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Q68EM7 (RHG17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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:
Rho GTPase-activating protein 17
Alternative name(s):
Rho-type GTPase-activating protein 17
RhoGAP interacting with CIP4 homologs protein 1
Short name=RICH-1
Gene names
Name:ARHGAP17
Synonyms:RICH1
ORF Names:MSTP066, MSTP110
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca2+-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1. Ref.1 Ref.7

Subunit structure

Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85. Ref.1 Ref.6 Ref.7

Subcellular location

Membrane; Peripheral membrane protein. Cytoplasm. Cell junctiontight junction. Note: Associates with membranes and concentrates at sites of cell-cell contact. Ref.1 Ref.7

Tissue specificity

Ubiquitously expressed. Expressed at higher level in heart and placenta. Ref.1

Domain

The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions. Ref.7

Sequence similarities

Contains 1 BAR domain.

Contains 1 Rho-GAP domain.

Sequence caution

The sequence AAH01241.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAQ13586.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAQ13632.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q68EM7-1)

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: Q68EM7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     497-574: Missing.
Isoform 3 (identifier: Q68EM7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-273: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q68EM7-4)

Also known as: RICH1B;

The sequence of this isoform differs from the canonical sequence as follows:
     215-226: LLEAQADYHRKA → ISGRKNQPLGLP
     227-881: Missing.
Isoform 5 (identifier: Q68EM7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     839-881: DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → GFQNRIAASFLKCTQTQPAKTCLAASCWI
Note: No experimental confirmation available.
Isoform 6 (identifier: Q68EM7-6)

The sequence of this isoform differs from the canonical sequence as follows:
     840-881: SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → V
Isoform 7 (identifier: Q68EM7-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-467: Missing.
     468-496: TGNDSDSGTLERKRPASMAVMEGDLVKKE → MCGFNTCGPMGFCLSSLLAWCVDCFFSLC
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Rho GTPase-activating protein 17
PRO_0000280462

Regions

Domain14 – 246233BAR
Domain252 – 442191Rho-GAP
Motif753 – 76614SH3-binding Potential
Compositional bias521 – 816296Pro-rich

Amino acid modifications

Modified residue5751Phosphoserine Ref.8 Ref.12
Modified residue6791Phosphothreonine Ref.9

Natural variations

Alternative sequence1 – 467467Missing in isoform 7.
VSP_023682
Alternative sequence1 – 273273Missing in isoform 3.
VSP_023683
Alternative sequence215 – 22612LLEAQ…YHRKA → ISGRKNQPLGLP in isoform 4.
VSP_023684
Alternative sequence227 – 881655Missing in isoform 4.
VSP_023685
Alternative sequence468 – 49629TGNDS…LVKKE → MCGFNTCGPMGFCLSSLLAW CVDCFFSLC in isoform 7.
VSP_023686
Alternative sequence497 – 57478Missing in isoform 2.
VSP_023687
Alternative sequence839 – 88143DSNSR…ESTAL → GFQNRIAASFLKCTQTQPAK TCLAASCWI in isoform 5.
VSP_023688
Alternative sequence840 – 88142SNSRV…ESTAL → V in isoform 6.
VSP_023689

Experimental info

Mutagenesis2881R → A: Loss of function; leading to defects in tight junction maintenance. Ref.1
Sequence conflict1391K → E in BAB55203. Ref.2
Sequence conflict1671Q → R in CAC37948. Ref.1
Sequence conflict1861K → R in CAC37948. Ref.1
Sequence conflict2551E → A in BAB14506. Ref.2
Sequence conflict4041G → A in BAB55203. Ref.2
Sequence conflict5751S → C in BAC86144. Ref.2
Sequence conflict8551M → V in BAB55203. Ref.2

Sequences

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

Last modified October 11, 2004. Version 1.
Checksum: 92029DBFFEAD1001

FASTA88195,437
        10         20         30         40         50         60 
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT 

        70         80         90        100        110        120 
DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV 

       130        140        150        160        170        180 
DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM 

       190        200        210        220        230        240 
DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH 

       250        260        270        280        290        300 
QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK 

       310        320        330        340        350        360 
AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL 

       370        380        390        400        410        420 
WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA 

       430        440        450        460        470        480 
AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK 

       490        500        510        520        530        540 
RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP 

       550        560        570        580        590        600 
EPPPQSSRAE SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG 

       610        620        630        640        650        660 
QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSSGTS 

       670        680        690        700        710        720 
QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR YSSSLSPIQA PNHPPPQPPT 

       730        740        750        760        770        780 
QATPLMHTKP NSQGPPNPMA LPSEHGLEQP SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA 

       790        800        810        820        830        840 
GGNPETAQPH AGTLPRPRPV PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDS 

       850        860        870        880 
NSRVSEPHRS IFPEMHSDSA SKDVPGRILL DIDNDTESTA L 

« Hide

Isoform 2 [UniParc].

