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Q96CW1 (AP2M1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
AP-2 complex subunit mu
Alternative name(s):
AP-2 mu chain
Adapter-related protein complex 2 subunit mu
Adaptin-mu2
Adaptor protein complex AP-2 subunit mu
Clathrin assembly protein complex 2 mu medium chain
Clathrin coat assembly protein AP50
Clathrin coat-associated protein AP50
HA2 50 kDa subunit
Plasma membrane adaptor AP-2 50 kDa protein
Gene names
Name:AP2M1
Synonyms:CLAPM1, KIAA0109
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 By similarity. Plays a role in endocytosis of frizzled family members upon Wnt signaling By similarity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Subunit structure

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts with ATP6V1H and MEGF10. Interacts with EGFR. Interacts with F2R. Interacts with PIP5K1C; tyrosine phosphorylation of PIP5K1C weakens the interaction By similarity. Interacts with KIAA0319; required for clathrin-mediated endocytosis of KIAA0319. Interacts with DVL2 (via DEP domain) By similarity. Ref.7 Ref.13 Ref.14 Ref.17

Subcellular location

Cell membrane. Membranecoated pit; Peripheral membrane protein; Cytoplasmic side. Note: AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV By similarity.

Sequence similarities

Belongs to the adaptor complexes medium subunit family.

Contains 1 MHD (mu homology) domain.

Sequence caution

The sequence BAA09762.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processEndocytosis
Protein transport
Transport
   Cellular componentCell membrane
Coated pit
Membrane
   Coding sequence diversityAlternative splicing
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

membrane organization

Traceable author statement. Source: Reactome

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentclathrin adaptor complex

Inferred from electronic annotation. Source: InterPro

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lysosomal membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

transporter activity

Traceable author statement PubMed 7989329PubMed 8595912. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279584EBI-297683,EBI-6377335From a different organism.
EGFRP005334EBI-297683,EBI-297353

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96CW1-1)

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: Q96CW1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     141-142: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435AP-2 complex subunit mu
PRO_0000193774

Regions

Domain170 – 434265MHD

Sites

Binding site3411Phosphatidylinositol lipid headgroup By similarity
Binding site3431Phosphatidylinositol lipid headgroup By similarity
Binding site3451Phosphatidylinositol lipid headgroup By similarity
Binding site3541Phosphatidylinositol lipid headgroup By similarity
Binding site3561Phosphatidylinositol lipid headgroup By similarity

Amino acid modifications

Modified residue451Phosphoserine Ref.16
Modified residue1561Phosphothreonine Ref.16

Natural variations

Alternative sequence141 – 1422Missing in isoform 2.
VSP_034599

Experimental info

Sequence conflict1061V → L in AAA93254. Ref.1

Secondary structure

................................... 435
Helix Strand Turn

Details...

Sequences

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

Last modified August 16, 2004. Version 2.
Checksum: 82803219BA279954

FASTA43549,655
        10         20         30         40         50         60 
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR 

        70         80         90        100        110        120 
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN IKNNFVLIYE LLDEILDFGY 

       130        140        150        160        170        180 
PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES 

       190        200        210        220        230        240 
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS 

       250        260        270        280        290        300 
IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK 

       310        320        330        340        350        360 
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG 

       370        380        390        400        410        420 
MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK 

       430 
WVRYIGRSGI YETRC 

« Hide

Isoform 2 [UniParc].

Checksum: 76399E78B0AC7E8A
Show »

