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Q9Y6D9 (MD1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitotic spindle assembly checkpoint protein MAD1
Alternative name(s):
Mitotic arrest deficient 1-like protein 1
Short name=MAD1-like protein 1
Mitotic checkpoint MAD1 protein homolog
Short name=HsMAD1
Short name=hMAD1
Tax-binding protein 181
Gene names
Name:MAD1L1
Synonyms:MAD1, TXBP181
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding. Ref.3 Ref.6 Ref.16

Subunit structure

Homodimer. Heterodimerizes with MAD2L1 in order to form a tetrameric MAD1L1-MAD2L1 core complex. Perturbation of the original MAD1L1-MAD2L1 structure by the spindle checkpoint may decrease MAD2L1 affinity for MAD1L1. CDC20 can compete with MAD1L1 for MAD2L1 binding, until the attachment and/or tension dampen the checkpoint signal, preventing further release of MAD2L1 on to CDC20. Also able to interact with the BUB1/BUB3 complex and the viral Tax protein. Interacts with NEK2. Interacts with TPR; the interactions occurs in a microtubule-independent manner. Ref.1 Ref.2 Ref.7 Ref.10 Ref.14 Ref.16 Ref.21

Subcellular location

Nucleus. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Note: From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Colocalizes with NEK2 at the kinetochore. Ref.1 Ref.7 Ref.10 Ref.16

Tissue specificity

Expressed weakly at G0/G1 and highly at late S and G2/M phase.

Induction

Increased by p53/TP53. Ref.3

Post-translational modification

Phosphorylated; by BUB1. Become hyperphosphorylated in late S through M phases or after mitotic spindle damage. Ref.1 Ref.2

Involvement in disease

Defects in MAD1L1 are involved in the development and/or progression of various types of cancer.

Sequence similarities

Belongs to the MAD1 family.

Sequence caution

The sequence AAC52059.1 differs from that shown. Reason: Frameshift at position 663.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitotic anaphase

Non-traceable author statement Ref.1. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle checkpoint

Non-traceable author statement Ref.1. Source: UniProtKB

mitotic metaphase

Non-traceable author statement Ref.1. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle assembly checkpoint

Traceable author statement. Source: Reactome

mitotic telophase

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of metaphase plate congression

Inferred from direct assay Ref.16. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

centrosome

Non-traceable author statement Ref.1. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.16. Source: UniProtKB

mitotic spindle

Inferred from direct assay Ref.16. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

spindle

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.21Ref.7Ref.10Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAD2L1Q1325710EBI-742610,EBI-78203
MAXP612442EBI-742610,EBI-751711

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718Mitotic spindle assembly checkpoint protein MAD1
PRO_0000213800

Regions

Region380 – 532153Necessary for interaction with NEK2
Coiled coil46 – 632587 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19 Ref.20
Modified residue161Phosphoserine Ref.12
Modified residue611N6-acetyllysine Ref.15
Modified residue2141Phosphoserine Ref.9
Modified residue4281Phosphoserine Ref.8 Ref.12 Ref.17

Natural variations

Natural variant291S → L in a lymphoid cancer cell line; somatic mutation. Ref.24
VAR_019707
Natural variant591R → C in a prostate cancer cell line; somatic mutation. Ref.24
Corresponds to variant rs28939694 [ dbSNP | Ensembl ].
VAR_019708
Natural variant1601N → S. Ref.23
VAR_019709
Natural variant2991T → A in lung cancer cell line; somatic mutation. Ref.23
VAR_019710
Natural variant3601R → Q in a prostate cancer cell line; somatic mutation. Ref.24
VAR_019711
Natural variant5001T → M. Ref.23 Ref.24
Corresponds to variant rs193231481 [ dbSNP | Ensembl ].
VAR_019712
Natural variant5111E → K. Ref.23
VAR_019713
Natural variant5161E → K in a breast cancer cell line; somatic mutation. Ref.24
VAR_019714
Natural variant5561R → C in a prostate cancer cell line; somatic mutation. Ref.24
VAR_019715
Natural variant5561R → H in one individual with lung cancer. Ref.23
VAR_019716
Natural variant5581R → H in a cancer cell line. Ref.22 Ref.23 Ref.24
Corresponds to variant rs1801368 [ dbSNP | Ensembl ].
VAR_019717
Natural variant5691E → K in a breast cancer cell line; somatic mutation. Ref.24
VAR_019718
Natural variant5721R → H in a cancer cell line. Ref.22
Corresponds to variant rs1801500 [ dbSNP | Ensembl ].
VAR_019719

Experimental info

Sequence conflict189 – 1902EL → DV in AAC52059. Ref.1
Sequence conflict189 – 1902EL → DV in AAD24498. Ref.3
Sequence conflict2601K → E in AAC52059. Ref.1
Sequence conflict2601K → E in AAD24498. Ref.3
Sequence conflict2681Missing in AAC52059. Ref.1

Secondary structure

....................... 718
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y6D9 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: DA65529856A37EE3

FASTA71883,067
        10         20         30         40         50         60 
MEDLGENTMV LSTLRSLNNF ISQRVEGGSG LDISTSAPGS LQMQYQQSMQ LEERAEQIRS 

        70         80         90        100        110        120 
KSHLIQVERE KMQMELSHKR ARVELERAAS TSARNYEREV DRNQELLTRI RQLQEREAGA 

       130        140        150        160        170        180 
EEKMQEQLER NRQCQQNLDA ASKRLREKED SLAQAGETIN ALKGRISELQ WSVMDQEMRV 

       190        200        210        220        230        240 
KRLESEKQEL QEQLDLQHKK CQEANQKIQE LQASQEARAD HEQQIKDLEQ KLSLQEQDAA 

       250        260        270        280        290        300 
IVKNMKSELV RLPRLERELK QLREESAHLR EMRETNGLLQ EELEGLQRKL GRQEKMQETL 

       310        320        330        340        350        360 
VGLELENERL LAKLQSWERL DQTMGLSIRT PEDLSRFVVE LQQRELALKD KNSAVTSSAR 

       370        380        390        400        410        420 
GLEKARQQLQ EELRQVSGQL LEERKKRETH EALARRLQKR VLLLTKERDG MRAILGSYDS 

       430        440        450        460        470        480 
ELTPAEYSPQ LTRRMREAED MVQKVHSHSA EMEAQLSQAL EELGGQKQRA DMLEMELKML 

       490        500        510        520        530        540 
KSQSSSAEQS FLFSREEADT LRLKVEELEG ERSRLEEEKR MLEAQLERRA LQGDYDQSRT 

       550        560        570        580        590        600 
KVLHMSLNPT SVARQRLRED HSQLQAECER LRGLLRAMER GGTVPADLEA AAASLPSSKE 

       610        620        630        640        650        660 
VAELKKQVES AELKNQRLKE VFQTKIQEFR KACYTLTGYQ IDITTENQYR LTSLYAEHPG 

       670        680        690        700        710 
DCLIFKATSP SGSKMQLLET EFSHTVGELI EVHLRRQDSI PAFLSSLTLE LFSRQTVA 

« Hide

References

« Hide 'large scale' references
[1]"Human T cell leukemia virus type 1 oncoprotein Tax targets the human mitotic checkpoint protein MAD1."
Jin D.-Y., Spencer F., Jeang K.-T.
Cell 93:81-91(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, HETEROTETRAMERIZATION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH MAD2L1 AND VIRAL TAX.
[2]"Phosphorylation of human MAD1 by the BUB1 kinase in vitro."
Seeley T.W., Wang L., Zhen J.Y.
Biochem. Biophys. Res. Commun. 257:589-595(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY BUB1, INTERACTION WITH BUB1/BUB3 COMPLEX.
Tissue: Testis.
[3]"Mitotic checkpoint locus MAD1L1 maps to human chromosome 7p22 and mouse chromosome 5."
Jin D.-Y., Kozak C.A., Pangilinan F., Spencer F., Green E.D., Jeang K.-T.
Genomics 55:363-364(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Pancreas.
[6]"Multiple tumor suppressor pathways negatively regulate telomerase."
Lin S.Y., Elledge S.J.
Cell 113:881-889(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"NEK2A interacts with MAD1 and possibly functions as a novel integrator of the spindle checkpoint signaling."
Lou Y., Yao J., Zereshki A., Dou Z., Ahmed K., Wang H., Hu J., Wang Y., Yao X.
J. Biol. Chem. 279:20049-20057(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK2.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint."
Lee S.H., Sterling H., Burlingame A., McCormick F.
Genes Dev. 22:2926-2931(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TPR AND MAD2L1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator."
Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E., Tavares A., Johansen J., Johansen K.M., Maiato H.
J. Cell Biol. 184:647-657(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TPR.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis."
Nakano H., Funasaka T., Hashizume C., Wong R.W.
J. Biol. Chem. 285:10841-10849(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TPR, SUBCELLULAR LOCATION.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint."
Sironi L., Mapelli M., Knapp S., De Antoni A., Jeang K.-T., Musacchio A.
EMBO J. 21:2496-2506(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 493-579 IN COMPLEX WITH MAD2L1, COMPETITIVE INHIBITOR OF MAD2L1-CDC20 INTERACTION.
[22]"Characterization of MAD2B and other mitotic spindle checkpoint genes."
Cahill D.P., da Costa L.T., Carson-Walter E.B., Kinzler K.W., Vogelstein B., Lengauer C.
Genomics 58:181-187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-558 AND HIS-572.
[23]"Search for in vivo somatic mutations in the mitotic checkpoint gene, hMAD1, in human lung cancers."
Nomoto S., Haruki N., Takahashi T., Masuda A., Koshikawa T., Takahashi T., Fujii Y., Osada H., Takahashi T.
Oncogene 18:7180-7183(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LUNG CANCER ALA-299, VARIANTS SER-160; MET-500; LYS-511; HIS-556 AND HIS-558.
[24]"Mutations in the mitotic check point gene, MAD1L1, in human cancers."
Tsukasaki K., Miller C.W., Greenspun E., Eshaghian S., Kawabata H., Fujimoto T., Tomonaga M., Sawyers C., Said J.W., Koeffler H.P.
Oncogene 20:3301-3305(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CANCER LEU-29; CYS-59; GLN-360; LYS-516; CYS-556 AND LYS-569, VARIANTS MET-500 AND HIS-558.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33822 mRNA. Translation: AAC52059.1. Frameshift.
AF123318 mRNA. Translation: AAD20359.1.
AF083811 mRNA. Translation: AAD24498.1.
AC005282 Genomic DNA. No translation available.
AC006433 Genomic DNA. No translation available.
AC069288 Genomic DNA. Translation: AAS07503.1.
AC104129 Genomic DNA. Translation: AAP21876.1.
AC110781 Genomic DNA. No translation available.
BC009964 mRNA. Translation: AAH09964.1.
CCDSCCDS43539.1.
RefSeqNP_001013858.1. NM_001013836.1.
NP_001013859.1. NM_001013837.1.
NP_003541.2. NM_003550.2.
XP_005249933.1. XM_005249876.1.
XP_006715851.1. XM_006715788.1.
UniGeneHs.654838.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GO4X-ray2.05E/F/G/H485-584[»]
4DZOX-ray1.76A/B597-718[»]
ProteinModelPortalQ9Y6D9.
SMRQ9Y6D9. Positions 485-584, 598-716.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113971. 30 interactions.
DIPDIP-29654N.
IntActQ9Y6D9. 20 interactions.
MINTMINT-1435591.
STRING9606.ENSP00000382562.

PTM databases

PhosphoSiteQ9Y6D9.

Polymorphism databases

DMDM52783153.

Proteomic databases

MaxQBQ9Y6D9.
PaxDbQ9Y6D9.
PeptideAtlasQ9Y6D9.
PRIDEQ9Y6D9.

Protocols and materials databases

DNASU8379.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265854; ENSP00000265854; ENSG00000002822.
ENST00000399654; ENSP00000382562; ENSG00000002822.
ENST00000406869; ENSP00000385334; ENSG00000002822.
GeneID8379.
KEGGhsa:8379.
UCSCuc003sle.1. human.

Organism-specific databases

CTD8379.
GeneCardsGC07M001855.
HGNCHGNC:6762. MAD1L1.
HPACAB015338.
HPA003635.
MIM602686. gene.
neXtProtNX_Q9Y6D9.
PharmGKBPA372.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275166.
HOGENOMHOG000004808.
HOVERGENHBG052441.
KOK06638.
OMAGAEEKMQ.
PhylomeDBQ9Y6D9.
TreeFamTF101083.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9Y6D9.
BgeeQ9Y6D9.
CleanExHS_MAD1L1.
GenevestigatorQ9Y6D9.

Family and domain databases

InterProIPR008672. Mad1.
[Graphical view]
PANTHERPTHR23168. PTHR23168. 1 hit.
PfamPF05557. MAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAD1L1. human.
EvolutionaryTraceQ9Y6D9.
GeneWikiMad1.
GenomeRNAi8379.
NextBio31368.
PROQ9Y6D9.
SOURCESearch...

Entry information

Entry nameMD1L1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6D9
Secondary accession number(s): Q13312 expand/collapse secondary AC list , Q75MI0, Q86UM4, Q9UNH0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM