSTEPVEPPSIEPGLPASAYSRTVERERFVLMAYVQP
Protein: Alkaline phosphatase L (L-AP) (EC 3.1.3.1) (Low-molecular-weight alkaline phosphatase A) (Protein DING) (P35482)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Has both a phosphomonoesterase and phosphodiesterase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:11985723, ECO:0000269|PubMed:8454193}. Periplasm {ECO:0000269|PubMed:8454193}. Note=Secreted and to some extent periplasmic (PubMed:8454193). Secretion is hxc-dependent and xcp-independent (PubMed:11985723). {ECO:0000269|PubMed:11985723, ECO:0000269|PubMed:8454193}.
Interaction partners:
- Phosphate transport system permease protein PstA
- Phosphate import ATP-binding protein PstB
- Phosphate-specific transport system accessory protein PhoU homolog
- Membrane protein component of ABC phosphate transporter
- Phosphate regulon sensor protein PhoR
- DNA repair protein
- Phosphate regulon transcriptional regulatory protein PhoB
- ShlB/FhaC/HecB family hemolysin secretion/activation protein
- Phosphate transporter
- Porin
Sequence:
MFKRSLIAASLSVAALVSAQAMAVTGGGASLPAELYKGSADSILPANFSYAVTGSGTGKNAFLTNNSSLFGTTGTVHYAGSDSVLSGSELTTYNSNYNGTYGPLIQIPSVATSVTVPYRKDGNTTLNLTSAQLCDAFSGAKTTWGQLLGTTDSTPIRIVYRTGSSGTTELFTRHLNSICPTRFATNSTFTNARLPAGGTLPSNWVGVAATSTVVSTVKATNGSLGYVSPDAVNINSNAEVSRVNGNLPTQANVSTALGSVAPPANAADRADPSKWVPVFTNPSAGYSIVGYTNFVFGQCYKDASVSTDVRAFINKHYGGTTTNAAVAAHGFIPLTPAWKSAIVSAFYTGTSENLAIGNTNVCNTKGRP
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (Q8T046)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004438}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004438}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004438}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004387}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004387}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004387}.
Interaction partners:
Sequence:
MTAAPYNYNYIFKYIIIGDMGVGKSCLLHQFTEKKFMANCPHTIGVEFGTRIIEVDDKKIKLQIWDTAGQERFRAVTRSYHRGAAGALMVYDITRRSTYNHLSSWLTDTRNLTNPSTVIFLIGNKSDLESTREVTYEEAKEFADENGLMFLEASAMTGQNVEEAFLETARKIYQNIQEGRLDLNASESGVQHRPSQPSRTSLSSEATGAKDQCSC
Protein: Transcriptional modulator WTM2 (Q12206)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional modulator with roles in meiotic regulation and silencing.
Interaction partners:
- Transcriptional modulator WTM1
- Ribonucleoside-diphosphate reductase small chain 2
- Chromatin modification-related protein EAF3
- Histone deacetylase RPD3
- Probable histone deacetylase HOS2
- Transcriptional regulatory protein SDS3
- Histone acetyltransferase type B catalytic subunit
- Transcriptional regulatory protein PHO23
- Transcriptional regulatory protein RCO1
- Transcriptional regulatory protein SIN3
Sequence:
MAKSKSSQGASGARRKPAPSLYQHISSFKPQFSTRVDDVLHFSKTLTWRSEIIPDKSKGTLTTSLLYSQGSDIYEIDTTLPLKTFYDDDDDDDNDDDDEEGNGKTKSAATPNPEYGDAFQDVEGKPLRPKWIYQGETVAKMQYLESSDDSTAIAMSKNGSLAWFRDEIKVPVHIVQEMMGPATRYSSIHSLTRPGSLAVSDFDVSTNMDTVVKSQSNGYEEDSILKIIDNSDRPGDILRTVHVPGTNVAHSVRFFNNHLFASCSDDNILRFWDTRTADKPLWTLSEPKNGRLTSFDSSQVTENLFVTGFSTGVIKLWDARAVQLATTDLTHRQNGEEPIQNEIAKLFHSGGDSVVDILFSQTSATEFVTVGGTGNVYHWDMEYSFSRNDDDNEDEVRVAAPEELQGQCLKFFHTGGTRRSSNQFGKRNTVALHPVINDFVGTVDSDSLVTAYKPFLASDFIGRGYDD
Protein: UDP-glycosyltransferase 73C10 (EC 2.4.1.368) (Oleanolate 3-O-glucosyltransferase UGT73C10) (K4GKX2)
Organism: Barbarea vulgaris (Yellow rocket) (Erysimum barbarea)
Function: Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc to the C-3 position of the oleanane sapogenins oleanolate and hederagenin, and to the C-28 carboxylic group of the lupane sapogenin betulinate. The monoglucosylated hederagenin 3-O-beta-D-glucoside is a feeding deterrent of the yellow-striped flea beetle (Phyllotreta nemorum).
