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P05455 (LA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 171. 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:
Lupus La protein
Alternative name(s):
La autoantigen
La ribonucleoprotein
Sjoegren syndrome type B antigen
Short name=SS-B
Gene names
Name:SSB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. Ref.2 Ref.10

Subunit structure

Interacts with DDX15. May interact with RUFY1. Ref.12 Ref.13

Subcellular location

Nucleus Probable.

Post-translational modification

Phosphorylated. The phosphorylation sites are at the C-terminal part of the protein. Ref.11

The N-terminus is blocked.

Miscellaneous

Sera from patients with systemic lupus erythematosus (SLE) often contain antibodies that react with the normal cellular La protein as if this antigen was foreign.

Sequence similarities

Contains 1 HTH La-type RNA-binding domain.

Contains 1 RRM (RNA recognition motif) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB82EBI-358037,EBI-6927928From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Lupus La protein
PRO_0000207599

Regions

Domain7 – 9993HTH La-type RNA-binding
Domain111 – 18777RRM

Amino acid modifications

Modified residue1161N6-acetyllysine Ref.20
Modified residue1281N6-acetyllysine Ref.20
Modified residue3281N6-acetyllysine Ref.20
Modified residue3411N6-acetyllysine By similarity
Modified residue3601N6-acetyllysine Ref.20
Modified residue3661Phosphoserine; by CK2 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.23

Natural variations

Natural variant481P → S.
Corresponds to variant rs17160793 [ dbSNP | Ensembl ].
VAR_034066

Experimental info

Sequence conflict541K → E in AAA36577. Ref.8

Secondary structure

..................................................... 408
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05455 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: EC153C15F9187FC4

FASTA40846,837
        10         20         30         40         50         60 
MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE IMIKFNRLNR 

        70         80         90        100        110        120 
LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV TDEYKNDVKN RSVYIKGFPT 

       130        140        150        160        170        180 
DATLDDIKEW LEDKGQVLNI QMRRTLHKAF KGSIFVVFDS IESAKKFVET PGQKYKETDL 

       190        200        210        220        230        240 
LILFKDDYFA KKNEERKQNK VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL 

       250        260        270        280        290        300 
DDQTCREDLH ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE 

       310        320        330        340        350        360 
VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS GKGKVQFQGK 

       370        380        390        400 
KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK TENGAGDQ 

« Hide

References

« Hide 'large scale' references
[1]"Ribonucleoprotein SS-B/La belongs to a protein family with consensus sequences for RNA-binding."
Chan E.K.L., Sullivan K.F., Tan E.M.
Nucleic Acids Res. 17:2233-2244(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic structure and amino acid sequence domains of the human La autoantigen."
Chambers J.C., Kenan D., Martin B.J., Keene J.D.
J. Biol. Chem. 263:18043-18051(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ROLE IN LUPUS ERYTHEMATOSUS.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Placenta and Skeletal muscle.
[8]"Characteristics and epitope mapping of a cloned human autoantigen La."
Sturgess A.D., Peterson M.G., McNeilage L.J., Whittingham S., Coppel R.S.
J. Immunol. 140:3212-3218(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-408.
[9]"Isolation and analysis of cDNA clones expressing human lupus La antigen."
Chambers J.C., Keene J.D.
Proc. Natl. Acad. Sci. U.S.A. 82:2115-2119(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-97.
[10]"Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III."
Gottlieb E., Steitz J.A.
EMBO J. 8:851-861(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes."
Fan H., Sakulich A.L., Goodier J.L., Zhang X., Qin J., Maraie R.J.
Cell 88:707-715(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-366.
[12]"The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a putative DEAH-box RNA helicase."
Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S., Van Venrooij W.J., Pruijn G.J.M.
RNA 8:1428-1443(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX15.
[13]"Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes."
Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J., van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.
Mol. Biol. Cell 15:611-624(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUFY1.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[18]"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].
[19]"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-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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-116; LYS-128; LYS-328 AND LYS-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element."
Jacks A., Babon J., Kelly G., Manolaridis I., Cary P.D., Curry S., Conte M.R.
Structure 11:833-843(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 225-334.
[25]"Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein."
Alfano C., Sanfelice D., Babon J., Kelly G., Jacks A., Curry S., Conte M.R.
Nat. Struct. Mol. Biol. 11:323-329(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-202.
[26]"Structural basis for recognition and sequestration of UUU(OH) 3' termini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen."
Teplova M., Yuan Y.R., Phan A.T., Malinina L., Ilin S., Teplov A., Patel D.J.
Mol. Cell 21:75-85(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-194.
[27]"Structural analysis reveals conformational plasticity in the recognition of RNA 3' ends by the human La protein."
Kotik-Kogan O., Valentine E.R., Sanfelice D., Conte M.R., Curry S.
Structure 16:852-862(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-194.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13697 mRNA. Translation: CAA31985.1.
J04205 mRNA. Translation: AAA51885.1.
BT009862 mRNA. Translation: AAP88864.1.
AB451228 mRNA. Translation: BAG70042.1.
AC009967 Genomic DNA. Translation: AAY14868.1.
CH471058 Genomic DNA. Translation: EAX11258.1.
CH471058 Genomic DNA. Translation: EAX11259.1.
BC001289 mRNA. Translation: AAH01289.1.
BC020818 mRNA. Translation: AAH20818.1.
M20328 mRNA. Translation: AAA36577.1.
PIRA31888.
RefSeqNP_003133.1. NM_003142.4.
XP_005246868.1. XM_005246811.1.
UniGeneHs.632535.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OWXNMR-A225-334[»]
1S79NMR-A105-202[»]
1S7ANMR-A1-103[»]
1YTYX-ray2.29A/B1-194[»]
1ZH5X-ray1.85A/B1-194[»]
2VODX-ray2.10A/B4-194[»]
2VONX-ray2.10A/B4-194[»]
2VOOX-ray1.80A/B4-194[»]
2VOPX-ray2.80A4-194[»]
DisProtDP00229.
ProteinModelPortalP05455.
SMRP05455. Positions 10-188, 225-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112619. 55 interactions.
DIPDIP-29750N.
IntActP05455. 23 interactions.
MINTMINT-5002383.
STRING9606.ENSP00000260956.

Chemistry

ChEMBLCHEMBL2040701.

PTM databases

PhosphoSiteP05455.

Polymorphism databases

DMDM125985.

Proteomic databases

PaxDbP05455.
PeptideAtlasP05455.
PRIDEP05455.

Protocols and materials databases

DNASU6741.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260956; ENSP00000260956; ENSG00000138385.
ENST00000409333; ENSP00000386636; ENSG00000138385.
GeneID6741.
KEGGhsa:6741.
UCSCuc002ufk.3. human.

Organism-specific databases

CTD6741.
GeneCardsGC02P170619.
HGNCHGNC:11316. SSB.
HPACAB004643.
HPA012385.
HPA017287.
MIM109090. gene.
neXtProtNX_P05455.
PharmGKBPA36140.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5193.
HOGENOMHOG000006947.
HOVERGENHBG001407.
InParanoidP05455.
KOK11090.
OMASHGEIKW.
PhylomeDBP05455.
TreeFamTF314476.

Gene expression databases

ArrayExpressP05455.
BgeeP05455.
CleanExHS_SSB.
GenevestigatorP05455.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.30.70.330. 2 hits.
InterProIPR002344. Lupus_La.
IPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR014886. RRM_3.
IPR000504. RRM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF05383. La. 1 hit.
PF00076. RRM_1. 1 hit.
PF08777. RRM_3. 1 hit.
[Graphical view]
PRINTSPR00302. LUPUSLA.
SMARTSM00715. LA. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50961. HTH_LA. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05455.
GeneWikiSjogren_syndrome_antigen_B.
GenomeRNAi6741.
NextBio26296.
PMAP-CutDBP05455.
PROP05455.
SOURCESearch...

Entry information

Entry nameLA_HUMAN
AccessionPrimary (citable) accession number: P05455
Secondary accession number(s): Q15367, Q53XJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 171 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 2

Human chromosome 2: entries, gene names and cross-references to MIM