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Protein

Glomulin

Gene

GLMN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for normal development of the vasculature. May represent a naturally occurring ligand of the immunophilins FKBP59 and FKBP12. May function as an membrane anchoring protein. Isoform 1 may stimulate the p70S6K pathway. Isoform 2 may inhibit cell proliferation and increase IL2 production.2 Publications

GO - Molecular functioni

  • hepatocyte growth factor receptor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI
  • ubiquitin-protein transferase inhibitor activity Source: MGI

GO - Biological processi

  • muscle cell differentiation Source: UniProtKB
  • negative regulation of protein ubiquitination Source: GOC
  • negative regulation of T cell proliferation Source: UniProtKB
  • neural tube closure Source: Ensembl
  • positive regulation of cytokine secretion Source: UniProtKB
  • positive regulation of interleukin-2 biosynthetic process Source: UniProtKB
  • positive regulation of phosphorylation Source: UniProtKB
  • regulation of gene expression, epigenetic Source: UniProtKB
  • regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • vasculogenesis Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ92990.

Names & Taxonomyi

Protein namesi
Recommended name:
Glomulin
Alternative name(s):
FK506-binding protein-associated protein
Short name:
FAP
FKBP-associated protein
Gene namesi
Name:GLMN
Synonyms:FAP48, FAP68, VMGLOM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14373. GLMN.

Subcellular locationi

GO - Cellular componenti

  • Cul2-RING ubiquitin ligase complex Source: MGI
  • Cul3-RING ubiquitin ligase complex Source: MGI
  • Cul4A-RING E3 ubiquitin ligase complex Source: MGI
  • cullin-RING ubiquitin ligase complex Source: MGI
  • intracellular Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Glomuvenous malformations (GVMs)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by the presence of smooth-muscle-like glomus cells in the media surrounding distended vascular lumens.
See also OMIM:138000
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti393 – 3931Missing in GVMs. 1 Publication
VAR_017241

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi219 – 2191P → A: Loss of interaction with FKBP12 and FKBP59. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiGLMN.
MIMi138000. phenotype.
Orphaneti83454. Glomuvenous malformation.
PharmGKBiPA134870088.

Polymorphism and mutation databases

BioMutaiGLMN.
DMDMi38372884.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 594593GlomulinPRO_0000087513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Post-translational modificationi

Phosphorylated on tyrosine residues.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ92990.
MaxQBiQ92990.
PaxDbiQ92990.
PRIDEiQ92990.
TopDownProteomicsiQ92990-1. [Q92990-1]

PTM databases

iPTMnetiQ92990.
PhosphoSiteiQ92990.
SwissPalmiQ92990.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ92990.
CleanExiHS_GLMN.
ExpressionAtlasiQ92990. baseline and differential.
GenevisibleiQ92990. HS.

Organism-specific databases

HPAiHPA031446.
HPA031447.
HPA031448.

Interactioni

Subunit structurei

Monomer. Isoform 1 interacts with notphosphorylated MET and is released upon receptor phosphorylation. Isoform 2 interacts with FKBP59 and FKBP12. Isoform 1 is part of a SCF-like complex consisting of CUL7, RBX1, SKP1, FBXW8 and GLMN isoform 1.2 Publications

GO - Molecular functioni

  • hepatocyte growth factor receptor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

Protein-protein interaction databases

BioGridi116318. 73 interactions.
IntActiQ92990. 11 interactions.
MINTiMINT-1407127.
STRINGi9606.ENSP00000359385.

Structurei

Secondary structure

1
594
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Helixi28 – 3710Combined sources
Beta strandi38 – 403Combined sources
Helixi43 – 497Combined sources
Helixi55 – 606Combined sources
Helixi62 – 654Combined sources
Helixi66 – 749Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 9613Combined sources
Helixi99 – 1013Combined sources
Helixi102 – 1065Combined sources
Helixi107 – 1104Combined sources
Helixi115 – 1173Combined sources
Helixi118 – 13518Combined sources
Helixi140 – 15617Combined sources
Helixi173 – 19220Combined sources
Helixi199 – 22224Combined sources
Helixi236 – 25015Combined sources
Beta strandi251 – 2533Combined sources
Helixi255 – 2573Combined sources
Helixi283 – 29412Combined sources
Turni298 – 3025Combined sources
Helixi309 – 32416Combined sources
Helixi329 – 34416Combined sources
Helixi353 – 3575Combined sources
Helixi359 – 37416Combined sources
Helixi378 – 39417Combined sources
Helixi397 – 41115Combined sources
Helixi414 – 43017Combined sources
Turni440 – 4423Combined sources
Helixi444 – 45310Combined sources
Turni457 – 4615Combined sources
Turni464 – 4663Combined sources
Helixi468 – 48417Combined sources
Turni487 – 4893Combined sources
Helixi494 – 4963Combined sources
Helixi498 – 5047Combined sources
Helixi506 – 53328Combined sources
Helixi553 – 5553Combined sources
Helixi556 – 58126Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F52X-ray3.00E/F1-594[»]
ProteinModelPortaliQ92990.
SMRiQ92990. Positions 1-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili188 – 20821Sequence analysisAdd
BLAST
Coiled coili272 – 28918Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi123 – 1264Poly-Leu
Compositional biasi273 – 2786Poly-Glu

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4H. Eukaryota.
ENOG410YJ4Z. LUCA.
GeneTreeiENSGT00390000018446.
HOGENOMiHOG000043079.
HOVERGENiHBG044811.
InParanoidiQ92990.
OMAiKNQIDMS.
OrthoDBiEOG7B05DQ.
PhylomeDBiQ92990.
TreeFamiTF105319.