FASTA43349,389

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of the cDNA for human 50 kDa subunit of the clathrin assembly complex AP-2 (AP50)."
Tsui S.K.W., Waye M.M.Y., Liew C.C., Fung K., Lee C.Y.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart.
[2]"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Kidney, Placenta and Skin.
[7]"Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery."
Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T., Peterlin B.M.
J. Biol. Chem. 277:28521-28529(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATP6V1H.
[8]"Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network."
Nakatsu F., Ohno H.
Cell Struct. Funct. 28:419-429(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[9]"Clathrin-mediated endocytosis in AP-2-depleted cells."
Motley A., Bright N.A., Seaman M.N.J., Robinson M.S.
J. Cell Biol. 162:909-918(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[10]"Endocytosis of the viral chemokine receptor US28 does not require beta-arrestins but is dependent on the clathrin-mediated pathway."
Fraile-Ramos A., Kohout T.A., Waldhoer M., Marsh M.
Traffic 4:243-253(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[11]"Adaptors for clathrin coats: structure and function."
Owen D.J., Collins B.M., Evans P.R.
Annu. Rev. Cell Dev. Biol. 20:153-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[12]"Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference."
Huang F., Khvorova A., Marshall W., Sorkin A.
J. Biol. Chem. 279:16657-16661(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[13]"Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization."
Paing M.M., Johnston C.A., Siderovski D.P., Trejo J.
Mol. Cell. Biol. 26:3231-3242(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH F2R.
[14]"MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation."
Suzuki E., Nakayama M.
Exp. Cell Res. 313:3729-3742(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEGF10.
[15]"The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway."
Lau A.W., Chou M.M.
J. Cell Sci. 121:4008-4017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
[16]"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-45 AND THR-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"The dyslexia-associated protein KIAA0319 interacts with adaptor protein 2 and follows the classical clathrin-mediated endocytosis pathway."
Levecque C., Velayos-Baeza A., Holloway Z.G., Monaco A.P.
Am. J. Physiol. 297:C160-C168(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIAA0319.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Study of the interaction of the medium chain mu 2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T-lymphocyte antigen 4 and CD28."
Follows E.R., McPheat J.C., Minshull C., Moore N.C., Pauptit R.A., Rowsell S., Stacey C.L., Stanway J.J., Taylor I.W.F., Abbott W.M.
Biochem. J. 359:427-434(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 167-435 IN COMPLEX WITH CTLA4 INTERNALIZATION SIGNAL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36188 mRNA. Translation: AAA93254.1.
D63475 mRNA. Translation: BAA09762.2. Different initiation.
BT007308 mRNA. Translation: AAP35972.1.
AC131235 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78290.1.
CH471052 Genomic DNA. Translation: EAW78291.1.
BC004996 mRNA. Translation: AAH04996.1.
BC013796 mRNA. Translation: AAH13796.1.
BC014030 mRNA. Translation: AAH14030.1.
PIRG02088.
RefSeqNP_001020376.1. NM_001025205.1.
NP_004059.2. NM_004068.3.
UniGeneHs.518460.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6EX-ray3.60A164-435[»]
ProteinModelPortalQ96CW1.
SMRQ96CW1. Positions 1-435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107587. 118 interactions.
IntActQ96CW1. 56 interactions.
MINTMINT-140451.
STRING9606.ENSP00000292807.

PTM databases

PhosphoSiteQ96CW1.

Polymorphism databases

DMDM51316978.

Proteomic databases

PaxDbQ96CW1.
PRIDEQ96CW1.

Protocols and materials databases

DNASU1173.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292807; ENSP00000292807; ENSG00000161203. [Q96CW1-1]
ENST00000382456; ENSP00000371894; ENSG00000161203. [Q96CW1-2]
ENST00000439647; ENSP00000409081; ENSG00000161203. [Q96CW1-2]
GeneID1173.
KEGGhsa:1173.
UCSCuc003fmw.3. human. [Q96CW1-2]
uc011bqy.2. human. [Q96CW1-1]

Organism-specific databases

CTD1173.
GeneCardsGC03P183892.
HGNCHGNC:564. AP2M1.
HPAHPA036849.
MIM601024. gene.
neXtProtNX_Q96CW1.
PharmGKBPA24855.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315786.
HOGENOMHOG000173246.
HOVERGENHBG050516.
InParanoidQ96CW1.
KOK11826.
OrthoDBEOG72RMXV.
PhylomeDBQ96CW1.
TreeFamTF300722.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_6900. Immune System.
SignaLinkQ96CW1.

Gene expression databases

ArrayExpressQ96CW1.
BgeeQ96CW1.
CleanExHS_AP2M1.
GenevestigatorQ96CW1.

Family and domain databases

InterProIPR022775. AP_mu_sigma_su.
IPR001392. Clathrin_mu.
IPR008968. Clathrin_mu_C.
IPR018240. Clathrin_mu_CS.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PfamPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFPIRSF005992. Clathrin_mu. 1 hit.
PRINTSPR00314. CLATHRINADPT.
SUPFAMSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEPS00990. CLAT_ADAPTOR_M_1. 1 hit.
PS00991. CLAT_ADAPTOR_M_2. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAP2M1. human.
EvolutionaryTraceQ96CW1.
GeneWikiAP2M1.
GenomeRNAi1173.
NextBio4844.
PROQ96CW1.
SOURCESearch...

Entry information

Entry nameAP2M1_HUMAN
AccessionPrimary (citable) accession number: Q96CW1
Secondary accession number(s): A6NE12 expand/collapse secondary AC list , D3DNT1, P20172, P53679
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 119 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 chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM