Q9Y6D9 (MD1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MAD1L1
Synonyms:	MAD1, TXBP181

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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 TPR and NEK2. Ref.1 Ref.2 Ref.7 Ref.12 Ref.19
Subcellular location	Nucleus. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. 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. Co-localizes with NEK2 at the kinetochore. Ref.1 Ref.7 Ref.12
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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
Involvement in disease	Note=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 process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic anaphase Non-traceable author statement Ref.1. Source: UniProtKB mitotic cell cycle spindle assembly checkpoint Traceable author statement. Source: Reactome mitotic metaphase Non-traceable author statement Ref.1. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome mitotic telophase Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	actin 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 cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA spindle Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.19Ref.7Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAD2L1	Q13257	4	EBI-742610,EBI-78203
MAX	P61244	2	EBI-742610,EBI-878388

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 718

718

Mitotic spindle assembly checkpoint protein MAD1

PRO_0000213800

Regions

Region

380 – 532

153

Necessary for interaction with NEK2

Coiled coil

46 – 632

587

Potential

Amino acid modifications

Modified residue

16

1

Phosphoserine Ref.15

Modified residue

61

1

N6-acetyllysine Ref.17

Modified residue

214

1

Phosphoserine Ref.11

Modified residue

428

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16

Natural variations

Natural variant

29

1

S → L in a lymphoid cancer cell line; somatic mutation. Ref.22

VAR_019707

Natural variant

59

1

R → C in a prostate cancer cell line; somatic mutation. Ref.22
Corresponds to variant rs28939694 [ dbSNP | Ensembl ].

VAR_019708

Natural variant

160

1

N → S. Ref.21

VAR_019709

Natural variant

299

1

T → A in lung cancer cell line; somatic mutation. Ref.21

VAR_019710

Natural variant

360

1

R → Q in a prostate cancer cell line; somatic mutation. Ref.22

VAR_019711

Natural variant

500

1

T → M. Ref.21 Ref.22

VAR_019712

Natural variant

511

1

E → K. Ref.21

VAR_019713

Natural variant

516

1

E → K in a breast cancer cell line; somatic mutation. Ref.22

VAR_019714

Natural variant

556

1

R → C in a prostate cancer cell line; somatic mutation. Ref.22

VAR_019715

Natural variant

556

1

R → H in one individual with lung cancer. Ref.21

VAR_019716

Natural variant

558

1

R → H in a cancer cell line. Ref.20 Ref.21 Ref.22
Corresponds to variant rs1801368 [ dbSNP | Ensembl ].

VAR_019717

Natural variant

569

1

E → K in a breast cancer cell line; somatic mutation. Ref.22

VAR_019718

Natural variant

572

1

R → H in a cancer cell line. Ref.20
Corresponds to variant rs1801500 [ dbSNP | Ensembl ].

VAR_019719

Experimental info

Sequence conflict

189 – 190

2

EL → DV in AAC52059. Ref.1

Sequence conflict

189 – 190

2

EL → DV in AAD24498. Ref.3

Sequence conflict

260

1

K → E in AAC52059. Ref.1

Sequence conflict

260

1

K → E in AAD24498. Ref.3

Sequence conflict

268

1

Missing in AAC52059. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

718

Helix Strand Turn

Details...

Helix

487 – 492

6

Helix

494 – 528

35

Turn

537 – 539

3

Beta strand

540 – 547

8

Helix

549 – 575

27

Turn

580 – 582

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6D9 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: DA65529856A37EE3	FASTA	718	83,067
	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

References

	« Hide 'large scale' referencesShow '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: 9546394] [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: 10198256] [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: 10049595] [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. , 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: 12853948] [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: 15489334] [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: 12837246] [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: 14978040] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK2.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[11]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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: 18981471] [Abstract] Cited for: INTERACTION WITH TPR AND MAD2L1, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-428, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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: 12006501] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 493-579 IN COMPLEX WITH MAD2L1, COMPETITIVE INHIBITOR OF MAD2L1-CDC20 INTERACTION.
[20]	"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: 10366450] [Abstract] Cited for: VARIANTS HIS-558 AND HIS-572.
[21]	"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: 10597320] [Abstract] Cited for: VARIANT LUNG CANCER ALA-299, VARIANTS SER-160; MET-500; LYS-511; HIS-556 AND HIS-558.
[22]	"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: 11423979] [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.

IPI

IPI00940535.

RefSeq

NP_001013858.1. NM_001013836.1.
NP_001013859.1. NM_001013837.1.
NP_003541.2. NM_003550.2.

UniGene

Hs.654838.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GO4	X-ray	2.05	E/F/G/H	485-584	[»]

ProteinModelPortal

Q9Y6D9.

SMR

Q9Y6D9. Positions 485-584.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29654N.

IntAct

Q9Y6D9. 16 interactions.

MINT

MINT-1435591.

STRING

Q9Y6D9.

PTM databases

PhosphoSite

Q9Y6D9.

Polymorphism databases

DMDM

52783153.

Proteomic databases

PeptideAtlas

Q9Y6D9.

PRIDE

Q9Y6D9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399654; ENSP00000382562; ENSG00000002822.
ENST00000406869; ENSP00000385334; ENSG00000002822.
ENST00000455868; ENSP00000407197; ENSG00000002822.

GeneID

8379.

KEGG

hsa:8379.

UCSC

uc003slf.1. human.

Organism-specific databases

CTD

8379.

GeneCards

GC07M001855.

H-InvDB

HIX0006424.

HGNC

HGNC:6762. MAD1L1.

HPA

CAB015338.
HPA003635.

MIM

602686. gene.

neXtProt

NX_Q9Y6D9.

PharmGKB

PA372.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000001316.

HOVERGEN

HBG052441.

OrthoDB

EOG4KWJSG.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

Q9Y6D9.

Bgee

Q9Y6D9.

CleanEx

HS_MAD1L1.

Genevestigator

Q9Y6D9.

GermOnline

ENSG00000002822. Homo sapiens.

Family and domain databases

InterPro

IPR008672. MAD.
[Graphical view]

KO

K06638.

Pfam

PF05557. MAD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

31368.

SOURCE

Search...

Entry information

Entry name

MD1L1_HUMAN

Accession

Primary (citable) accession number: Q9Y6D9
Secondary accession number(s): Q13312 , Q75MI0, Q86UM4, Q9UNH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	September 27, 2004
Last modified:	January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.