wanglab/gogpt-training-data huggingface dataset:
Protein: PHD finger-like domain-containing protein 5A (PHD finger-like domain protein 5A) (Splicing factor 3B-associated 14 kDa protein) (SF3b14b) (P83870)
Organism: Mus musculus (Mouse)
Function: Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self-renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation. Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (By similarity). Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12054543, ECO:0000269|PubMed:18758164, ECO:0000269|PubMed:27749823}. Nucleus speckle {ECO:0000269|PubMed:18758164}.
Interaction partners:
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 2
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 3
- Splicing factor 3A subunit 2
- RNA-binding motif protein, X-linked 2
- Small nuclear ribonucleoprotein G
- U5 small nuclear ribonucleoprotein 200 kDa helicase
Sequence:
MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR
Protein: Kinesin heavy chain (Uncoordinated protein 116) (Protein unc-116) (P34540)
Organism: Caenorhabditis elegans
Function: Microtubule-dependent motor protein required for organelle transport. Plays a role in endosome transport. Required for the transport of mitochondria along the axon of motor neurons. Involved in the nuclear migration of hyp7 hypodermal precursor cells. Required for the formation of dendritic branches of PVD sensory neurons. In non-ciliated neurons such as the PVD and PHC neurons, required for the organization of minus-end out microtubules in dendrites. Also required for the minus-end out orientation of microtubules in dendrites of AQR gas-sensing neurons. Involved in the localization of unc-33 to neurites. Positively regulates cilium position and dendrite morphogenesis in the postembryonic AQR and PQR gas-sensing neurons. Plays a more prominent role in regulating dendrite morphogenesis in AQR than in PQR neurons. Plays a role in regulating the localization of grdn-1 to the distal dendrites of AQR sensory neurons.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19605495}.
Interaction partners:
- Kinesin light chain
- Kinesin light chain
- Kinesin 1 cargo adaptor alternative variant a
- JNK-interacting protein
- UNC-76
- Dynein heavy chain, cytoplasmic
- Dynein heavy chain linker domain-containing protein
- Dynein Heavy Chain
- HAP1 N-terminal domain-containing protein
- Mitochondrial Rho GTPase 1
Sequence:
MEPRTDGAECGVQVFCRIRPLNKTEEKNADRFLPKFPSEDSISLGGKVYVFDKVFKPNTTQEQVYKGAAYHIVQDVLSGYNGTVFAYGQTSSGKTHTMEGVIGDNGLSGIIPRIVADIFNHIYSMDENLQFHIKVSYYEIYNEKIRDLLDPEKVNLSIHEDKNRVPYVKGATERFVGGPDEVLQAIEDGKSNRMVAVTNMNEHSSRSHSVFLITVKQEHQTTKKQLTGKLYLVDLAGSEKVSKTGAQGTVLEEAKNINKSLTALGIVISALAEGTKSHVPYRDSKLTRILQESLGGNSRTTVIICASPSHFNEAETKSTLLFGARAKTIKNVVQINEELTAEEWKRRYEKEKEKNTRLAALLQAAALELSRWRAGESVSEVEWVNLSDSAQMAVSEVSGGSTPLMERSIAPAPPMLTSTTGPITDEEKKKYEEERVKLYQQLDEKDDEIQKVSQELEKLRQQVLLQEEALGTMRENEELIREENNRFQKEAEDKQQEGKEMMTALEEIAVNLDVRQAECEKLKRELEVVQEDNQSLEDRMNQATSLLNAHLDECGPKIRHFKEGIYNVIREFNIADIASQNDQLPDHDLLNHVRIGVSKLFSEYSAAKESSTAAEHDAEAKLAADVARVESGQDAGRMKQLLVKDQAAKEIKPLTDRVNMELTTLKNLKKEFMRVLVARCQANQDTEGEDSLSGPAQKQRIQFLENNLDKLTKVHKQLVRDNADLRVELPKMEARLRGREDRIKILETALRDSKQRSQAERKKYQQEVERIKEAVRQRNMRRMNAPQIVKPIRPGQVYTSPSAGMSQGAPNGSNA
Protein: Spermatid maturation protein 1 (Q5F289)
Organism: Mus musculus (Mouse)
Function: Required for proper cytoplasm removal during spermatogenesis.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:17426145}.
Interaction partners:
- Spermatid nuclear transition protein 1
- Ubiquilin-1
- Spermatogenesis-associated protein 3
- Protein chibby homolog 2
Sequence:
MAMAERPRPGWASYQNPNINNCQDMGNSILLLLGLIVCINIGINLVTLLWSRIRILLHRMFHIICEKETSTSLGKLVQPLRKQTYPKVHLRCTMDPVKMTVTPPPTRRRYRHRAPPSRRARCPIAWAPDTDDEKPPHQHPAICSRHWNDSKDWEGFQSMQEVWEPWTQDGLEQPPQTIRFQPAVEARPLKSEIRSDQGLEAYVYTVNPPPPSPEALSHKNNAAGSGGCVEGEQAQGQPVSPSFLGPANVPEIPRRHSSGRIVYDARDVRRRLRELTQEVEALSHCYPLVSGSSAAEGTGKDWVYRPLKGR
Protein: Securin (Pituitary tumor-transforming gene 1 protein) (Q9CQJ7)
Organism: Mus musculus (Mouse)
Function: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of p53/TP53. The negative regulation of p53/TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Separin
- Cell division cycle protein 20 homolog
- Cell division cycle protein 27 homolog
- Ubiquitin-conjugating enzyme E2 C
- Anaphase-promoting complex subunit 11
- Fizzy-related protein homolog
- Cyclin-dependent kinase 1
- Aurora kinase A
- Serine/threonine-protein kinase PLK1
- Mitotic checkpoint serine/threonine-protein kinase BUB1
Sequence:
MATLIFVDKDNEEPGRRLASKDGLKLGTGVKALDGKLQVSTPRVGKVFNAPAVPKASRKALGTVNRVAEKPMKTGKPLQPKQPTLTGKKITEKSTKTQSSVPAPDDAYPEIEKFFPFNPLDFESFDLPEEHQISLLPLNGVPLMTLNEERGLEKLLHLGPPSPLKTPFLSWESDPLYSPPSALSTLDVELPPVCYDADI
Protein: 2-Hydroxyacid oxidase 2 (HAOX2) (EC 1.1.3.15) ((S)-2-hydroxy-acid oxidase, peroxisomal) (Cell growth-inhibiting gene 16 protein) (Long chain alpha-hydroxy acid oxidase) (Long-chain L-2-hydroxy acid oxidase) (Q9NYQ3)
Organism: Homo sapiens (Human)
Function: Oxidase that catalyzes the oxidation of medium and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, to the correspondong 2-oxoacids. Its role in the oxidation of 2-hydroxy fatty acids may contribute to the general pathway of fatty acid alpha-oxidation (Probable). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2. Is not active on glycolate, glyoxylate, L-lactate and 2-hydroxybutanoate.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10777549}.
Interaction partners:
- Alanine--glyoxylate aminotransferase
- Glyoxylate reductase/hydroxypyruvate reductase
- Glycerol-3-phosphate phosphatase
- 2-Hydroxyacid oxidase 1
- Catalase
- 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
- D-amino-acid oxidase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Diphosphomevalonate decarboxylase
- GMP synthase
Sequence:
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLTDLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
Protein: Filamin-binding LIM protein 1 (FBLP-1) (CSX-associated LIM) (Q71FD7)
Organism: Mus musculus (Mouse)
Function: Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion (By similarity).
Subcellular location: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8WUP2}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q8WUP2}. Note=Associated with actin stress fiber at cell-ECM focal adhesion sites. Recruited and localized at actin stress fibers and clustered at cell-EMC adhesion sites through interaction with FERMT2. {ECO:0000250|UniProtKB:Q8WUP2}.
Interaction partners:
- Filamin-A
- Filamin-C
- Fermitin family homolog 2
- Filamin-B
- Vasodilator-stimulated phosphoprotein
- Fermitin family homolog 3
- Fermitin family homolog 1
- Scaffold protein ILK
Sequence:
MASKPEKRVASSVFITLAPPRRDVAVSEEVGQAACEARRARPWEMLPTKTPGAAVGRSPKTWTPSGKTNASLSGVTPQLSNGGCSLPPPSLNEEDLDLPPPPPPPSAYLPLPEEEPPVLPGKSLISDLEQLHLPPPPPPPPPQAPSKGSSVHPPPGHAIPSEEELPPPPEEPVTLPEREVSTDVCGFCHKPVSPRELAVEAMKRQYHAQCFTCRTCRRQLAGQRFYQKDGRPLCEPCYQDTLEKCGKCGEVVQEHVIRALGKAFHPPCFTCVTCARCISDESFALDSQNQVYCVADFYRKFAPVCSICENPIIPRDGKDAFKIECMGRNFHENCYRCEDCSVLLSVEPTDQGCYPLNDHLFCKPCHLKRSAAGCC
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Protein EMBRYO DEFECTIVE 1860) (Q8VYE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the TIM17:23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14730085}; Single-pass membrane protein {ECO:0000269|PubMed:14730085}.
Interaction partners:
- Probable mitochondrial import inner membrane translocase subunit TIM21
- Mitochondrial import inner membrane translocase subunit TIM23-2
- Mitochondrial import inner membrane translocase subunit TIM23-1
- Mitochondrial import inner membrane translocase subunit TIM23-3
- Mitochondrial import inner membrane translocase subunit TIM17-2
- Mitochondrial import receptor subunit TOM40-1
- Mitochondrial import inner membrane translocase subunit TIM44-2
- GrpE protein homolog 1
- Mitochondrial import inner membrane translocase subunit TIM44-1
- Mitochondrial import inner membrane translocase subunit PAM16 like 1
Sequence:
MASIVLRSRLLPRLAKLRSRNLRCFSAEASSTNSTSRYSGVTSTQSMFSDFPPPNQPPPPPPPQVEAAAAAATGKERKGLKYLGYALLWALTGATAATGYASFAYTIDEVNEKTKAFRESATKTPVIKSSGIDVIDKYQTKLYSAAMTGSARAIDKYLELREIVEEQVKGFTEPLSEKLLPDLHPAEQHVFTLVLDLNETLLYTDWKRERGWRTFKRPGVDAFLEHLGKFYEIVVYSDQMEMYVLPVCEKLDPNGYIRYKLARGATKYENGKHYRDLSKLNRDPKKILFVSANAFESTLQPENSVPIKPYKLEADDTALVDLIPFLEYVARNSPADIRPVLASFERKDIAKEFIDRSIEYQKRKQGQLGQGRFWRR
Protein: Odorant binding protein c (Odorant-binding protein 51a) (Q7KE33)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP02289p
- Odorant binding protein b
- Ductus ejaculatorius peptide 99B
- trypsin
- IP02285p
- Andropin
- Uncharacterized protein
- GH21475p
Sequence:
MKVFIGLVLLLAVTTLSSALFESEANECAKKLGITPDYFENFPHSSRVKCFYHCQMEKLEIIANGVVTPFDLKVLNISPESYDKYGVKVKPCLKLSHRDKCELGYLVFQCLKREFNL
Protein: Ninja-family protein AFP3 (ABI five-binding protein 3) (ABI5-binding protein 3) (Q94F39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a negative regulator of abscisic acid (ABA) response and stress responses.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Uncharacterized protein
Sequence:
MSKKQRLSEEDGEVEIELDLGLSLNGRFGVDPLAKTRLMRSTSVLDLVVNDRSGLSRTCSLPVETEEEWRKRKELQSLRRLEAKRKRSEKQRKHKACGGEEKVVEEGSIGSSGSGSSGLSEVDTLLPPVQATTNKSVETSPSSAQSQPENLGKEASQNIIEDMPFVSTTGDGPNGKKINGFLYRYRKGEEVRIVCVCHGSFLSPAEFVKHAGGGDVAHPLKHIVVNPSPFL
Protein: Lysophospholipid acyltransferase 2 (LPLAT 2) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 4) (Lyso-PC acyltransferase 4) (mLPCAT4) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 2) (O-acyltransferase domain-containing protein 2) (Q8R3I2)
Organism: Mus musculus (Mouse)
Function: Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophospholipid leading to the production of a phospholipid and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Catalyzes the acylation of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) and to a lesser extend lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE). Does not acylates lysophosphatidic acid (LPA) and lysophosphatidylserine. Prefers oleoyl-CoA as the acyl donor. May be involved in chondrocyte differentiation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:18287005}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Lysophospholipid acyltransferase LPCAT4
- Lysocardiolipin acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Phosphatidylethanolamine N-methyltransferase
- Choline/ethanolaminephosphotransferase 1
- Phosphatidate cytidylyltransferase 1
Sequence:
MATTSTTGSTLLQPLSNAVQLPIDQVNFVVCQLFALLAAVWFRTYLHSSKTSSFIRHVVATLLGLYLAFFCFGWYALHFLVQSGISYCIMIIAGVESMQQCCFVFALGYLSVCQITRVYIFDYGQYSADFSGPMMIITQKITSLAYEIHDGMFRKDEELTPSQRGLAVRRMPSLLEYVSYTCNFMGILAGPLCSYKDYIAFIEGRASHVAQPSENGKDEQHGKADPSPNAAVTEKLLVCGLSLLFHLTISNMLPVEYNIDEHFQATASWPTKATYLYVSLLAARPKYYFAWTLADAINNAAGFGFRGYDKNGVARWDLISNLRIQQIEMSTSFKMFLDNWNIQTALWLKRVCYERATFSPTIQTFFLSAIWHGVYPGYYLTFLTGVLMTLAARAVRNNFRHYFLEPPQLKLFYDLITWVATQITISYTVVPFVLLSIKPSFTFYSSWYYCLHVCSILVLLLLPVKKSQRRTSTQENVHLSQAKKFDERDNPLGQNSFSTMNNVCNQNRDTGSRHSSLTQ
Protein: Zinc finger protein 366 (Dendritic cell-specific transcript protein) (DC-SCRIPT) (Q8N895)
Organism: Homo sapiens (Human)
Function: Has transcriptional repression activity. Acts as corepressor of ESR1; the function seems to involve CTBP1 and histone deacetylases.
Subcellular location: Nucleus {ECO:0000269|PubMed:16393996, ECO:0000269|PubMed:17085477}.
Interaction partners:
- C-terminal-binding protein 1
Sequence:
MQKEMKMIKDEDVHFDLAVKKTPSFPHCLQPVASRGKAPQRHPFPEALRGPFSQFRYEPPPGDLDGFPGVFEGAGSRKRKSMPTKMPYNHPAEEVTLALHSEENKNHGLPNLPLLFPQPPRPKYDSQMIDLCNVGFQFYRSLEHFGGKPVKQEPIKPSAVWPQPTPTPFLPTPYPYYPKVHPGLMFPFFVPSSSPFPFSRHTFLPKQPPEPLLPRKAEPQESEETKQKVERVDVNVQIDDSYYVDVGGSQKRWQCPTCEKSYTSKYNLVTHILGHSGIKPHACTHCGKLFKQLSHLHTHMLTHQGTRPHKCQVCHKAFTQTSHLKRHMMQHSEVKPHNCRVCGRGFAYPSELKAHEAKHASGRENICVECGLDFPTLAQLKRHLTTHRGPIQYNCSECDKTFQYPSQLQNHMMKHKDIRPYICSECGMEFVQPHHLKQHSLTHKGVKEHKCGICGREFTLLANMKRHVLIHTNIRAYQCHLCYKSFVQKQTLKAHMIVHSDVKPFKCKLCGKEFNRMHNLMGHMHLHSDSKPFKCLYCPSKFTLKGNLTRHMKVKHGVMERGLHSQGLGRGRIALAQTAGVLRSLEQEEPFDLSQKRRAKVPVFQSDGESAQGSHCHEEEEEDNCYEVEPYSPGLAPQSQQLCTPEDLSTKSEHAPEVLEEACKEEKEDASKGEWEKRSKGDLGAEGGQERDCAGRDECLSLRAFQSTRRGPSFSDYLYFKHRDESLKELLERKMEKQAVLLGI
Protein: Vinculin (Metavinculin) (P85972)
Organism: Rattus norvegicus (Rat)
Function: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P12003}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic side {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P12003}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P12003}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19343716}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side {ECO:0000250|UniProtKB:Q64727}. Cell projection, podosome {ECO:0000250|UniProtKB:Q64727}. Note=Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions. {ECO:0000250|UniProtKB:P12003}.
Interaction partners:
- Talin 1
- Talin 2
- Paxillin
- Breast cancer anti-estrogen resistance protein 1
- Zyxin
- Proto-oncogene tyrosine-protein kinase Src
- Filamin, alpha
- Focal adhesion kinase 1
- Vasodilator-stimulated phosphoprotein
- Ribonucleoprotein PTB-binding 1
Sequence:
MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVGKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPNASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGASPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEIAALTSKLGDLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLAAQLADLAARGEGESPQARALASQLQDSLKDLKTQMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGRLGATAEKAAAVGAANKSTVEGIQASVKTARELTPQVISAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
Protein: Cell division protein SepF (D4H018)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Involved in cell division. Probably acts as a membrane anchor for FstZ2, tethering its filaments to the division site. May be involved in septum closure.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:34103513}. Note=Localizes in a ring-like structure at the cell division plane at midcell. Localizes at the future site of cell division straight after the closure of the septum. Co-localizes with FtsZ1 and FtsZ2. FtsZ1 is important for its proper localization. {ECO:0000269|PubMed:34103513}.
Interaction partners:
- Cell division protein FtsZ 1
- Cell division protein FtsZ 2
- UvrABC system protein A
Sequence:
MGIMSKILGGGGSRTTEDYVELDLDDFDTARGDAGLSVHIAEIGGQQDVIAIKDAVYDGNLVIADITRHTTSDSTMEHIIDDLRQVAREVDGDIVQKGDDQIVITPTGISISRQKLNG
Protein: Dolichol kinase (EC 2.7.1.108) (Transmembrane protein 15) (Q9UPQ8)
Organism: Homo sapiens (Human)
Function: Catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis. Dol-P is a lipid carrier essential for the synthesis of N-linked and O-linked oligosaccharides and for GPI anchors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16923818}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- Polyprenal reductase
- Dolichyldiphosphatase 1
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Phosphomannomutase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Cardiolipin synthase
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MTRECPSPAPGPGAPLSGSVLAEAAVVFAVVLSIHATVWDRYSWCAVALAVQAFYVQYKWDRLLQQGSAVFQFRMSANSGLLPASMVMPLLGLVMKERCQTAGNPFFERFGIVVAATGMAVALFSSVLALGITRPVPTNTCVILGLAGGVIIYIMKHSLSVGEVIEVLEVLLIFVYLNMILLYLLPRCFTPGEALLVLGGISFVLNQLIKRSLTLVESQGDPVDFFLLVVVVGMVLMGIFFSTLFVFMDSGTWASSIFFHLMTCVLSLGVVLPWLHRLIRRNPLLWLLQFLFQTDTRIYLLAYWSLLATLACLVVLYQNAKRSSSESKKHQAPTIARKYFHLIVVATYIPGIIFDRPLLYVAATVCLAVFIFLEYVRYFRIKPLGHTLRSFLSLFLDERDSGPLILTHIYLLLGMSLPIWLIPRPCTQKGSLGGARALVPYAGVLAVGVGDTVASIFGSTMGEIRWPGTKKTFEGTMTSIFAQIISVALILIFDSGVDLNYSYAWILGSISTVSLLEAYTTQIDNLLLPLYLLILLMA
Protein: Uncharacterized protein YebG (P0ACY9)
Organism: Escherichia coli (strain K12)
Interaction partners:
- DNA damage-inducible protein I
- LexA repressor
- DNA repair protein RecN
- Protein UmuD
- Protein YebF
- Cell division inhibitor SulA
- DNA damage-inducible protein D
- Holliday junction branch migration complex subunit RuvA
- Protein RecA
- Uncharacterized protein YbfE
Sequence:
MAVEVKYVVIREGEEKMSFTSKKEADAYDKMLDTADLLDTWLTNSPVQMEDEQREALSLWLAEQKDVLSTILKTGKLPSPQVVGAESEEEDASHAA
Protein: Insulin-like growth factor 1 (Insulin-like growth factor I) (Q5U743)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKEVHLKNASRGSAGNKNYRM
Protein: Putative adhesion G protein-coupled receptor F2P (Adhesion G-protein coupled receptor F2) (G-protein coupled receptor 111) (G-protein coupled receptor PGR20) (Q8IZF7)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGLTAYGNRRVQPGELPFGANLTLIHTRAQPVICSKLLLTKRVSPISFFLSKFQNSWGEDGWVQLDQLPSPNAVSSDQVHCSAGCTHRKCGWAASKSKEKVPARPHGVCDGVCTDYSQCTQPCPPDTQGNMGFSCRQKTWHKITDTCQTLNALNIFEEDSRLVQPFEDNIKISVYTGKSETITDMLLQKCPTDLSCVIRNIQQSPWIPGNIAVIVQLLHNISTAIWTGVDEAKMQSYSTIANHILNSKSISNWTFIPDRNSSYILLHSVNSFARRLFIDKHPVDISDVFIHTMGTTISGDNIGKNFTFSMRINDTSNEVTGRVLISRDELRKVPSPSQVISIAFPTIGAILEASLLENVTVNGLVLSAILPKELKRISLIFEKISKSEERRTQCVGWHSVENRWDQQACKMIQENSQQAVCKCRPSKLFTSFSILMSPHILESLILTYITYVGLGISICSLILCLSIEVLVWSQVTKTEITYLRHVCIVNIAATLLMADVWFIVASFLSGPITHHKGCVAATFFVHFFYLSVFFWMLAKALLILYGIMIVFHTLPKSVLVASLFSVGYGCPLAIAAITVAATEPGKGYLRPEICWLNWDMTKALLAFVIPALAIVVVNLITVTLVIVKTQRAAIGNSMFQEVRAIVRISKNIAILTPLLGLTWGFGVATVIDDRSLAFHIIFSLLNAFQVSPDASDQVQSERIHEDVL
Protein: Cytochrome b5 isoform A (AtCb5-A) (Cytochrome b5 isoform D) (AtCb5-D) (Q9FDW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:17322552}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:17322552}; Single-pass membrane protein {ECO:0000255}. Note=Localizes preferentially on the chloroplast envelope. Localizes in stromule (stroma-filled tubular extensions of the plastid envelope membrane). {ECO:0000269|PubMed:17322552}.
Interaction partners:
- NADH--cytochrome b5 reductase 1
- NADH-cytochrome b5 reductase-like protein
- Bax inhibitor 1
- Dihydroceramide fatty acyl 2-hydroxylase FAH1
- Very-long-chain aldehyde decarbonylase CER1
- Probable lysophospholipase BODYGUARD 1
- Dihydroceramide fatty acyl 2-hydroxylase FAH2
- Probable steroid-binding protein 3
- Very-long-chain aldehyde decarbonylase CER3
- Ergosterol biosynthetic protein 28
Sequence:
MPTLTKLYSMEEAATHNKQDDCWVVIDGKVYDVSSYMDEHPGGDDVLLAVAGKDATDDFEDAGHSKDARELMEKYFIGELDESSLPEIPELKIYKKDQPQDSVQKLFDLTKQYWVVPVSIITISVAVSVLFSRKT