Family and domain databases

InterProiIPR019516. Glomulin/ALF4.
IPR013877. YAP-bd/ALF4/Glomulin.
[Graphical view]
PANTHERiPTHR15430. PTHR15430. 1 hit.
PfamiPF08568. Kinetochor_Ybp2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92990-1) [UniParc]FASTAAdd to basket

Also known as: FAP68, FKBP-associated protein 68 kDa

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVEELQSII KRCQILEEQD FKEEDFGLFQ LAGQRCIEEG HTDQLLEIIQ
60 70 80 90 100
NEKNKVIIKN MGWNLVGPVV RCLLCKDKED SKRKVYFLIF DLLVKLCNPK
110 120 130 140 150
ELLLGLLELI EEPSGKQISQ SILLLLQPLQ TVIQKLHNKA YSIGLALSTL
160 170 180 190 200
WNQLSLLPVP YSKEQIQMDD YGLCQCCKAL IEFTKPFVEE VIDNKENSLE
210 220 230 240 250
NEKLKDELLK FCFKSLKCPL LTAQFFEQSE EGGNDPFRYF ASEIIGFLSA
260 270 280 290 300
IGHPFPKMIF NHGRKKRTWN YLEFEEEENK QLADSMASLA YLVFVQGIHI
310 320 330 340 350
DQLPMVLSPL YLLQFNMGHI EVFLQRTEES VISKGLELLE NSLLRIEDNS
360 370 380 390 400
LLYQYLEIKS FLTVPQGLVK VMTLCPIETL RKKSLAMLQL YINKLDSQGK
410 420 430 440 450
YTLFRCLLNT SNHSGVEAFI IQNIKNQIDM SLKRTRNNKW FTGPQLISLL
460 470 480 490 500
DLVLFLPEGA ETDLLQNSDR IMASLNLLRY LVIKDNENDN QTGLWTELGN
510 520 530 540 550
IENNFLKPLH IGLNMSKAHY EAEIKNSQEA QKSKDLCSIT VSGEEIPNMP
560 570 580 590
PEMQLKVLHS ALFTFDLIES VLARVEELIE IKTKSTSEEN IGIK
Length:594
Mass (Da):68,208
Last modified:November 14, 2003 - v2
Checksum:iCE19050F1F692378
GO
Isoform 2 (identifier: Q92990-2) [UniParc]FASTAAdd to basket

Also known as: FAP48, FKBP-associated protein 48 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     406-417: CLLNTSNHSGVE → EHVTTNGLQDHS
     418-594: Missing.

Show »
Length:417
Mass (Da):48,166
Checksum:iEFA18B54B381E2AD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361L → S.
Corresponds to variant rs35258161 [ dbSNP | Ensembl ].
VAR_061653
Natural varianti393 – 3931Missing in GVMs. 1 Publication
VAR_017241

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei406 – 41712CLLNT…HSGVE → EHVTTNGLQDHS in isoform 2. 1 PublicationVSP_008882Add
BLAST
Alternative sequencei418 – 594177Missing in isoform 2. 1 PublicationVSP_008883Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73704 mRNA. Translation: AAC50908.1.
AJ347709 mRNA. Translation: CAC69882.1.
AJ302735 mRNA. Translation: CAC82938.1.
AJ302727
, AJ302728, AJ302729, AJ302730, AJ302731, AJ302732, AJ302733, AJ302734 Genomic DNA. Translation: CAC88124.1.
AL451010 Genomic DNA. Translation: CAH70761.1.
CH471097 Genomic DNA. Translation: EAW73098.1.
BC001257 mRNA. Translation: AAH01257.1.
CCDSiCCDS738.1. [Q92990-1]
RefSeqiNP_001306612.1. NM_001319683.1.
NP_444504.1. NM_053274.2. [Q92990-1]
XP_011538846.1. XM_011540544.1. [Q92990-1]
XP_011538847.1. XM_011540545.1. [Q92990-1]
XP_011538848.1. XM_011540546.1. [Q92990-1]
UniGeneiHs.49105.

Genome annotation databases

EnsembliENST00000370360; ENSP00000359385; ENSG00000174842. [Q92990-1]
ENST00000495106; ENSP00000436829; ENSG00000174842. [Q92990-2]
GeneIDi11146.
KEGGihsa:11146.
UCSCiuc001dor.4. human. [Q92990-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73704 mRNA. Translation: AAC50908.1.
AJ347709 mRNA. Translation: CAC69882.1.
AJ302735 mRNA. Translation: CAC82938.1.
AJ302727
, AJ302728, AJ302729, AJ302730, AJ302731, AJ302732, AJ302733, AJ302734 Genomic DNA. Translation: CAC88124.1.
AL451010 Genomic DNA. Translation: CAH70761.1.
CH471097 Genomic DNA. Translation: EAW73098.1.
BC001257 mRNA. Translation: AAH01257.1.
CCDSiCCDS738.1. [Q92990-1]
RefSeqiNP_001306612.1. NM_001319683.1.
NP_444504.1. NM_053274.2. [Q92990-1]
XP_011538846.1. XM_011540544.1. [Q92990-1]
XP_011538847.1. XM_011540545.1. [Q92990-1]
XP_011538848.1. XM_011540546.1. [Q92990-1]
UniGeneiHs.49105.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F52X-ray3.00E/F1-594[»]
ProteinModelPortaliQ92990.
SMRiQ92990. Positions 1-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116318. 73 interactions.
IntActiQ92990. 11 interactions.
MINTiMINT-1407127.
STRINGi9606.ENSP00000359385.

PTM databases

iPTMnetiQ92990.
PhosphoSiteiQ92990.
SwissPalmiQ92990.

Polymorphism and mutation databases

BioMutaiGLMN.
DMDMi38372884.

Proteomic databases

EPDiQ92990.
MaxQBiQ92990.
PaxDbiQ92990.
PRIDEiQ92990.
TopDownProteomicsiQ92990-1. [Q92990-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370360; ENSP00000359385; ENSG00000174842. [Q92990-1]
ENST00000495106; ENSP00000436829; ENSG00000174842. [Q92990-2]
GeneIDi11146.
KEGGihsa:11146.
UCSCiuc001dor.4. human. [Q92990-1]

Organism-specific databases

CTDi11146.
GeneCardsiGLMN.
HGNCiHGNC:14373. GLMN.
HPAiHPA031446.
HPA031447.
HPA031448.
MalaCardsiGLMN.
MIMi138000. phenotype.
601749. gene.
neXtProtiNX_Q92990.
Orphaneti83454. Glomuvenous malformation.
PharmGKBiPA134870088.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG4H. Eukaryota.
ENOG410YJ4Z. LUCA.
GeneTreeiENSGT00390000018446.
HOGENOMiHOG000043079.
HOVERGENiHBG044811.
InParanoidiQ92990.
OMAiKNQIDMS.
OrthoDBiEOG7B05DQ.
PhylomeDBiQ92990.
TreeFamiTF105319.

Enzyme and pathway databases

SignaLinkiQ92990.

Miscellaneous databases

ChiTaRSiGLMN. human.
GeneWikiiGLMN.
GenomeRNAii11146.
NextBioi42372.
PROiQ92990.
SOURCEiSearch...

Gene expression databases

BgeeiQ92990.
CleanExiHS_GLMN.
ExpressionAtlasiQ92990. baseline and differential.
GenevisibleiQ92990. HS.

Family and domain databases

InterProiIPR019516. Glomulin/ALF4.
IPR013877. YAP-bd/ALF4/Glomulin.
[Graphical view]
PANTHERiPTHR15430. PTHR15430. 1 hit.
PfamiPF08568. Kinetochor_Ybp2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin."
    Chambraud B., Radanyi C., Camonis J.H., Shazand K., Rajkowski K., Baulieu E.-E.
    J. Biol. Chem. 271:32923-32929(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Leukemia.
  2. "Ligand-regulated binding of FAP68 to the hepatocyte growth factor receptor."
    Grisendi S., Chambraud B., Gout I., Comoglio P.M., Crepaldi T.
    J. Biol. Chem. 276:46632-46638(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, INTERACTION WITH MET.
  3. "Mutations in a novel factor, glomulin, are responsible for glomuvenous malformations ('glomangiomas')."
    Brouillard P., Boon L.M., Mulliken J.B., Enjolras O., Ghassibe M., Warman M.L., Tan O.T., Olsen B.R., Vikkula M.
    Am. J. Hum. Genet. 70:866-874(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT GVMS ASN-393 DEL.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  7. "The FKBP-associated protein FAP48 is an antiproliferative molecule and a player in T cell activation that increases IL2 synthesis."
    Krummrei U., Baulieu E.-E., Chambraud B.
    Proc. Natl. Acad. Sci. U.S.A. 100:2444-2449(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52."
    Neye H.
    Regul. Pept. 97:147-152(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-219.
  9. "Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis."
    Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CUL7; SKP1; FBXW8 AND RBX1.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLMN_HUMAN
AccessioniPrimary (citable) accession number: Q92990
Secondary accession number(s): Q5VVC3, Q9BVE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 14, 2003
Last modified: May 11, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Rapamycin and FK506 abolish the interaction in a dose dependent manner.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.