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Q9Y6D9

- MD1L1_HUMAN

UniProt

Q9Y6D9 - MD1L1_HUMAN

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Protein

Mitotic spindle assembly checkpoint protein MAD1

Gene

MAD1L1

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

Functioni

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.3 Publications

GO - Biological processi

  1. mitotic cell cycle Source: Reactome
  2. mitotic cell cycle checkpoint Source: UniProtKB
  3. mitotic nuclear division Source: UniProtKB-KW
  4. mitotic spindle assembly checkpoint Source: Reactome
  5. regulation of metaphase plate congression Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_491. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MAD1L1
Synonyms:MAD1, TXBP181
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:6762. MAD1L1.

Subcellular locationi

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.

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: HPA
  4. cytosol Source: Reactome
  5. kinetochore Source: UniProtKB
  6. mitotic spindle Source: UniProtKB
  7. nucleus Source: HPA
  8. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Disease mutation

Organism-specific databases

PharmGKBiPA372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Mitotic spindle assembly checkpoint protein MAD1PRO_0000213800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei61 – 611N6-acetyllysine1 Publication
Modified residuei214 – 2141Phosphoserine1 Publication
Modified residuei428 – 4281Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated; by BUB1. Become hyperphosphorylated in late S through M phases or after mitotic spindle damage.6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y6D9.
PaxDbiQ9Y6D9.
PeptideAtlasiQ9Y6D9.
PRIDEiQ9Y6D9.

PTM databases

PhosphoSiteiQ9Y6D9.

Expressioni

Tissue specificityi

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

Inductioni

Increased by p53/TP53.1 Publication

Gene expression databases

BgeeiQ9Y6D9.
CleanExiHS_MAD1L1.
ExpressionAtlasiQ9Y6D9. baseline and differential.
GenevestigatoriQ9Y6D9.

Organism-specific databases

HPAiCAB015338.
HPA003635.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAD2L1Q1325711EBI-742610,EBI-78203
MAXP612442EBI-742610,EBI-751711
TPRP122702EBI-742610,EBI-1048528

Protein-protein interaction databases

BioGridi113971. 37 interactions.
DIPiDIP-29654N.
IntActiQ9Y6D9. 24 interactions.
MINTiMINT-1435591.
STRINGi9606.ENSP00000382562.

Structurei

Secondary structure

1
718
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi494 – 52835Combined sources
Turni537 – 5393Combined sources
Beta strandi540 – 5478Combined sources
Helixi549 – 57527Combined sources
Helixi599 – 63739Combined sources
Beta strandi638 – 6447Combined sources
Turni645 – 6473Combined sources
Beta strandi648 – 6536Combined sources
Beta strandi663 – 6675Combined sources
Beta strandi675 – 6784Combined sources
Helixi683 – 6853Combined sources
Helixi687 – 6937Combined sources
Helixi700 – 71516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GO4X-ray2.05E/F/G/H485-584[»]
4DZOX-ray1.76A/B597-718[»]
ProteinModelPortaliQ9Y6D9.
SMRiQ9Y6D9. Positions 485-584, 598-716.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6D9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni380 – 532153Necessary for interaction with NEK2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili46 – 632587Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the MAD1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG275166.
GeneTreeiENSGT00390000001316.
HOGENOMiHOG000004808.
HOVERGENiHBG052441.
InParanoidiQ9Y6D9.
KOiK06638.
OMAiGAEEKMQ.
PhylomeDBiQ9Y6D9.
TreeFamiTF101083.

Family and domain databases

InterProiIPR008672. Mad1.
[Graphical view]
PANTHERiPTHR23168. PTHR23168. 1 hit.
PfamiPF05557. MAD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6D9-1) [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
MEDLGENTMV LSTLRSLNNF ISQRVEGGSG LDISTSAPGS LQMQYQQSMQ
60 70 80 90 100
LEERAEQIRS KSHLIQVERE KMQMELSHKR ARVELERAAS TSARNYEREV
110 120 130 140 150
DRNQELLTRI RQLQEREAGA EEKMQEQLER NRQCQQNLDA ASKRLREKED
160 170 180 190 200
SLAQAGETIN ALKGRISELQ WSVMDQEMRV KRLESEKQEL QEQLDLQHKK
210 220 230 240 250
CQEANQKIQE LQASQEARAD HEQQIKDLEQ KLSLQEQDAA IVKNMKSELV
260 270 280 290 300
RLPRLERELK QLREESAHLR EMRETNGLLQ EELEGLQRKL GRQEKMQETL
310 320 330 340 350
VGLELENERL LAKLQSWERL DQTMGLSIRT PEDLSRFVVE LQQRELALKD
360 370 380 390 400
KNSAVTSSAR GLEKARQQLQ EELRQVSGQL LEERKKRETH EALARRLQKR
410 420 430 440 450
VLLLTKERDG MRAILGSYDS ELTPAEYSPQ LTRRMREAED MVQKVHSHSA
460 470 480 490 500
EMEAQLSQAL EELGGQKQRA DMLEMELKML KSQSSSAEQS FLFSREEADT
510 520 530 540 550
LRLKVEELEG ERSRLEEEKR MLEAQLERRA LQGDYDQSRT KVLHMSLNPT
560 570 580 590 600
SVARQRLRED HSQLQAECER LRGLLRAMER GGTVPADLEA AAASLPSSKE
610 620 630 640 650
VAELKKQVES AELKNQRLKE VFQTKIQEFR KACYTLTGYQ IDITTENQYR
660 670 680 690 700
LTSLYAEHPG DCLIFKATSP SGSKMQLLET EFSHTVGELI EVHLRRQDSI
710
PAFLSSLTLE LFSRQTVA
Length:718
Mass (Da):83,067
Last modified:September 27, 2004 - v2
Checksum:iDA65529856A37EE3
GO
Isoform 2 (identifier: Q9Y6D9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MEDLGENTMV...EQIRSKSHLI → MLPARGCVRK...PCIWPCPWHT
     66-157: Missing.

Note: No experimental confirmation available.

Show »
Length:626
Mass (Da):72,286
Checksum:iC0506A8710806387
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1902EL → DV in AAC52059. (PubMed:9546394)Curated
Sequence conflicti189 – 1902EL → DV in AAD24498. (PubMed:10049595)Curated
Sequence conflicti260 – 2601K → E in AAC52059. (PubMed:9546394)Curated
Sequence conflicti260 – 2601K → E in AAD24498. (PubMed:10049595)Curated
Sequence conflicti268 – 2681Missing in AAC52059. (PubMed:9546394)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291S → L in a lymphoid cancer cell line; somatic mutation. 1 Publication
VAR_019707
Natural varianti59 – 591R → C in a prostate cancer cell line; somatic mutation. 1 Publication
Corresponds to variant rs28939694 [ dbSNP | Ensembl ].
VAR_019708
Natural varianti160 – 1601N → S.1 Publication
VAR_019709
Natural varianti299 – 2991T → A in lung cancer cell line; somatic mutation. 1 Publication
VAR_019710
Natural varianti360 – 3601R → Q in a prostate cancer cell line; somatic mutation. 1 Publication
VAR_019711
Natural varianti500 – 5001T → M.2 Publications
Corresponds to variant rs193231481 [ dbSNP | Ensembl ].
VAR_019712
Natural varianti511 – 5111E → K.1 Publication
VAR_019713
Natural varianti516 – 5161E → K in a breast cancer cell line; somatic mutation. 1 Publication
VAR_019714
Natural varianti556 – 5561R → C in a prostate cancer cell line; somatic mutation. 1 Publication
VAR_019715
Natural varianti556 – 5561R → H in one individual with lung cancer. 1 Publication
VAR_019716
Natural varianti558 – 5581R → H in a cancer cell line. 3 Publications
Corresponds to variant rs1801368 [ dbSNP | Ensembl ].
VAR_019717
Natural varianti569 – 5691E → K in a breast cancer cell line; somatic mutation. 1 Publication
VAR_019718
Natural varianti572 – 5721R → H in a cancer cell line. 1 Publication
Corresponds to variant rs1801500 [ dbSNP | Ensembl ].
VAR_019719

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6565MEDLG…KSHLI → MLPARGCVRKRTVWPRLARV LIVTLLTLELSYAPLPCQLS GVPYNTGDPVGRWARPCIWP CPWHT in isoform 2. 1 PublicationVSP_056160Add
BLAST
Alternative sequencei66 – 15792Missing in isoform 2. 1 PublicationVSP_056161Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33822 mRNA. Translation: AAC52059.1. Frameshift.
AF123318 mRNA. Translation: AAD20359.1.
AF083811 mRNA. Translation: AAD24498.1.
AK090959 mRNA. Translation: BAG52253.1.
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.
CCDSiCCDS43539.1. [Q9Y6D9-1]
RefSeqiNP_001013858.1. NM_001013836.1. [Q9Y6D9-1]
NP_001013859.1. NM_001013837.1. [Q9Y6D9-1]
NP_003541.2. NM_003550.2. [Q9Y6D9-1]
XP_005249933.1. XM_005249876.1. [Q9Y6D9-1]
XP_006715851.1. XM_006715788.1. [Q9Y6D9-1]
UniGeneiHs.654838.

Genome annotation databases

EnsembliENST00000265854; ENSP00000265854; ENSG00000002822. [Q9Y6D9-1]
ENST00000399654; ENSP00000382562; ENSG00000002822. [Q9Y6D9-1]
ENST00000402746; ENSP00000384155; ENSG00000002822. [Q9Y6D9-3]
ENST00000406869; ENSP00000385334; ENSG00000002822. [Q9Y6D9-1]
GeneIDi8379.
KEGGihsa:8379.
UCSCiuc003sle.1. human. [Q9Y6D9-1]

Polymorphism databases

DMDMi52783153.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33822 mRNA. Translation: AAC52059.1 . Frameshift.
AF123318 mRNA. Translation: AAD20359.1 .
AF083811 mRNA. Translation: AAD24498.1 .
AK090959 mRNA. Translation: BAG52253.1 .
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 .
CCDSi CCDS43539.1. [Q9Y6D9-1 ]
RefSeqi NP_001013858.1. NM_001013836.1. [Q9Y6D9-1 ]
NP_001013859.1. NM_001013837.1. [Q9Y6D9-1 ]
NP_003541.2. NM_003550.2. [Q9Y6D9-1 ]
XP_005249933.1. XM_005249876.1. [Q9Y6D9-1 ]
XP_006715851.1. XM_006715788.1. [Q9Y6D9-1 ]
UniGenei Hs.654838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GO4 X-ray 2.05 E/F/G/H 485-584 [» ]
4DZO X-ray 1.76 A/B 597-718 [» ]
ProteinModelPortali Q9Y6D9.
SMRi Q9Y6D9. Positions 485-584, 598-716.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113971. 37 interactions.
DIPi DIP-29654N.
IntActi Q9Y6D9. 24 interactions.
MINTi MINT-1435591.
STRINGi 9606.ENSP00000382562.

PTM databases

PhosphoSitei Q9Y6D9.

Polymorphism databases

DMDMi 52783153.

Proteomic databases

MaxQBi Q9Y6D9.
PaxDbi Q9Y6D9.
PeptideAtlasi Q9Y6D9.
PRIDEi Q9Y6D9.

Protocols and materials databases

DNASUi 8379.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265854 ; ENSP00000265854 ; ENSG00000002822 . [Q9Y6D9-1 ]
ENST00000399654 ; ENSP00000382562 ; ENSG00000002822 . [Q9Y6D9-1 ]
ENST00000402746 ; ENSP00000384155 ; ENSG00000002822 . [Q9Y6D9-3 ]
ENST00000406869 ; ENSP00000385334 ; ENSG00000002822 . [Q9Y6D9-1 ]
GeneIDi 8379.
KEGGi hsa:8379.
UCSCi uc003sle.1. human. [Q9Y6D9-1 ]

Organism-specific databases

CTDi 8379.
GeneCardsi GC07M001855.
HGNCi HGNC:6762. MAD1L1.
HPAi CAB015338.
HPA003635.
MIMi 602686. gene.
neXtProti NX_Q9Y6D9.
PharmGKBi PA372.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG275166.
GeneTreei ENSGT00390000001316.
HOGENOMi HOG000004808.
HOVERGENi HBG052441.
InParanoidi Q9Y6D9.
KOi K06638.
OMAi GAEEKMQ.
PhylomeDBi Q9Y6D9.
TreeFami TF101083.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_491. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSi MAD1L1. human.
EvolutionaryTracei Q9Y6D9.
GeneWikii Mad1.
GenomeRNAii 8379.
NextBioi 31368.
PROi Q9Y6D9.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6D9.
CleanExi HS_MAD1L1.
ExpressionAtlasi Q9Y6D9. baseline and differential.
Genevestigatori Q9Y6D9.

Family and domain databases

InterProi IPR008672. Mad1.
[Graphical view ]
PANTHERi PTHR23168. PTHR23168. 1 hit.
Pfami PF05557. MAD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), INDUCTION, FUNCTION.
  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: Amygdala.
  5. "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.
    , 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].
  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: Pancreas.
  7. "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.
  8. "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.
  9. "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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. "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.
  12. "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.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. "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.
  16. "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].
  17. "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.
  18. "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.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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].
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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.
  23. "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.
  24. "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.
  25. Cited for: VARIANTS CANCER LEU-29; CYS-59; GLN-360; LYS-516; CYS-556 AND LYS-569, VARIANTS MET-500 AND HIS-558.

Entry informationi

Entry nameiMD1L1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6D9
Secondary accession number(s): B3KR41
, Q13312, Q75MI0, Q86UM4, Q9UNH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: November 26, 2014
This is version 127 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

External Data

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