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Protein

Glucocorticoid modulatory element-binding protein 1

Gene

GMEB1

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

Functioni

Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter. Essential auxiliary factor for the replication of parvoviruses.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi113 – 1131Zinc
Binding sitei139 – 1391DNA
Binding sitei143 – 1431DNA
Binding sitei146 – 1461DNA
Binding sitei157 – 1571DNA
Metal bindingi170 – 1701Zinc
Metal bindingi174 – 1741Zinc
Metal bindingi178 – 1781Zinc

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Glucocorticoid modulatory element-binding protein 1
Short name:
GMEB-1
Alternative name(s):
DNA-binding protein p96PIF
Parvovirus initiation factor p96
Short name:
PIF p96
Gene namesi
Name:GMEB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4370. GMEB1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28755.

Polymorphism and mutation databases

BioMutaiGMEB1.
DMDMi22001627.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 573572Glucocorticoid modulatory element-binding protein 1PRO_0000074089Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y692.
MaxQBiQ9Y692.
PaxDbiQ9Y692.
PRIDEiQ9Y692.

PTM databases

iPTMnetiQ9Y692.
PhosphoSiteiQ9Y692.

Expressioni

Gene expression databases

BgeeiQ9Y692.
CleanExiHS_GMEB1.
ExpressionAtlasiQ9Y692. baseline and differential.
GenevisibleiQ9Y692. HS.

Organism-specific databases

HPAiHPA044811.
HPA052975.

Interactioni

Subunit structurei

Homodimer, and heterodimer of GMEB1 and GMEB2. GMEB1 and GMEB2 form the parvovirus initiator complex (PIF). Interacts with the glucocorticoid receptor (NR3C1) and NCOA2/TIF2 (By similarity). May interact with HSP27 and CREB-binding protein (CBP).By similarity

Protein-protein interaction databases

BioGridi115930. 15 interactions.
IntActiQ9Y692. 15 interactions.
MINTiMINT-1181706.
STRINGi9606.ENSP00000294409.

Structurei

Secondary structure

1
573
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 998Combined sources
Beta strandi102 – 1076Combined sources
Helixi108 – 1103Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi126 – 1283Combined sources
Helixi130 – 1367Combined sources
Helixi140 – 1423Combined sources
Helixi145 – 1484Combined sources
Beta strandi149 – 1513Combined sources
Helixi156 – 1616Combined sources
Turni168 – 1725Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OQJX-ray1.55A/B89-182[»]
ProteinModelPortaliQ9Y692.
SMRiQ9Y692. Positions 90-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 16685SANDPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili321 – 36747Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 SAND domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00410000025596.
HOGENOMiHOG000231857.
HOVERGENiHBG051742.
InParanoidiQ9Y692.
OMAiAAMQDGG.
OrthoDBiEOG7QZG9C.
PhylomeDBiQ9Y692.
TreeFamiTF317090.

Family and domain databases

Gene3Di3.10.390.10. 1 hit.
InterProiIPR024830. GMEB1/2.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
[Graphical view]
PANTHERiPTHR10417. PTHR10417. 1 hit.
PfamiPF01342. SAND. 1 hit.
[Graphical view]
SMARTiSM00258. SAND. 1 hit.
[Graphical view]
SUPFAMiSSF63763. SSF63763. 1 hit.
PROSITEiPS50864. SAND. 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: Q9Y692-1) [UniParc]FASTAAdd to basket

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
MANAEVSVPV GDVVVVPTEG NEGENPEDTK TQVILQLQPV QQGLFIDGHF
60 70 80 90 100
YNRIYEAGSE NNTAVVAVET HTIHKIEEGI DTGTIEANED MEIAYPITCG
110 120 130 140 150
ESKAILLWKK FVCPGINVKC VKFNDQLISP KHFVHLAGKS TLKDWKRAIR
160 170 180 190 200
LGGIMLRKMM DSGQIDFYQH DKVCSNTCRS TKFDLLISSA RAPVPGQQTS
210 220 230 240 250
VVQTPTSADG SITQIAISEE SMEEAGLEWN SALTAAVTMA TEEGVKKDSE
260 270 280 290 300
EISEDTLMFW KGIADVGLME EVVCNIQKEI EELLRGVQQR LIQAPFQVTD
310 320 330 340 350
AAVLNNVAHT FGLMDTVKKV LDNRRNQVEQ GEEQFLYTLT DLERQLEEQK
360 370 380 390 400
KQGQDHRLKS QTVQNVVLMP VSTPKPPKRP RLQRPASTTV LSPSPPVQQP
410 420 430 440 450
QFTVISPITI TPVGQSFSMG NIPVATLSQG SSPVTVHTLP SGPQLFRYAT
460 470 480 490 500
VVSSAKSSSP DTVTIHPSSS LALLSSTAMQ DGSTLGNMTT MVSPVELVAM
510 520 530 540 550
ESGLTSAIQA VESTSEDGQT IIEIDPAPDP EAEDTEGKAV ILETELRTEE
560 570
KVVAEMEEHQ HQVHNVEIVV LED
Length:573
Mass (Da):62,591
Last modified:July 26, 2002 - v2
Checksum:i8175B0730F1550B8
GO
Isoform 2 (identifier: Q9Y692-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     44-53: Missing.

Show »
Length:563
Mass (Da):61,327
Checksum:iDFDF1EA16BAFB055
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4011Q → E in AAD39355 (PubMed:10386584).Curated
Sequence conflicti463 – 4631V → M in BAA91410 (PubMed:14702039).Curated
Sequence conflicti548 – 5481T → I in BAA91410 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141V → A.
Corresponds to variant rs11557120 [ dbSNP | Ensembl ].
VAR_051894

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei44 – 5310Missing in isoform 2. 4 PublicationsVSP_005970

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099013 mRNA. Translation: AAD39355.1.
AF173868 mRNA. Translation: AAD51352.1.
AF203694 mRNA. Translation: AAG01189.1.
AK000892 mRNA. Translation: BAA91410.1.
AL645729 Genomic DNA. Translation: CAH72427.1.
CH471059 Genomic DNA. Translation: EAX07677.1.
BC001473 mRNA. Translation: AAH01473.1.
CCDSiCCDS327.1. [Q9Y692-1]
CCDS328.1. [Q9Y692-2]
RefSeqiNP_001306603.1. NM_001319674.1. [Q9Y692-2]
NP_006573.2. NM_006582.3. [Q9Y692-1]
NP_077808.1. NM_024482.2. [Q9Y692-2]
XP_011538820.1. XM_011540518.1. [Q9Y692-1]
XP_011538821.1. XM_011540519.1. [Q9Y692-1]
XP_011538823.1. XM_011540521.1. [Q9Y692-2]
UniGeneiHs.632373.

Genome annotation databases

EnsembliENST00000294409; ENSP00000294409; ENSG00000162419. [Q9Y692-1]
ENST00000361872; ENSP00000355186; ENSG00000162419. [Q9Y692-2]
ENST00000373816; ENSP00000362922; ENSG00000162419. [Q9Y692-2]
GeneIDi10691.
KEGGihsa:10691.
UCSCiuc001bqz.4. human. [Q9Y692-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099013 mRNA. Translation: AAD39355.1.
AF173868 mRNA. Translation: AAD51352.1.
AF203694 mRNA. Translation: AAG01189.1.
AK000892 mRNA. Translation: BAA91410.1.
AL645729 Genomic DNA. Translation: CAH72427.1.
CH471059 Genomic DNA. Translation: EAX07677.1.
BC001473 mRNA. Translation: AAH01473.1.
CCDSiCCDS327.1. [Q9Y692-1]
CCDS328.1. [Q9Y692-2]
RefSeqiNP_001306603.1. NM_001319674.1. [Q9Y692-2]
NP_006573.2. NM_006582.3. [Q9Y692-1]
NP_077808.1. NM_024482.2. [Q9Y692-2]
XP_011538820.1. XM_011540518.1. [Q9Y692-1]
XP_011538821.1. XM_011540519.1. [Q9Y692-1]
XP_011538823.1. XM_011540521.1. [Q9Y692-2]
UniGeneiHs.632373.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OQJX-ray1.55A/B89-182[»]
ProteinModelPortaliQ9Y692.
SMRiQ9Y692. Positions 90-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115930. 15 interactions.
IntActiQ9Y692. 15 interactions.
MINTiMINT-1181706.
STRINGi9606.ENSP00000294409.

PTM databases

iPTMnetiQ9Y692.
PhosphoSiteiQ9Y692.

Polymorphism and mutation databases

BioMutaiGMEB1.
DMDMi22001627.

Proteomic databases

EPDiQ9Y692.
MaxQBiQ9Y692.
PaxDbiQ9Y692.
PRIDEiQ9Y692.

Protocols and materials databases

DNASUi10691.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294409; ENSP00000294409; ENSG00000162419. [Q9Y692-1]
ENST00000361872; ENSP00000355186; ENSG00000162419. [Q9Y692-2]
ENST00000373816; ENSP00000362922; ENSG00000162419. [Q9Y692-2]
GeneIDi10691.
KEGGihsa:10691.
UCSCiuc001bqz.4. human. [Q9Y692-1]

Organism-specific databases

CTDi10691.
GeneCardsiGMEB1.
HGNCiHGNC:4370. GMEB1.
HPAiHPA044811.
HPA052975.
MIMi604409. gene.
neXtProtiNX_Q9Y692.
PharmGKBiPA28755.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00410000025596.
HOGENOMiHOG000231857.
HOVERGENiHBG051742.
InParanoidiQ9Y692.
OMAiAAMQDGG.
OrthoDBiEOG7QZG9C.
PhylomeDBiQ9Y692.
TreeFamiTF317090.

Miscellaneous databases

EvolutionaryTraceiQ9Y692.
GeneWikiiGMEB1.
GenomeRNAii10691.
NextBioi40635.
PROiQ9Y692.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y692.
CleanExiHS_GMEB1.
ExpressionAtlasiQ9Y692. baseline and differential.
GenevisibleiQ9Y692. HS.

Family and domain databases

Gene3Di3.10.390.10. 1 hit.
InterProiIPR024830. GMEB1/2.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
[Graphical view]
PANTHERiPTHR10417. PTHR10417. 1 hit.
PfamiPF01342. SAND. 1 hit.
[Graphical view]
SMARTiSM00258. SAND. 1 hit.
[Graphical view]
SUPFAMiSSF63763. SSF63763. 1 hit.
PROSITEiPS50864. SAND. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of hGMEB1, a novel glucocorticoid modulatory element binding protein."
    Theriault J.R., Charette S.J., Lambert H., Landry J.
    FEBS Lett. 452:170-176(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cervix carcinoma.
  2. "Two new members of the emerging KDWK family of combinatorial transcription modulators bind as a heterodimer to flexibly spaced PuCGPy half-sites."
    Christensen J., Cotmore S.F., Tattersall P.
    Mol. Cell. Biol. 19:7741-7750(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 159-172.
    Tissue: Cervix carcinoma.
  3. "Properties of the glucocorticoid modulatory element binding proteins GMEB-1 and -2: potential new modifiers of glucocorticoid receptor transactivation and members of the family of KDWK proteins."
    Kaul S., Blackford J.A. Jr., Chen J., Ogryzko V.V., Simons S.S. Jr.
    Mol. Endocrinol. 14:1010-1027(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Heart.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Embryo.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 2).
    Tissue: Trophoblast.
  8. "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].
  9. "Crystal structure and nuclear magnetic resonance analyses of the SAND domain from glucocorticoid modulatory element binding protein-1 reveals deoxyribonucleic acid and zinc binding regions."
    Surdo P.L., Bottomley M.J., Sattler M., Scheffzek K.
    Mol. Endocrinol. 17:1283-1295(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 87-182, DNA-BINDING, ZINC-BINDING.

Entry informationi

Entry nameiGMEB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y692
Secondary accession number(s): B1AT48, Q9NWH1, Q9UKD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 26, 2002
Last modified: May 11, 2016
This is version 144 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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
  6. SIMILARITY comments
    Index of protein domains and families

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.