Checksum: 9F42C390ACBAFADA
Show »

FASTA80387,609
Isoform 3 [UniParc].

Checksum: 8060364C667A5535
Show »

FASTA60864,267
Isoform 4 (RICH1B) [UniParc].

Checksum: C849839D16E68AE1
Show »

FASTA22625,760
Isoform 5 [UniParc].

Checksum: B2797018F447B1FF
Show »

FASTA86793,855
Isoform 6 [UniParc].

Checksum: 333F5437A7222C79
Show »

FASTA84090,929
Isoform 7 [UniParc].

Checksum: B20A13496205E5A8
Show »

FASTA41442,512

References

« Hide 'large scale' references
[1]"Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1."
Richnau N., Aspenstroem P.
J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FNBP1 AND TRIP10, MUTAGENESIS OF ARG-288.
[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 1; 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 634-881 (ISOFORM 5).
Tissue: Placenta and Teratocarcinoma.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Brain.
[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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-881 (ISOFORM 6).
Tissue: Cervix and Eye.
[5]Liu Y.Q., Zhao B., Xu Y.Y., Wang X.Y., Liu B., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-881.
Tissue: Aorta.
[6]"Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP."
Reczek D., Bretscher A.
J. Cell Biol. 153:191-206(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC9A3R1.
[7]"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAR, INTERACTION WITH AMOT; MPP5; INADL; PARD3; CAPZA; CAPZB; CD2AP AND SH3KBP1.
[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-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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 THR-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ306731 mRNA. Translation: CAC37948.1.
AJ306732 mRNA. Translation: CAC37949.1.
AK001170 mRNA. No translation available.
AK023281 mRNA. Translation: BAB14506.1.
AK027567 mRNA. Translation: BAB55203.1.
AK125358 mRNA. Translation: BAC86144.1.
AK291691 mRNA. Translation: BAF84380.1.
AL833975 mRNA. Translation: CAD38819.1.
BC001241 mRNA. Translation: AAH01241.1. Different initiation.
BC080195 mRNA. Translation: AAH80195.1.
AF163257 mRNA. Translation: AAQ13586.1. Different initiation.
AF173885 mRNA. Translation: AAQ13632.1. Different initiation.
CCDSCCDS32408.1. [Q68EM7-2]
CCDS32409.1. [Q68EM7-1]
PIRF59433.
RefSeqNP_001006635.1. NM_001006634.2. [Q68EM7-1]
NP_060524.4. NM_018054.5. [Q68EM7-2]
XP_005255471.1. XM_005255414.1. [Q68EM7-6]
UniGeneHs.373793.

3D structure databases

ProteinModelPortalQ68EM7.
SMRQ68EM7. Positions 25-232, 246-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120424. 29 interactions.
IntActQ68EM7. 7 interactions.
MINTMINT-195688.

PTM databases

PhosphoSiteQ68EM7.

Polymorphism databases

DMDM74736331.

Proteomic databases

MaxQBQ68EM7.
PaxDbQ68EM7.
PRIDEQ68EM7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289968; ENSP00000289968; ENSG00000140750. [Q68EM7-1]
ENST00000303665; ENSP00000303130; ENSG00000140750. [Q68EM7-2]
ENST00000441763; ENSP00000406950; ENSG00000140750. [Q68EM7-4]
GeneID55114.
KEGGhsa:55114.
UCSCuc002dmy.3. human. [Q68EM7-7]
uc002dna.3. human. [Q68EM7-1]
uc002dnc.3. human. [Q68EM7-2]
uc002dng.1. human. [Q68EM7-4]

Organism-specific databases

CTD55114.
GeneCardsGC16M024931.
HGNCHGNC:18239. ARHGAP17.
HPAHPA041703.
MIM608293. gene.
neXtProtNX_Q68EM7.
PharmGKBPA134908575.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329716.
HOVERGENHBG000015.
InParanoidQ68EM7.
OMASICHHSH.
OrthoDBEOG7MKW5G.
PhylomeDBQ68EM7.
TreeFamTF350627.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ68EM7.
BgeeQ68EM7.
GenevestigatorQ68EM7.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
1.20.1270.60. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamPF03114. BAR. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00721. BAR. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
PROSITEPS51021. BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGAP17. human.
GenomeRNAi55114.
NextBio58744.
PROQ68EM7.
SOURCESearch...

Entry information

Entry nameRHG17_HUMAN
AccessionPrimary (citable) accession number: Q68EM7
Secondary accession number(s): A8K6M6 expand/collapse secondary AC list , Q6ZUS4, Q7Z2F2, Q8NDG2, Q96KS2, Q96KS3, Q96SS8, Q9BVF6, Q9H8U5, Q9NW54
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 97 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 chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM