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Q13561 (DCTN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynactin subunit 2
Alternative name(s):
50 kDa dynein-associated polypeptide
Dynactin complex 50 kDa subunit
Short name=DCTN-50
p50 dynamitin
Gene names
Name:DCTN2
Synonyms:DCTN50
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development.

Subunit structure

Subunit of dynactin, a multiprotein complex associated with dynein. Interacts with BICD2 and CEP135 By similarity. Interacts with DYNAP, ECM29 and MAPRE1. Ref.9 Ref.13 Ref.14

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Membrane; Peripheral membrane protein Ref.1.

Sequence similarities

Belongs to the dynactin subunit 2 family.

Sequence caution

The sequence AAO34395.1 differs from that shown. Reason: Frameshift at position 381.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

cell proliferation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from mutant phenotype Ref.1. Source: UniProtKB

mitotic spindle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614Ref.1. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

dynactin complex

Inferred from direct assay Ref.1. Source: UniProtKB

dynein complex

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

growth cone

Inferred from electronic annotation. Source: Ensembl

kinetochore

Inferred from direct assay Ref.1. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionmotor activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9Ref.14. Source: UniProtKB

spectrin binding

Inferred from direct assay PubMed 23704327. Source: MGI

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13561-1)

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.
Isoform 2 (identifier: Q13561-2)

The sequence of this isoform differs from the canonical sequence as follows:
     35-35: A → AFAQEL
Isoform 3 (identifier: Q13561-3)

The sequence of this isoform differs from the canonical sequence as follows:
     35-35: A → AEL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 401400Dynactin subunit 2
PRO_0000079821

Regions

Coiled coil99 – 13234 Potential
Coiled coil214 – 24431 Potential
Coiled coil379 – 39921 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.17
Modified residue61Phosphotyrosine Ref.10
Modified residue831Phosphoserine Ref.12
Modified residue861Phosphotyrosine By similarity

Natural variations

Alternative sequence351A → AFAQEL in isoform 2.
VSP_040485
Alternative sequence351A → AEL in isoform 3.
VSP_040486

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: C2FF01A9739337B2

FASTA40144,231
        10         20         30         40         50         60 
MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK 

        70         80         90        100        110        120 
RVGTKGLDFS DRIGKTKRTG YESGEYEMLG EGLGVKETPQ QKYQRLLHEV QELTTEVEKI 

       130        140        150        160        170        180 
KTTVKESATE EKLTPVLLAK QLAALKQQLV ASHLEKLLGP DAAINLTDPD GALAKRLLLQ 

       190        200        210        220        230        240 
LEATKNSKGG SGGKTTGTPP DSSLVTYELH SRPEQDKFSQ AAKVAELEKR LTELETAVRC 

       250        260        270        280        290        300 
DQDAQNPLSA GLQGACLMET VELLQAKVSA LDLAVLDQVE ARLQSVLGKV NEIAKHKASV 

       310        320        330        340        350        360 
EDADTQSKVH QLYETIQRWS PIASTLPELV QRLVTIKQLH EQAMQFGQLL THLDTTQQMI 

       370        380        390        400 
ANSLKDNTTL LTQVQTTMRE NLATVEGNFA SIDERMKKLG K 

« Hide

Isoform 2 [UniParc].

Checksum: 1166997A6D07479D
Show »

FASTA40644,820
Isoform 3 [UniParc].

Checksum: 864FD68AF5433E22
Show »

FASTA40344,473

References

« Hide 'large scale' references
[1]"Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis."
Echeverri C.J., Paschal B.M., Vaughan K.T., Vallee R.B.
J. Cell Biol. 132:617-633(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
[2]"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. expand/collapse author list , 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).
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., 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. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Placenta, Skin and Uterus.
[5]"Human 50 kD dynactin subunit, p50 dynamitin, isolated from HeLa cells."
Aumais J.P., Yu-Lee L.-Y.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-385 (ISOFORM 3).
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Tissue: Platelet.
[7]Bienvenut W.V., Ramsay A., Leung H.Y.
Submitted (FEB-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 6-14; 79-96; 106-119; 157-185; 231-282 AND 366-395, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[9]"The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain."
Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E.
Curr. Biol. 9:425-428(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPRE1.
[10]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ECM29.
[14]"A novel human dynactin-associated protein, dynAP, promotes activation of Akt, and ergosterol-related compounds induce dynAP-dependent apoptosis of human cancer cells."
Kunoh T., Noda T., Koseki K., Sekigawa M., Takagi M., Shin-ya K., Goshima N., Iemura S., Natsume T., Wada S., Mukai Y., Ohta S., Sasaki R., Mizukami T.
Mol. Cancer Ther. 9:2934-2942(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYNAP.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U50733 mRNA. Translation: AAC50423.1.
AK314705 mRNA. Translation: BAG37252.1.
AC022366 Genomic DNA. No translation available.
AC022506 Genomic DNA. No translation available.
BC000718 mRNA. Translation: AAH00718.1.
BC009468 mRNA. Translation: AAH09468.1.
BC014083 mRNA. Translation: AAH14083.1.
AY189155 mRNA. Translation: AAO34395.1. Frameshift.
CCDSCCDS44930.1. [Q13561-2]
CCDS58245.1. [Q13561-1]
RefSeqNP_001248341.1. NM_001261412.1. [Q13561-3]
NP_001248342.1. NM_001261413.1. [Q13561-1]
NP_006391.1. NM_006400.4. [Q13561-2]
UniGeneHs.289123.

3D structure databases

ProteinModelPortalQ13561.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115794. 52 interactions.
IntActQ13561. 24 interactions.
MINTMINT-206219.
STRING9606.ENSP00000408910.

PTM databases

PhosphoSiteQ13561.

Polymorphism databases

DMDM22096346.

2D gel databases

REPRODUCTION-2DPAGEIPI00220503.

Proteomic databases

MaxQBQ13561.
PaxDbQ13561.
PRIDEQ13561.

Protocols and materials databases

DNASU10540.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000434715; ENSP00000408910; ENSG00000175203. [Q13561-2]
ENST00000548249; ENSP00000447824; ENSG00000175203. [Q13561-1]
GeneID10540.
KEGGhsa:10540.
UCSCuc001som.2. human. [Q13561-2]
uc009zpv.2. human. [Q13561-1]

Organism-specific databases

CTD10540.
GeneCardsGC12M057924.
H-InvDBHIX0010763.
HGNCHGNC:2712. DCTN2.
HPAHPA039715.
HPA040040.
MIM607376. gene.
neXtProtNX_Q13561.
PharmGKBPA27181.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39555.
HOVERGENHBG051323.
InParanoidQ13561.
KOK10424.
OMATQQMIAN.
OrthoDBEOG7JT6WG.
PhylomeDBQ13561.
TreeFamTF105247.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_6900. Immune System.
SignaLinkQ13561.

Gene expression databases

ArrayExpressQ13561.
BgeeQ13561.
CleanExHS_DCTN2.
GenevestigatorQ13561.

Family and domain databases

InterProIPR028133. Dynamitin.
[Graphical view]
PANTHERPTHR15346:SF0. PTHR15346:SF0. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDCTN2. human.
GeneWikiDCTN2.
GenomeRNAi10540.
NextBio39989.
PMAP-CutDBQ13561.
PROQ13561.
SOURCESearch...

Entry information

Entry nameDCTN2_HUMAN
AccessionPrimary (citable) accession number: Q13561
Secondary accession number(s): B2RBK5, Q86YN2, Q9BW17
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 4 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

MIM cross-references

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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM