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Q8TD16 (BICD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein bicaudal D homolog 2

Short name=Bic-D 2
Gene names
Name:BICD2
Synonyms:KIAA0699
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the dynein-dynactin interactions on the surface of membranous organelles, by associating with these complexes. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex By similarity.

Subunit structure

Interacts with DCTN2 and RAB6A. Interacts with NEK9. Interacts with DNAI1. Ref.1 Ref.15 Ref.16

Subcellular location

Golgi apparatus. Cytoplasmcytoskeleton. Note: In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends By similarity. Its localization is dependent on microtubule morphology.

Tissue specificity

Ubiquitous.

Domain

The fourth coiled coil region is involved in Golgi targeting and in the interaction with DCTN2 By similarity.

Post-translational modification

Phosphorylated by NEK9 in vitro. Ref.1

Involvement in disease

Spinal muscular atrophy, lower extremity-predominant 2, autosomal dominant (SMALED2) [MIM:615290]: An autosomal dominant form of spinal muscular atrophy characterized by early-childhood onset of muscle weakness and atrophy predominantly affecting the proximal and distal muscles of the lower extremity, although some patients may show upper extremity involvement. The disorder results in delayed walking, waddling gait, difficulty walking, and loss of distal reflexes. Some patients may have foot deformities or hyperlordosis, and some show mild upper motor signs, such as spasticity. Sensation, bulbar function, and cognitive function are preserved. The disorder shows very slow progression throughout life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17

Sequence similarities

Belongs to the BicD family.

Sequence caution

The sequence BAA31674.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TD16-1)

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: Q8TD16-2)

The sequence of this isoform differs from the canonical sequence as follows:
     824-824: L → VSHTCACASDRAEGTGLANQVFCSEKHSIYCD
Note: Due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 824823Protein bicaudal D homolog 2
PRO_0000205359

Regions

Region663 – 803141Interacts with RAB6A By similarity
Coiled coil20 – 269250 Potential
Coiled coil338 – 537200 Potential
Coiled coil666 – 808143 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.9 Ref.14
Modified residue1901Phosphoserine Ref.7 Ref.8
Modified residue2241Phosphoserine Ref.7
Modified residue3431Phosphoserine Ref.7
Modified residue3951Phosphoserine Ref.7
Modified residue5821Phosphoserine Ref.5 Ref.6 Ref.7 Ref.11 Ref.13
Modified residue8211Phosphothreonine Ref.8
Modified residue8231Phosphoserine Ref.8

Natural variations

Alternative sequence8241L → VSHTCACASDRAEGTGLANQ VFCSEKHSIYCD in isoform 2.
VSP_007969
Natural variant901K → R. Ref.17
Corresponds to variant rs61754130 [ dbSNP | Ensembl ].
VAR_070111
Natural variant1071S → L in SMALED2; causes Golgi fragmentation; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein. Ref.15 Ref.16 Ref.17
VAR_070112
Natural variant1881N → T in SMALED2; causes Golgi fragmentation. Ref.17
VAR_070113
Natural variant1891I → F in SMALED2. Ref.16
VAR_070114
Natural variant5011R → P in SMALED2; the mutation causes increased interaction with dynein; the mutant protein accumulates abnormally in the perinuclear region where it forms ring-like structures that colocalize with RAB6A. Ref.16
VAR_070115
Natural variant5081K → T in SMALED2. Ref.16
VAR_070116
Natural variant7031T → M in SMALED2; causes Golgi fragmentation. Ref.17
VAR_070117
Natural variant7741E → G in SMALED2; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein. Ref.15
VAR_070118

Sequences

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

Last modified June 1, 2002. Version 1.
Checksum: 9C49138FF416378D

FASTA82493,533
        10         20         30         40         50         60 
MSAPSEEEEY ARLVMEAQPE WLRAEVKRLS HELAETTREK IQAAEYGLAV LEEKHQLKLQ 

        70         80         90        100        110        120 
FEELEVDYEA IRSEMEQLKE AFGQAHTNHK KVAADGESRE ESLIQESASK EQYYVRKVLE 

       130        140        150        160        170        180 
LQTELKQLRN VLTNTQSENE RLASVAQELK EINQNVEIQR GRLRDDIKEY KFREARLLQD 

       190        200        210        220        230        240 
YSELEEENIS LQKQVSVLRQ NQVEFEGLKH EIKRLEEETE YLNSQLEDAI RLKEISERQL 

       250        260        270        280        290        300 
EEALETLKTE REQKNSLRKE LSHYMSINDS FYTSHLHVSL DGLKFSDDAA EPNNDAEALV 

       310        320        330        340        350        360 
NGFEHGGLAK LPLDNKTSTP KKEGLAPPSP SLVSDLLSEL NISEIQKLKQ QLMQMEREKA 

       370        380        390        400        410        420 
GLLATLQDTQ KQLEHTRGSL SEQQEKVTRL TENLSALRRL QASKERQTAL DNEKDRDSHE 

       430        440        450        460        470        480 
DGDYYEVDIN GPEILACKYH VAVAEAGELR EQLKALRSTH EAREAQHAEE KGRYEAEGQA 

       490        500        510        520        530        540 
LTEKVSLLEK ASRQDRELLA RLEKELKKVS DVAGETQGSL SVAQDELVTF SEELANLYHH 

       550        560        570        580        590        600 
VCMCNNETPN RVMLDYYREG QGGAGRTSPG GRTSPEARGR RSPILLPKGL LAPEAGRADG 

       610        620        630        640        650        660 
GTGDSSPSPG SSLPSPLSDP RREPMNIYNL IAIIRDQIKH LQAAVDRTTE LSRQRIASQE 

       670        680        690        700        710        720 
LGPAVDKDKE ALMEEILKLK SLLSTKREQI TTLRTVLKAN KQTAEVALAN LKSKYENEKA 

       730        740        750        760        770        780 
MVTETMMKLR NELKALKEDA ATFSSLRAMF ATRCDEYITQ LDEMQRQLAA AEDEKKTLNS 

       790        800        810        820 
LLRMAIQQKL ALTQRLELLE LDHEQTRRGR AKAAPKTKPA TPSL 

« Hide

Isoform 2 [UniParc].

Checksum: DE52F8A0D1FCDFD8
Show »

FASTA85596,806

References

« Hide 'large scale' references
[1]"Purification, cloning, and characterization of Nek8, a novel NIMA-related kinase, and its candidate substrate Bicd2."
Holland P.M., Milne A., Garka K., Johnson R.S., Willis C., Sims J.E., Rauch C.T., Bird T.A., Virca G.D.
J. Biol. Chem. 277:16229-16240(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NEK9, PHOSPHORYLATION BY NEK9.
[2]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [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] OF 239-824 (ISOFORM 1).
Tissue: Pancreas and Skin.
[5]"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 SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[6]"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-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-190; SER-224; SER-343; SER-395 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-190; THR-821 AND SER-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Molecular defects in the motor adaptor BICD2 cause proximal spinal muscular atrophy with autosomal-dominant inheritance."
Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L., Chamova T., Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E., De Winter V., Ooms T., Timmerman V., Tournev I., Jordanova A.
Am. J. Hum. Genet. 92:955-964(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMALED2 LEU-107 AND GLY-774, CHARACTERIZATION OF VARIANTS SMALED2 LEU-107 AND GLY-774, INTERACTION WITH DNAI1 AND RAB6A.
[16]"Mutations in BICD2 cause dominant congenital spinal muscular atrophy and hereditary spastic paraplegia."
UK10K
Oates E.C., Rossor A.M., Hafezparast M., Gonzalez M., Speziani F., Macarthur D.G., Lek M., Cottenie E., Scoto M., Foley A.R., Hurles M., Houlden H., Greensmith L., Auer-Grumbach M., Pieber T.R., Strom T.M., Schule R., Herrmann D.N. expand/collapse author list , Sowden J.E., Acsadi G., Menezes M.P., Clarke N.F., Zuechner S., Muntoni F., North K.N., Reilly M.M.
Am. J. Hum. Genet. 92:965-973(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMALED2 LEU-107; PHE-189; PRO-501 AND THR-508, CHARACTERIZATION OF VARIANTS SMALED2 LEU-107 AND PRO-501, INTERACTION WITH DNAI1.
[17]"Mutations in BICD2, which encodes a golgin and important motor adaptor, cause congenital autosomal-dominant spinal muscular atrophy."
Neveling K., Martinez-Carrera L.A., Hoelker I., Heister A., Verrips A., Hosseini-Barkooie S.M., Gilissen C., Vermeer S., Pennings M., Meijer R., Te Riele M., Frijns C.J., Suchowersky O., Maclaren L., Rudnik-Schoeneborn S., Sinke R.J., Zerres K., Lowry R.B. expand/collapse author list , Lemmink H.H., Garbes L., Veltman J.A., Schelhaas H.J., Scheffer H., Wirth B.
Am. J. Hum. Genet. 92:946-954(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMALED2 LEU-107; THR-188 AND MET-703, CHARACTERIZATION OF VARIANTS SMALED2 LEU-107; THR-188 AND MET-703, VARIANT ARG-90.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY052562 mRNA. Translation: AAL12246.1.
AB014599 mRNA. Translation: BAA31674.1. Different initiation.
AL137074, AL136981 Genomic DNA. Translation: CAI14369.1.
AL137074, AL136981 Genomic DNA. Translation: CAI14370.1.
AL136981, AL137074 Genomic DNA. Translation: CAI41013.1.
AL136981, AL137074 Genomic DNA. Translation: CAI41014.1.
BC004296 mRNA. Translation: AAH04296.1.
BC073970 mRNA. Translation: AAH73970.1.
CCDSCCDS35064.1. [Q8TD16-2]
CCDS6700.1. [Q8TD16-1]
RefSeqNP_001003800.1. NM_001003800.1. [Q8TD16-2]
NP_056065.1. NM_015250.3. [Q8TD16-1]
UniGeneHs.436939.

3D structure databases

ProteinModelPortalQ8TD16.
SMRQ8TD16. Positions 716-797.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116891. 14 interactions.
DIPDIP-53426N.
IntActQ8TD16. 8 interactions.
MINTMINT-5006473.
STRING9606.ENSP00000349351.

PTM databases

PhosphoSiteQ8TD16.

Polymorphism databases

DMDM34098604.

Proteomic databases

MaxQBQ8TD16.
PaxDbQ8TD16.
PRIDEQ8TD16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356884; ENSP00000349351; ENSG00000185963. [Q8TD16-2]
ENST00000375512; ENSP00000364662; ENSG00000185963. [Q8TD16-1]
GeneID23299.
KEGGhsa:23299.
UCSCuc004aso.1. human. [Q8TD16-1]
uc004asp.1. human. [Q8TD16-2]

Organism-specific databases

CTD23299.
GeneCardsGC09M095473.
HGNCHGNC:17208. BICD2.
HPAHPA023013.
HPA024452.
MIM609797. gene.
615290. phenotype.
neXtProtNX_Q8TD16.
Orphanet363454. Autosomal dominant childhood-onset proximal spinal muscular atrophy with contractures.
PharmGKBPA134969018.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291306.
HOVERGENHBG050686.
OMARNVLTNT.
OrthoDBEOG7BZVRK.
PhylomeDBQ8TD16.
TreeFamTF323833.

Gene expression databases

BgeeQ8TD16.
CleanExHS_BICD2.
GenevestigatorQ8TD16.

Family and domain databases

InterProIPR018477. Bicaudal-D_microtubule-assoc.
[Graphical view]
PANTHERPTHR31233. PTHR31233. 1 hit.
PfamPF09730. BicD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBICD2.
GenomeRNAi23299.
NextBio45128.
PROQ8TD16.
SOURCESearch...

Entry information

Entry nameBICD2_HUMAN
AccessionPrimary (citable) accession number: Q8TD16
Secondary accession number(s): O75181 expand/collapse secondary AC list , Q5TBQ2, Q5TBQ3, Q96LH2, Q9BT84, Q9H561
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 106 of the entry and version 1 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 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 9

Human chromosome 9: entries, gene names and cross-references to MIM