Interaction partners:
Sequence:
MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFENVLSRAIESGLPISIVQVKLPSQEAGLPEGNETFDSLVSTKLLVPFFKAVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNREILENLKSDKEHFVVPYFPDRVEFTRPQVPLATYVPGEWHEIKEDMVEADKTSYGVIVNTYQELEPAYANGYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLDSKEEGSVLYVCLGSICSLPLSQLKELGLGLEESQRPFIWVVRGWEKNKELLEWFSESGFEERVKDRGLLIKGWSPQMLILAHHSVGGFLTHCGWNSTLEGITSGVPLLTWPLFGDQFCNQKLVVQVLKVGVSAGVEEVTNWGEEEKIGVLVDKEGVKKAVEELMGESDDAKEIRKRVKELGQLAHKAVEEGGSSHSNITSLLEDIMQLAQPNN
Protein: Prestin (Solute carrier family 26 member 5) (Q9EPH0)
Organism: Rattus norvegicus (Rat)
Function: Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity).
Subcellular location: Lateral cell membrane {ECO:0000269|PubMed:11125015, ECO:0000269|PubMed:11867734, ECO:0000305|PubMed:11274441}; Multi-pass membrane protein {ECO:0000269|PubMed:24710176}. Note=Lateral membrane of outer hair cells (PubMed:11125015, PubMed:11867734). Alters profoundly the shape of its surrounding lipid bilayer (By similarity). {ECO:0000250|UniProtKB:P58743, ECO:0000269|PubMed:11125015, ECO:0000269|PubMed:11867734}.
Interaction partners:
- Hepatic sodium/bile acid cotransporter
- Transmembrane channel-like protein
- Carboxypeptidase D
- Potassium voltage-gated channel subfamily KQT member 4
- Unconventional myosin-VI
- Oncomodulin
Sequence:
MDHAEENEIPAETQKYLVERPIFSHPVLQERLHVKDKVTDSIGDKLKQAFTCTPKKVRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLHESYSVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGICNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYTVLGQLPDTDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSSALKRKTGVNPAIIMGARRKAMRKYAKEVGNANIANATVVKVDAEVDGENATKPEEEDDEVKFPPIVIKTTFPEELQRFLPQGENIHTVILDFTQVNFMDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTSNRFFENPALKELLFHSIHDAVLGSQVREAMAEQETTVLPPQEDMEPNATPTTPEA
Protein: Protein X (HBx) (Peptide X) (pX) (Q89246)
Organism: Woodchuck hepatitis virus
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04074}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04074}. Host mitochondrion {ECO:0000256|HAMAP-Rule:MF_04074}. Note=Mainly cytoplasmic as only a fraction is detected in the nucleus. In cytoplasm, a minor fraction associates with mitochondria or proteasomes. {ECO:0000256|HAMAP-Rule:MF_04074}.
Interaction partners:
Sequence:
MAARLCCHLDSARDVLLLRPFGPQSSGPPFPRPSAGSAASPASSLSTSDESDFPLGRLPACFASASGPCCLVFTCAELRTMDSTVNFVSWHANRQLGMPSKDLWTPYIKDQLLTKWEEGSIDPRLSIFVLGGCRHKCMRLL
Protein: Ethylene-responsive transcription factor 1A (AtERF1A) (Ethylene-responsive element-binding factor 1A) (EREBP-1A) (O80337)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSMTADSQSDYAFLESIRRHLLGESEPILSESTASSVTQSCVTGQSIKPVYGRNPSFSKLYPCFTESWGDLPLKENDSEDMLVYGILNDAFHGGWEPSSSSSDEDRSSFPSVKIETPESFAAVDSVPVKKEKTSPVSAAVTAAKGKHYRGVRQRPWGKFAAEIRDPAKNGARVWLGTFETAEDAALAYDRAAFRMRGSRALLNFPLRVNSGEPDPVRIKSKRSSFSSSNENGAPKKRRTVAAGGGMDKGLTVKCEVVEVARGDRLLVL
Protein: Protein transport protein SEC20 (P28791)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: SNARE required for targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:1537327}; Single-pass type IV membrane protein {ECO:0000269|PubMed:1537327}.
Interaction partners:
- Protein transport protein TIP20
- Protein transport protein USE1
- Protein transport protein SEC22
- Syntaxin UFE1
- Protein transport protein DSL1
- Protein transport protein SEC39
- Synaptobrevin homolog YKT6
- Protein transport protein BOS1
- Protein transport protein BET1
- Integral membrane protein SED5
Sequence:
MVVTFLQDLEVLQDALLNNLQKLSAISRRKESGESKHDNKDSFAAIANEHNDEEEEIEFEDLVNIIESKVSDFESVLKCSIVEMTYKYPELKLQWEKSPRYDQCDKLHIVKLDKQMNEDIYAQLVEELDFVLQFVDWFYCYRLKVKEILRQHHKRDLAWNDEKRDRAIKFHAVDYDKLHQGTSSSSSLTSTSMEKASTREKLLSKTKQLTNNLVRGNQILQSGILQSDLNLDELRAQTNSLTQIDDKYTQFETVFKKTADLVKVLENASHQEKRDVYLSLGFLLCCVSWVLWRRIFKLPVKLGLWLLFKFFKGILVTLGLVKSYAGSSSSLQAPSLVLNAPILATTTTSSATSVEPFASVSAVSSIQRAVDEAVDRIVSHDEL
Protein: Retinoic acid induced 1 (A8MXE8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQSFRERCGFHGKQQNYQQTSQETSRLENYRQPSQAGLSCDRQRLLAKDYYNPQPYPSYEGGAGTPSGTAAAVAADKYHRGSKALPTQQGLQGRPAFPGYGVQDSSPYPGRYAGEESLQAWGAPQPPPPQPQPLPAGVAKYDENLMKKTAVPPSRQYAEQGAQVPFRTHSLHVQQPPPPQQPLAYPKLQRQKLQNDIASPLPFPQGTHFPQHSQSFPTSSTYSSSVQGGGQGAHSYKSCTAPTAQPHDRPLTASSSLAPGQRVQNLHAYQSGRLSYDQQQQQQQQQQQQQQALQSRHHAQETLHYQNLAKYQHYGQQGQGYCQPDAAVRTPEQYYQTFSPSSSHSPARSVGRSPSYSSTPSPLMPNLENFPYSQQPLSTGAFPAGITDHSHFMPLLNPSPTDATSSVDTQAGNCKPLQKDKLPENLLSDLSLQSLTALTSQVENISNTVQQLLLSKAAVPQKKGVKNLVSRTPEQHKSQHCSPEGSGYSAEPAGTPLSEPPSSTPQSTHAEPQEADYLSGSEDPLERSFLYCNQARGSPARVNSNSKAKPESVSTCSVTSPDDMSTKSDDSFQSLHGSLPLDSFSKFVAGERDCPRLLLSALAQEDLASEILGLQEAIGEKADKAWAEAPSLVKDSSKPPFSLENHSACLDSVAKSAWPRPGEPEALPDSLQLDKGGNAKDFSPGLFEDPSVAFATPDPKKTTGPLSFGTKPTLGVPAPDPTTAAFDCFPDTTAASSADSANPFAWPEENLGDACPRWGLHPGELTKGLEQGGKASDGISKGDTHEASACLGFQEEDPPGEKVASLPGDFKQEEVGGVKEEAGGLLQCPEVAKADRWLEDSRHCCSTADFGDLPLLPPTSRKEDLEAEEEYSSLCELLGSPEQRPGMQDPLSPKAPLICTKEEVEEVLDSKAGWGSPCHLSGESVILLGPTVGTESKVQSWF
Protein: ATP-dependent Clp protease proteolytic subunit 2 (EC 3.4.21.92) (Endopeptidase Clp 2) (P9WPC3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit 1
- ATP-dependent Clp protease ATP-binding subunit ClpX
- ATP-dependent Clp protease ATP-binding subunit ClpC1
- Chaperone protein ClpB
- Trigger factor
- Co-chaperonin GroES
- Uncharacterized protein Rv2667
- Nucleoid-associated protein Rv3716c
- Hydrolase
- Large ribosomal subunit protein uL11
Sequence:
MNSQNSQIQPQARYILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLESLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAVLLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLMETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLSAQTA
Protein: Toll-like receptor 4 (Toll4) (CD antigen CD284) (Q9QX05)
Organism: Rattus norvegicus (Rat)
Function: Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (By similarity). Activated by the signaling pathway regulator NMI which acts as damage-associated molecular patterns (DAMPs) in response to cell injury or pathogen invasion, therefore promoting nuclear factor NF-kappa-B activation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O00206}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O00206}. Early endosome {ECO:0000250|UniProtKB:O00206}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9QUK6}. Note=Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis. Colocalizes with RFTN1 at cell membrane and then together with RFTN1 moves to endosomes, upon lipopolysaccharide stimulation. {ECO:0000250|UniProtKB:O00206}.
Interaction partners:
- High mobility group protein B1
- TNF receptor-associated factor 6
- Myeloid differentiation primary response protein MyD88
- Monocyte differentiation antigen CD14
- Toll/interleukin-1 receptor domain-containing adapter protein
- Platelet glycoprotein 4
- Toll-like receptor 2
- High mobility group protein B1
- TIR domain-containing adapter molecule 2
- 60 kDa heat shock protein, mitochondrial
Sequence:
MMPLLHLAGTLIMALFLSCLRPGSLNPCIEVLPNITYQCMDQNLSKIPHDIPYSTKNLDLSFNPLKILRSYSFTNFSQLQWLDLSRCEIETIEDKAWHGLNQLSTLVLTGNPIKSFSPGSFSGLTNLENLVAVETKMTSLEGFHIGQLISLKKLNVAHNLIHSFKLPEYFSNLTNLEHVDLSYNYIQTISVKDLQFLRENPQVNLSLDLSLNPIDSIQAQAFQGIRLHELTLRSNFNSSNVLKMCLQNMTGLHVHRLILGEFKNERNLESFDRSVMEGLCNVSIDEFRLTYINHFSDDIYNLNCLANISAMSFTGVHIKHIADVPRHFKWQSLSIIRCHLKPFPKLSLPFLKSWTLTTNREDISFGQLALPSLRYLDLSRNAMSFRGCCSYSDFGTNNLKYLDLSFNGVILMSANFMGLEELEYLDFQHSTLKKVTEFSVFLSLEKLLYLDISYTNTKIDFDGIFLGLISLNTLKMAGNSFKDNTLSNVFTNTTNLTFLDLSKCQLEQISRGVFDTLYRLQLLNMSHNNLLFLDPSHYKQLYSLRTLDCSFNRIETSKGILQHFPKSLAVFNLTNNSVACICEYQNFLQWVKDQKMFLVNVEQMKCASPIDMKASLVLDFTNSTCYIYKTIISVSVVSVLVVATVAFLIYHFYFHLILIAGCKKYSRGESIYDAFVIYSSQNEDWVRNELVKNLEEGVPRFQLCLHYRDFIPGVAIAANIIQEGFHKSRKVIVVVSRHFIQSRWCIFEYEIAQTWQFLSSRSGIIFIVLEKVEKSLLRQQVELYRLLSRNTYLEWEDNALGRHIFWRRLKKALLDGKALNPDETSEEEQEATTLT
Protein: Protein disulfide isomerase Creld2 (EC 5.3.4.1) (Cysteine-rich with EGF-like domain protein 2) (Q9CYA0)
Organism: Mus musculus (Mouse)
Function: Protein disulfide isomerase (Probable). Might play a role in the unfolded protein response (Probable). May regulate transport of alpha4-beta2 neuronal acetylcholine receptor (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6UXH1}.
Interaction partners:
- Stromal cell-derived factor 2-like protein 1
- Mesencephalic astrocyte-derived neurotrophic factor
- DnaJ homolog subfamily B member 11
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A4
- Hypoxia up-regulated protein 1
- Endoplasmin
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Protein disulfide-isomerase A6
- Derlin-3
Sequence:
MHLLLAAAFGLLLLLPPPGAVASRKPTMCQRCRTLVDKFNQGMANTARKNFGGGNTAWEEKTLSKYEFSEIRLLEIMEGLCDSSDFECNQLLEQQEEQLEAWWQTLKKEHPNLFEWFCVHTLKACCLPGTYGPDCQECQGGSERPCSGNGYCSGDGSRQGDGSCQCHTGYKGPLCIDCTDGFFSLQRNETHSICSACDESCKTCSGPSNKDCIQCEVGWARVEDACVDVDECAAETSPCSDGQYCENVNGSYTCEDCDSTCVGCTGKGPANCKECIAGYTKESGQCTDIDECSLEEKACKRKNENCYNVPGSFVCVCPEGFEETEDACVQTAEGKVTEENPTQPPSREDL
Protein: Enriched in surface-labeled proteome protein 11 (Q583Y1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRSVCLLLLSLVMHANGNFFGISLENRCQPLSSLKGVNRAILNKSGEEYKESDELFCERGAPEQFKCNCGVATTCLSKKDPWGNNIGVCGCCPPWLFLFYTFFTIIVGFAIASAFYICCCRGKWWFDGYPKAIIPAFSRRGPGTVVPAAVPLPPTLFRGYRTTDFVNDTAATRPVVDGESAGTRTQREGASSLWNNDQIVDDEP
Protein: FI18627p1 (NTPase, isoform E (EC 3.6.1.42, EC 3.6.1.6, EC 3.6.1.64)) (Q9VQI8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTNTDVRKRKLATDEKPPRRKSSGSPNASSGGNRGPSGLKISFLCLIISVILLLFVFGFVSENASPYLARLASKFGYSKVQYAAIIDAGSTGSRVLAYKFNRSFIDNKLVLYEELFKERKPGLSSFADNPAEGAHSIKLLLDEARAFIPKEHWSSTPLVLKATAGLRLLPASKAENILNAVRDLFAKSEFSVDMDAVEIMDGTDEGIFSWFTVNFLLGRLSKTNQAAALDLGGGSTQVTFSPTDPDQVPVYDKYMHEVVTSSKKINVFTHSYLGLGLMAARHAVFTHGYKKEDTVLESVCVNPIIANRTWTYGNVQYKVSGKENGKSSAEQPIVDFDACLELVKSKVMPLVKPKPFTLKQHAVAAFSYYFERAIESGLVDPLAGGETTVEAYRKKAQEICAIPNDEQPFMCFDLTFISTLLREGFGLNDGKKIKLYKKIDGHEISWALGCAYNVLTSDEKFSNS
Protein: Katanin p60 ATPase-containing subunit A-like 2 (Katanin p60 subunit A-like 2) (EC 5.6.1.1) (p60 katanin-like 2) (Q8IYT4)
Organism: Homo sapiens (Human)
Function: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03025}. Cytoplasm {ECO:0000269|PubMed:26929214}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26929214}. Note=Localizes within the cytoplasm, partially overlapping with microtubules in interphase and to the mitotic spindle and spindle poles during mitosis. {ECO:0000269|PubMed:26929214}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 12
- UBX domain-containing protein 7
- 26S proteasome non-ATPase regulatory subunit 1
- Katanin p80 WD40 repeat-containing subunit B1
Sequence:
MELSYQTLKFTHQAREACEMRTEARRKNLLILISHYLTQEGYIDTANALEQETKLGLRRFEVCDNIDLETILMEYESYYFVKFQKYPKIVKKSSDTAENNLPQRSRGKTRRMMNDSCQNLPKINQQRPRSKTTAGKTGDTKSLNKEHPNQEVVDNTRLESANFGLHISRIRKDSGEENAHPRRGQIIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDLPSREARQAMIYHWLPPVSKSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKIFDALENHQSESSDLPRIQLDIVTTADFLDVLTHTKPSAKNLAQRYSDWQREFESV
Protein: Inner membrane protein YiaW (P0ADK4)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YiaV
Sequence:
MFLDYFALGVLIFVFLVIFYGIIILHDIPYLIAKKRNHPHADAIHVAGWVSLFTLHVIWPFLWIWATLYRPERGWGMQSHDSSVMQLQQRIAGLEKQLADIKSSSAE
Protein: Fructose-1,6-bisphosphate aldolase (FBP aldolase) (EC 4.1.2.13) (Q9JXV5)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Enolase
- Transketolase
- Transaldolase
- Fructose-1,6-bisphosphatase class 1
- Glucose-6-phosphate isomerase 1
- Glucose-6-phosphate isomerase 2
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Sequence:
MALVSMRQLLDHAAENSYGLPAFNVNNLEQMRAIMEAADQVDAPVIVQASAGARKYAGAPFLRHLILAAVEEFPHIPVVMHQDHGASPDVCQRSIQLGFSSVMMDGSLMEDGKTPSSYEYNVNATRTVVNFSHACGVSVEGEIGVLGNLETGEAGEEDGVGAVGKLSHDQMLTSVEDAVCFVKDTGVDALAIAVGTSHGAYKFTRPPTGDVLRIDRIKEIHQALPNTHIVMHGSSSVPQEWLKVINEYGGNIGETYGVPVEEIVEGIKHGVRKVNIDTDLRLASTGAVRRYLAENPSDFDPRKYLSKTIEAMKQICLDRYLAFGCEGQAGKIKPVSLEKMASRYAKGELNQIVK
Protein: [histone H3]-trimethyl-L-lysine(9) demethylase (EC 1.14.11.66) (F1LS62)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Lysine-specific histone demethylase
- Lysine-specific demethylase 3A
- Histone H3.1
- Histone H3
- Histone H3.3
- Androgen receptor
- Hypoxia-inducible factor 1-alpha
- Histone-lysine N-methyltransferase
Sequence:
MEVVEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKPMTVKEFRQLANSSKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRNDMVKISMDIFVKKFQPDRYQIWKQGKDIYTIDHTKPTPESTPEVKTWLQRRKKLRKAPKSLQGNKSLSKRPKAEEDEEFAEFIGEEVSSPAVCPRHLKVTEKPEKFKLANIGASSEKEASDTRIQVDQSLTNDTKLSGKSCINSSVIDEIQPENDTANAVTSPSTLKKASDLIPFSHGHITGKESRLLKILQLESPKIPSSLAESNRVLTEGEENDEEGHASNLEPGEVPDALSEERNGLNVPKIIEGQPKTTKSWRHPLGKPPARSPMTLVKQQVASDEELPEVLSIDEEVEETESWAKPLIHLWQTKSPNFMAEQEYNATVAKMEPNCAICTLLMPYYKPDNSKEENDSRWETAVNEVVQSGRKTKPIIPEMCFIYSEENVEYSPPNAFLEEDGTSLLISCSKCFVRVHASCYGVPSHEVCDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNQWAHVICAVAVPEVRFTNVPERTQIDVDRIPLQRLKLKCIFCRQRVKRVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHRVNSNVKSKTCEKAISVGQTVITKHRNTRYYSCRVIDVTSQIFYEVMFDDGSFSRDTFPEDIVSRNCVKLGPPAEGEVIQVKWPDGKLYGAKYLGSNVAYMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADVIQGERKRQRVLSSRLKNEYVDDPVYRTFLKSSFQKKCQKRQ
Protein: Amyloid beta precursor like protein 1 (F5GZ08)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLASLEKDKTAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRSGSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPGTPDPSGTAVGDPSTRSWPPGSRVEGAEDEEEEESFPQPVDDYFVEPPQAEEEEETVPPPSSHTLAVVGKVTPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVHTHLQVIEERVNQSLGLLDQNPHLAQELRPQIQELLHSEHLGPSELEAPAPGGSSEDKGGLQPPDSKDDTPMTLPKGSTEQDAASPEKEKMNPLEQYERKVNASVPRGFPFHSSEIQRDELAPAGTGVSREAVSGLLIMGAGGGSLIVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP