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Protein

Myeloid leukemia factor 1

Gene

MLF1

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

Functioni

Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses RFWD2/COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Differentiation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SIGNORiP58340.

Names & Taxonomyi

Protein namesi
Recommended name:
Myeloid leukemia factor 1
Alternative name(s):
Myelodysplasia-myeloid leukemia factor 1
Gene namesi
Name:MLF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:7125. MLF1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Shuttles between the cytoplasm and nucleus.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving MLF1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with NPM1/NPM.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei16 – 172Breakpoint for translocation to form NPM-MLF1

Organism-specific databases

MalaCardsiMLF1.
PharmGKBiPA30843.

Polymorphism and mutation databases

BioMutaiMLF1.
DMDMi17368170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 268268Myeloid leukemia factor 1PRO_0000220752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei32 – 321PhosphoserineCombined sources
Modified residuei34 – 341Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation is required for binding to YWHAZ.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP58340.
MaxQBiP58340.
PeptideAtlasiP58340.
PRIDEiP58340.

PTM databases

iPTMnetiP58340.
PhosphoSiteiP58340.

Expressioni

Tissue specificityi

Most abundant in testis, ovary, skeletal muscle, heart, kidney and colon. Low expression in spleen, thymus and peripheral blood leukocytes.

Gene expression databases

BgeeiP58340.
CleanExiHS_MLF1.
ExpressionAtlasiP58340. baseline and differential.
GenevisibleiP58340. HS.

Organism-specific databases

HPAiHPA017903.

Interactioni

Subunit structurei

Interacts with CENPU. Also interacts with NRBP1/MADM, YWHAZ/14-3-3-zeta and HNRPUL2/MANP. NRBP1 recruits a serine kinase which phosphorylates both itself and MLF1. Phosphorylated MLF1 then binds to YWHAZ and is retained in the cytoplasm. Retained in the nucleus by binding to HNRPUL2. Binds to COPS3/CSN3 which is required for suppression of RFWD2 and activation of p53.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A8K1F42EBI-721328,EBI-9357094
DNAJB6O751902EBI-721328,EBI-1053164
PSMD2Q132002EBI-721328,EBI-357648
YWHAEP622583EBI-721328,EBI-356498

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110437. 51 interactions.
IntActiP58340. 85 interactions.
MINTiMINT-1427321.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UALX-ray1.80P29-42[»]
3UBWX-ray1.90P29-42[»]
ProteinModelPortaliP58340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 12576Interaction with COPS3Add
BLAST

Sequence similaritiesi

Belongs to the MLF family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000005023.
HOGENOMiHOG000045671.
HOVERGENiHBG019060.
InParanoidiP58340.
KOiK15622.
OMAiPFQAVDR.
PhylomeDBiP58340.
TreeFamiTF317561.

Family and domain databases

InterProiIPR019376. Myeloid_leukemia_factor.
[Graphical view]
PfamiPF10248. Mlf1IP. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P58340-1) [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
MFRMLNSSFE DDPFFSESIL AHRENMRQMI RSFSEPFGRD LLSISDGRGR
60 70 80 90 100
AHNRRGHNDG EDSLTHTDVS SFQTMDQMVS NMRNYMQKLE RNFGQLSVDP
110 120 130 140 150
NGHSFCSSSV MTYSKIGDEP PKVFQASTQT RRAPGGIKET RKAMRDSDSG
160 170 180 190 200
LEKMAIGHHI HDRAHVIKKS KNKKTGDEEV NQEFINMNES DAHAFDEEWQ
210 220 230 240 250
SEVLKYKPGR HNLGNTRMRS VGHENPGSRE LKRREKPQQS PAIEHGRRSN
260
VLGDKLHIKG SSVKSNKK
Length:268
Mass (Da):30,627
Last modified:November 2, 2001 - v1
Checksum:i08774217329F737A
GO
Isoform 2 (identifier: P58340-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.
     94-136: Missing.

Show »
Length:200
Mass (Da):23,117
Checksum:iCFF347E5F40C1BFF
GO
Isoform 3 (identifier: P58340-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MFRMLNSSFEDDPFF → MLKEVLQREGKSYKSETLMYIKKARASENKL
     65-65: T → TATSCSLVPFGDFGGM

Note: No experimental confirmation available.
Show »
Length:299
Mass (Da):33,888
Checksum:i75E81192D63D7948
GO
Isoform 5 (identifier: P58340-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.

Show »
Length:243
Mass (Da):27,625
Checksum:i061E87A385C3E063
GO
Isoform 4 (identifier: P58340-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.
     65-65: T → TATSCSLVPFGDFGGM

Note: No experimental confirmation available.
Show »
Length:258
Mass (Da):29,095
Checksum:i68BC1583FCAA0F23
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti226 – 2261P → T.
Corresponds to variant rs15967 [ dbSNP | Ensembl ].
VAR_022070

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525Missing in isoform 2, isoform 4 and isoform 5. 2 PublicationsVSP_043130Add
BLAST
Alternative sequencei1 – 1515MFRML…DDPFF → MLKEVLQREGKSYKSETLMY IKKARASENKL in isoform 3. 1 PublicationVSP_043725Add
BLAST
Alternative sequencei65 – 651T → TATSCSLVPFGDFGGM in isoform 3 and isoform 4. 1 PublicationVSP_043726
Alternative sequencei94 – 13643Missing in isoform 2. 1 PublicationVSP_043131Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49054 mRNA. Translation: AAA99997.1.
AY848700 mRNA. Translation: AAX46015.1.
AY848702 mRNA. Translation: AAX46017.1.
AK056948 mRNA. Translation: BAB71320.1.
AK096889 mRNA. Translation: BAC04885.1.
AK297488 mRNA. Translation: BAG59906.1.
AC025033 Genomic DNA. No translation available.
AC106707 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78689.1.
CH471052 Genomic DNA. Translation: EAW78690.1.
BC007045 mRNA. Translation: AAH07045.1.
CCDSiCCDS3182.1. [P58340-1]
CCDS46945.1. [P58340-5]
CCDS56286.1. [P58340-3]
CCDS56287.1. [P58340-4]
CCDS56288.1. [P58340-2]
RefSeqiNP_001123628.1. NM_001130156.2. [P58340-5]
NP_001123629.1. NM_001130157.2. [P58340-5]
NP_001182361.1. NM_001195432.1. [P58340-3]
NP_001182362.1. NM_001195433.1. [P58340-2]
NP_001182363.1. NM_001195434.1. [P58340-4]
NP_071888.1. NM_022443.4. [P58340-1]
XP_005247537.1. XM_005247480.2. [P58340-4]
XP_011511154.1. XM_011512852.1. [P58340-4]
XP_011511155.1. XM_011512853.1. [P58340-5]
UniGeneiHs.85195.

Genome annotation databases

EnsembliENST00000355893; ENSP00000348157; ENSG00000178053. [P58340-1]
ENST00000359117; ENSP00000352025; ENSG00000178053. [P58340-5]
ENST00000392822; ENSP00000376568; ENSG00000178053. [P58340-3]
ENST00000469452; ENSP00000418595; ENSG00000178053. [P58340-2]
ENST00000471745; ENSP00000420134; ENSG00000178053. [P58340-4]
ENST00000478894; ENSP00000417777; ENSG00000178053. [P58340-4]
ENST00000482628; ENSP00000417141; ENSG00000178053. [P58340-5]
ENST00000484955; ENSP00000417835; ENSG00000178053. [P58340-5]
ENST00000618075; ENSP00000484169; ENSG00000178053. [P58340-2]
ENST00000619577; ENSP00000483337; ENSG00000178053. [P58340-4]
GeneIDi4291.
KEGGihsa:4291.
UCSCiuc003fbx.4. human. [P58340-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, 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
L49054 mRNA. Translation: AAA99997.1.
AY848700 mRNA. Translation: AAX46015.1.
AY848702 mRNA. Translation: AAX46017.1.
AK056948 mRNA. Translation: BAB71320.1.
AK096889 mRNA. Translation: BAC04885.1.
AK297488 mRNA. Translation: BAG59906.1.
AC025033 Genomic DNA. No translation available.
AC106707 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78689.1.
CH471052 Genomic DNA. Translation: EAW78690.1.
BC007045 mRNA. Translation: AAH07045.1.
CCDSiCCDS3182.1. [P58340-1]
CCDS46945.1. [P58340-5]
CCDS56286.1. [P58340-3]
CCDS56287.1. [P58340-4]
CCDS56288.1. [P58340-2]
RefSeqiNP_001123628.1. NM_001130156.2. [P58340-5]
NP_001123629.1. NM_001130157.2. [P58340-5]
NP_001182361.1. NM_001195432.1. [P58340-3]
NP_001182362.1. NM_001195433.1. [P58340-2]
NP_001182363.1. NM_001195434.1. [P58340-4]
NP_071888.1. NM_022443.4. [P58340-1]
XP_005247537.1. XM_005247480.2. [P58340-4]
XP_011511154.1. XM_011512852.1. [P58340-4]
XP_011511155.1. XM_011512853.1. [P58340-5]
UniGeneiHs.85195.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UALX-ray1.80P29-42[»]
3UBWX-ray1.90P29-42[»]
ProteinModelPortaliP58340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110437. 51 interactions.
IntActiP58340. 85 interactions.
MINTiMINT-1427321.

PTM databases

iPTMnetiP58340.
PhosphoSiteiP58340.

Polymorphism and mutation databases

BioMutaiMLF1.
DMDMi17368170.

Proteomic databases

EPDiP58340.
MaxQBiP58340.
PeptideAtlasiP58340.
PRIDEiP58340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355893; ENSP00000348157; ENSG00000178053. [P58340-1]
ENST00000359117; ENSP00000352025; ENSG00000178053. [P58340-5]
ENST00000392822; ENSP00000376568; ENSG00000178053. [P58340-3]
ENST00000469452; ENSP00000418595; ENSG00000178053. [P58340-2]
ENST00000471745; ENSP00000420134; ENSG00000178053. [P58340-4]
ENST00000478894; ENSP00000417777; ENSG00000178053. [P58340-4]
ENST00000482628; ENSP00000417141; ENSG00000178053. [P58340-5]
ENST00000484955; ENSP00000417835; ENSG00000178053. [P58340-5]
ENST00000618075; ENSP00000484169; ENSG00000178053. [P58340-2]
ENST00000619577; ENSP00000483337; ENSG00000178053. [P58340-4]
GeneIDi4291.
KEGGihsa:4291.
UCSCiuc003fbx.4. human. [P58340-1]

Organism-specific databases

CTDi4291.
GeneCardsiMLF1.
HGNCiHGNC:7125. MLF1.
HPAiHPA017903.
MalaCardsiMLF1.
MIMi601402. gene.
neXtProtiNX_P58340.
PharmGKBiPA30843.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000005023.
HOGENOMiHOG000045671.
HOVERGENiHBG019060.
InParanoidiP58340.
KOiK15622.
OMAiPFQAVDR.
PhylomeDBiP58340.
TreeFamiTF317561.

Enzyme and pathway databases

SIGNORiP58340.

Miscellaneous databases

ChiTaRSiMLF1. human.
GeneWikiiMLF1.
GenomeRNAii4291.
PROiP58340.
SOURCEiSearch...

Gene expression databases

BgeeiP58340.
CleanExiHS_MLF1.
ExpressionAtlasiP58340. baseline and differential.
GenevisibleiP58340. HS.

Family and domain databases

InterProiIPR019376. Myeloid_leukemia_factor.
[Graphical view]
PfamiPF10248. Mlf1IP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid leukemia produces a novel fusion gene, NPM-MLF1."
    Yoneda-Kato N., Look A.T., Kirstein M.N., Valentine M.B., Raimondi S.C., Cohen K.J., Carroll A.J., Morris S.W.
    Oncogene 12:265-275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION.
    Tissue: Skeletal muscle and Testis.
  2. Feng X., Ling S., Zhang H., Song X., Wang G., Chen K., Zhu C.
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5).
  3. "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] (ISOFORMS 3; 4 AND 5).
    Tissue: Brain and Skeletal muscle.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(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] (ISOFORM 1).
    Tissue: Urinary bladder.
  7. "cDNA cloning and characterization of a novel gene encoding the MLF1-interacting protein MLF1IP."
    Hanissian S.H., Akbar U., Teng B., Janjetovic Z., Hoffmann A., Hitzler J.K., Iscove N., Hamre K., Du X., Tong Y., Mukatira S., Robertson J.H., Morris S.W.
    Oncogene 23:3700-3707(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CENPU.
  8. "Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via COP9 signalosome subunit 3."
    Yoneda-Kato N., Tomoda K., Umehara M., Arata Y., Kato J.-Y.
    EMBO J. 24:1739-1749(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COPS3.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  10. "Structural insights of the MLF1/14-3-3 interaction."
    Molzan M., Weyand M., Rose R., Ottmann C.
    FEBS J. 279:563-571(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-42 IN COMPLEX WITH YWHAE, PHOSPHORYLATION AT SER-34.

Entry informationi

Entry nameiMLF1_HUMAN
AccessioniPrimary (citable) accession number: P58340
Secondary accession number(s): E9PEU9
, Q2TLE3, Q2TLE5, Q8N8F8, Q96MH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: July 6, 2016
This is version 121 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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.