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Q9Y6M4 (KC1G3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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:
Casein kinase I isoform gamma-3

Short name=CKI-gamma 3
EC=2.7.11.1
Gene names
Name:CSNK1G3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Inhibited by triazolodiamine 1, 5-amino-3-{[4-(aminosulfonyl)phenyl]amino}-N-(2,6-difluorophenyl)-1H-1,2,4-triazole-1-carbothioamide, (S)-propane-1,2-diol, 2-({6-[(3-chlorophenyl)amino]-9-isopropyl-9H-purin-2-yl}amino)-3-methylbutan-1-ol, N2-[(1R,2S)-2-aminocyclohexyl]-N6-(3-chlorophenyl)-9-ethyl-9H-purine-2,6-diamine and [4-amino-2-(3-chloroanilino)-1,3-thiazol-5-yl](4-fluorophenyl)methanone.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Post-translational modification

Autophosphorylated By similarity.

Miscellaneous

Triazolodiamine 1 is a commercial name for 5-amino-3-([4-(aminosulfonyl)phenyl]amino)-N-(2,6-difluorophenyl)-1H-1,2,4-triazole-1-carbothioamide.

Sequence similarities

Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.

Contains 1 protein kinase domain.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6M4-1)

Also known as: 3;

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: Q9Y6M4-2)

Also known as: 3L; CSNK1G3L;

The sequence of this isoform differs from the canonical sequence as follows:
     430-430: K → NCQKVLNMW
Isoform 3 (identifier: Q9Y6M4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     363-394: Missing.
     430-430: K → NCQKVLNMW
Note: Contains a phosphoserine at position 365. Contains a phosphoserine at position 366.
Isoform 4 (identifier: Q9Y6M4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     282-282: E → EE
     363-394: Missing.
     430-430: K → NCQKVLNMW
Note: Contains a phosphoserine at position 367.
Isoform 5 (identifier: Q9Y6M4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.
     363-394: Missing.
     430-430: K → NCQKVLNMW
Note: Contains a phosphoserine at position 291.
Isoform 6 (identifier: Q9Y6M4-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-113: Missing.
     282-282: E → EE
     363-394: Missing.
     430-430: K → NCQKVLNMW
Note: Contains a phosphoserine at position 254.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Casein kinase I isoform gamma-3
PRO_0000192846

Regions

Domain43 – 313271Protein kinase
Nucleotide binding49 – 579ATP By similarity
Region117 – 1259Inhibitors binding

Sites

Active site1621Proton acceptor By similarity
Binding site721ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue4131Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 113113Missing in isoform 6.
VSP_047053
Alternative sequence1 – 7575Missing in isoform 5.
VSP_047054
Alternative sequence2821E → EE in isoform 4 and isoform 6.
VSP_047055
Alternative sequence363 – 39432Missing in isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_010256
Alternative sequence4301K → NCQKVLNMW in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_004749

Experimental info

Sequence conflict911K → E in AAH47567. Ref.5
Sequence conflict1741G → R in AAD26525. Ref.1
Sequence conflict1741G → R in AAD26526. Ref.1
Sequence conflict2411Y → C in BAH14390. Ref.2
Sequence conflict3021D → E in AAD26525. Ref.1
Sequence conflict3021D → E in AAD26526. Ref.1

Secondary structure

.................................................... 447
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (3) [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 6FAEDD605579ED3A

FASTA44751,389
        10         20         30         40         50         60 
MENKKKDKDK SDDRMARPSG RSGHNTRGTG SSSSGVLMVG PNFRVGKKIG CGNFGELRLG 

        70         80         90        100        110        120 
KNLYTNEYVA IKLEPMKSRA PQLHLEYRFY KQLGSGDGIP QVYYFGPCGK YNAMVLELLG 

       130        140        150        160        170        180 
PSLEDLFDLC DRTFSLKTVL MIAIQLISRM EYVHSKNLIY RDVKPENFLI GRPGNKTQQV 

       190        200        210        220        230        240 
IHIIDFGLAK EYIDPETKKH IPYREHKSLT GTARYMSINT HLGKEQSRRD DLEALGHMFM 

       250        260        270        280        290        300 
YFLRGSLPWQ GLKADTLKER YQKIGDTKRA TPIEVLCENF PEMATYLRYV RRLDFFEKPD 

       310        320        330        340        350        360 
YDYLRKLFTD LFDRKGYMFD YEYDWIGKQL PTPVGAVQQD PALSSNREAH QHRDKMQQSK 

       370        380        390        400        410        420 
NQSADHRAAW DSQQANPHHL RAHLAADRHG GSVQVVSSTN GELNTDDPTA GRSNAPITAP 

       430        440 
TEVEVMDETK CCCFFKRRKR KTIQRHK 

« Hide

Isoform 2 (3L) (CSNK1G3L) [UniParc].

Checksum: 23C1F32F3559120F
Show »

FASTA45552,378
Isoform 3 [UniParc].

Checksum: 786AA3787897A4C5
Show »

FASTA42348,898
Isoform 4 [UniParc].

Checksum: 0D2C64F25039E090
Show »

FASTA42449,027
Isoform 5 [UniParc].

Checksum: 5AEB20AED88A1240
Show »

FASTA34840,729
Isoform 6 [UniParc].

Checksum: 9A87163AF2FC9AFF
Show »

FASTA31136,492

References

« Hide 'large scale' references
[1]"Cloning and chromosome mapping of the human casein kinase I gamma3 gene (CSNK1G3)."
Kusuda J., Hirai M., Toyoda A., Tanuma R., Hashimoto K.
Cytogenet. Cell Genet. 83:101-103(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[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] (ISOFORMS 4; 5 AND 6).
Tissue: Astrocyte, Brain and Embryonic brain.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[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: 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-413, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 (ISOFORM 6), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Structure of casein kinase 1 gamma 3."
Bunkoczi G., Salah E., Rellos P., Das S., Fedorov O., Savitsky P., Gileadi O., Sundstrom M., Edwards A., Arrowsmith C., Ugochukwu E., Weigelt J., Von Delft F., Knapp S.
Submitted (MAR-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 35-362 IN COMPLEX WITH INHIBITORS.
[13]"Inhibitor binding by casein kinases."
Bunkoczi G., Salah E., Rellos P., Das S., Fedorov O., Savitsky P., Debreczeni J.E., Gileadi O., Sundstrom M., Edwards A., Arrowsmith C., Weigelt J., Von Delft F., Knapp S.
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 35-362 IN COMPLEX WITH INHIBITORS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF049089 mRNA. Translation: AAD26525.1.
AF049090 mRNA. Translation: AAD26526.1.
AK289405 mRNA. Translation: BAF82094.1.
AK299739 mRNA. Translation: BAG61634.1.
AK316019 mRNA. Translation: BAH14390.1.
AC008541 Genomic DNA. No translation available.
AC026422 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW48872.1.
BC047567 mRNA. Translation: AAH47567.1.
RefSeqNP_001026982.1. NM_001031812.3.
NP_001038188.1. NM_001044723.2.
NP_001257501.1. NM_001270572.1.
NP_001257502.1. NM_001270573.1.
NP_001257503.1. NM_001270574.1.
NP_004375.2. NM_004384.4.
XP_005271949.1. XM_005271892.2.
XP_005271951.1. XM_005271894.2.
XP_005271952.1. XM_005271895.1.
UniGeneHs.129206.
Hs.741716.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CHLX-ray1.95A35-362[»]
2IZRX-ray1.30A35-362[»]
2IZSX-ray1.95A35-362[»]
2IZTX-ray2.00A35-362[»]
2IZUX-ray1.85A35-362[»]
4G16X-ray2.30A34-362[»]
4G17X-ray2.10A34-362[»]
4HGLX-ray2.40A34-362[»]
4HGSX-ray2.40A34-362[»]
ProteinModelPortalQ9Y6M4.
SMRQ9Y6M4. Positions 36-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107840. 5 interactions.
STRING9606.ENSP00000353904.

Chemistry

BindingDBQ9Y6M4.
ChEMBLCHEMBL5084.
GuidetoPHARMACOLOGY2001.

PTM databases

PhosphoSiteQ9Y6M4.

Polymorphism databases

DMDM47117932.

Proteomic databases

PaxDbQ9Y6M4.
PRIDEQ9Y6M4.

Protocols and materials databases

DNASU1456.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345990; ENSP00000334735; ENSG00000151292. [Q9Y6M4-3]
ENST00000360683; ENSP00000353904; ENSG00000151292. [Q9Y6M4-2]
ENST00000361991; ENSP00000354942; ENSG00000151292. [Q9Y6M4-1]
ENST00000395411; ENSP00000378806; ENSG00000151292. [Q9Y6M4-1]
ENST00000395412; ENSP00000378807; ENSG00000151292. [Q9Y6M4-2]
ENST00000510842; ENSP00000423838; ENSG00000151292. [Q9Y6M4-4]
ENST00000511130; ENSP00000421385; ENSG00000151292. [Q9Y6M4-6]
ENST00000512718; ENSP00000421998; ENSG00000151292. [Q9Y6M4-5]
ENST00000521364; ENSP00000429412; ENSG00000151292. [Q9Y6M4-3]
GeneID1456.
KEGGhsa:1456.
UCSCuc003ktn.4. human. [Q9Y6M4-3]
uc031skv.1. human. [Q9Y6M4-2]
uc031skw.1. human. [Q9Y6M4-1]

Organism-specific databases

CTD1456.
GeneCardsGC05P122909.
HGNCHGNC:2456. CSNK1G3.
HPAHPA027010.
MIM604253. gene.
neXtProtNX_Q9Y6M4.
PharmGKBPA26956.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000182054.
HOVERGENHBG000176.
KOK08958.
OMANREAHPH.
OrthoDBEOG7G1V66.
PhylomeDBQ9Y6M4.
TreeFamTF313349.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
SignaLinkQ9Y6M4.

Gene expression databases

ArrayExpressQ9Y6M4.
BgeeQ9Y6M4.
CleanExHS_CSNK1G3.
GenevestigatorQ9Y6M4.

Family and domain databases

InterProIPR022247. Casein_kinase-1_gamma_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF12605. CK1gamma_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSNK1G3. human.
EvolutionaryTraceQ9Y6M4.
GenomeRNAi1456.
NextBio35463704.
PROQ9Y6M4.
SOURCESearch...

Entry information

Entry nameKC1G3_HUMAN
AccessionPrimary (citable) accession number: Q9Y6M4
Secondary accession number(s): A8K040 expand/collapse secondary AC list , B4DSH2, B7Z9Q4, E7EVD0, Q86WZ7, Q9Y6M3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 133 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

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 chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM