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Protein

Hyaluronan mediated motility receptor

Gene

HMMR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cell motility. When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Hyaluronic acid

Enzyme and pathway databases

ReactomeiREACT_120996. Hyaluronan uptake and degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronan mediated motility receptor
Alternative name(s):
Intracellular hyaluronic acid-binding protein
Receptor for hyaluronan-mediated motility
CD_antigen: CD168
Gene namesi
Name:HMMR
Synonyms:IHABP, RHAMM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:5012. HMMR.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29340.

Chemistry

DrugBankiDB08818. Hyaluronan.

Polymorphism and mutation databases

BioMutaiHMMR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724Hyaluronan mediated motility receptorPRO_0000084007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine1 Publication
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO75330.
PaxDbiO75330.
PRIDEiO75330.

2D gel databases

REPRODUCTION-2DPAGEO75330.

PTM databases

PhosphoSiteiO75330.

Expressioni

Tissue specificityi

Expressed in breast cancer cell lines and in normal breast tissue.

Gene expression databases

BgeeiO75330.
CleanExiHS_HMMR.
ExpressionAtlasiO75330. baseline and differential.
GenevisibleiO75330. HS.

Organism-specific databases

HPAiCAB002433.
HPA040025.
HPA043926.

Interactioni

Subunit structurei

Subunit of the HARC complex.

Binary interactionsi

WithEntry#Exp.IntActNotes
MORN4Q8NDC43EBI-2556203,EBI-10269566

Protein-protein interaction databases

BioGridi109404. 25 interactions.
DIPiDIP-56496N.
IntActiO75330. 15 interactions.
MINTiMINT-4989385.
STRINGi9606.ENSP00000377492.

Structurei

3D structure databases

ProteinModelPortaliO75330.
SMRiO75330. Positions 645-678.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni635 – 64511Hyaluronic acid-bindingSequence AnalysisAdd
BLAST
Regioni657 – 66610Hyaluronic acid-bindingSequence Analysis

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG146600.
GeneTreeiENSGT00390000007135.
HOVERGENiHBG044411.
InParanoidiO75330.
KOiK06267.
OMAiNFALKTP.
PhylomeDBiO75330.
TreeFamiTF333963.

Family and domain databases

InterProiIPR026203. IHABP.
[Graphical view]
PANTHERiPTHR18956. PTHR18956. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75330-1) [UniParc]FASTAAdd to basket

Also known as: A

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.

« Hide

        10         20         30         40         50
MSFPKAPLKR FNDPSGCAPS PGAYDVKTLE VLKGPVSFQK SQRFKQQKES
60 70 80 90 100
KQNLNVDKDT TLPASARKVK SSESKESQKN DKDLKILEKE IRVLLQERGA
110 120 130 140 150
QDRRIQDLET ELEKMEARLN AALREKTSLS ANNATLEKQL IELTRTNELL
160 170 180 190 200
KSKFSENGNQ KNLRILSLEL MKLRNKRETK MRGMMAKQEG MEMKLQVTQR
210 220 230 240 250
SLEESQGKIA QLEGKLVSIE KEKIDEKSET EKLLEYIEEI SCASDQVEKY
260 270 280 290 300
KLDIAQLEEN LKEKNDEILS LKQSLEENIV ILSKQVEDLN VKCQLLEKEK
310 320 330 340 350
EDHVNRNREH NENLNAEMQN LKQKFILEQQ EREKLQQKEL QIDSLLQQEK
360 370 380 390 400
ELSSSLHQKL CSFQEEMVKE KNLFEEELKQ TLDELDKLQQ KEEQAERLVK
410 420 430 440 450
QLEEEAKSRA EELKLLEEKL KGKEAELEKS SAAHTQATLL LQEKYDSMVQ
460 470 480 490 500
SLEDVTAQFE SYKALTASEI EDLKLENSSL QEKAAKAGKN AEDVQHQILA
510 520 530 540 550
TESSNQEYVR MLLDLQTKSA LKETEIKEIT VSFLQKITDL QNQLKQQEED
560 570 580 590 600
FRKQLEDEEG RKAEKENTTA ELTEEINKWR LLYEELYNKT KPFQLQLDAF
610 620 630 640 650
EVEKQALLNE HGAAQEQLNK IRDSYAKLLG HQNLKQKIKH VVKLKDENSQ
660 670 680 690 700
LKSEVSKLRC QLAKKKQSET KLQEELNKVL GIKHFDPSKA FHHESKENFA
710 720
LKTPLKEGNT NCYRAPMECQ ESWK
Length:724
Mass (Da):84,100
Last modified:April 17, 2007 - v2
Checksum:iF2C3C0DBA863955F
GO
Isoform 2 (identifier: O75330-2) [UniParc]FASTAAdd to basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     76-90: Missing.

Show »
Length:709
Mass (Da):82,301
Checksum:i29E7F070B99FD30C
GO
Isoform 3 (identifier: O75330-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-75: K → KK

Show »
Length:725
Mass (Da):84,229
Checksum:i2515512EEDFB1DA1
GO
Isoform 4 (identifier: O75330-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: MSFPKAPLKR...DKDLKILEKE → MTLL

Show »
Length:638
Mass (Da):74,495
Checksum:iBFD153D3EC20FE5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031R → S in AAC32548 (PubMed:9601098).Curated
Sequence conflicti277 – 2771E → D in AAC52049 (PubMed:8890751).Curated
Sequence conflicti298 – 2981K → T in AAC52049 (PubMed:8890751).Curated
Sequence conflicti322 – 3221K → E in AAC52049 (PubMed:8890751).Curated
Sequence conflicti330 – 3323QER → REH in AAC52049 (PubMed:8890751).Curated
Sequence conflicti547 – 5471Q → R in BAF83266 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921R → C.1 Publication
Corresponds to variant rs299284 [ dbSNP | Ensembl ].
VAR_024155
Natural varianti305 – 3051N → K.
Corresponds to variant rs2303077 [ dbSNP | Ensembl ].
VAR_031661
Natural varianti320 – 3201N → K.
Corresponds to variant rs2303077 [ dbSNP | Ensembl ].
VAR_056917
Natural varianti332 – 3321R → H.
Corresponds to variant rs2303078 [ dbSNP | Ensembl ].
VAR_024156
Natural varianti368 – 3681V → A.2 Publications
Corresponds to variant rs299290 [ dbSNP | Ensembl ].
VAR_020044
Natural varianti484 – 4841A → V.2 Publications
Corresponds to variant rs299295 [ dbSNP | Ensembl ].
VAR_024157
Natural varianti557 – 5571D → H.
Corresponds to variant rs2230362 [ dbSNP | Ensembl ].
VAR_056918
Natural varianti595 – 5951L → I.
Corresponds to variant rs2230363 [ dbSNP | Ensembl ].
VAR_056919

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9090MSFPK…ILEKE → MTLL in isoform 4. 1 PublicationVSP_041266Add
BLAST
Alternative sequencei75 – 751K → KK in isoform 3. 2 PublicationsVSP_038378
Alternative sequencei76 – 9015Missing in isoform 2. 1 PublicationVSP_004286Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29343 mRNA. Translation: AAC52049.1.
AF032862 mRNA. Translation: AAC32548.1.
AK290577 mRNA. Translation: BAF83266.1.
AK303616 mRNA. Translation: BAG64626.1.
AC112205 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61522.1.
CH471062 Genomic DNA. Translation: EAW61523.1.
CH471062 Genomic DNA. Translation: EAW61524.1.
CH471062 Genomic DNA. Translation: EAW61525.1.
BC108904 mRNA. Translation: AAI08905.1.
CCDSiCCDS4362.1. [O75330-1]
CCDS4363.1. [O75330-2]
CCDS47334.1. [O75330-3]
CCDS47335.1. [O75330-4]
PIRiJC5016.
RefSeqiNP_001136028.1. NM_001142556.1. [O75330-3]
NP_001136029.1. NM_001142557.1. [O75330-4]
NP_036616.2. NM_012484.2. [O75330-1]
NP_036617.2. NM_012485.2. [O75330-2]
UniGeneiHs.740467.

Genome annotation databases

EnsembliENST00000353866; ENSP00000185942; ENSG00000072571. [O75330-2]
ENST00000358715; ENSP00000351554; ENSG00000072571. [O75330-1]
ENST00000393915; ENSP00000377492; ENSG00000072571. [O75330-3]
ENST00000432118; ENSP00000402673; ENSG00000072571. [O75330-4]
GeneIDi3161.
KEGGihsa:3161.
UCSCiuc003lzf.3. human. [O75330-1]
uc003lzg.3. human. [O75330-2]
uc003lzh.3. human. [O75330-3]
uc011dem.2. human. [O75330-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29343 mRNA. Translation: AAC52049.1.
AF032862 mRNA. Translation: AAC32548.1.
AK290577 mRNA. Translation: BAF83266.1.
AK303616 mRNA. Translation: BAG64626.1.
AC112205 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61522.1.
CH471062 Genomic DNA. Translation: EAW61523.1.
CH471062 Genomic DNA. Translation: EAW61524.1.
CH471062 Genomic DNA. Translation: EAW61525.1.
BC108904 mRNA. Translation: AAI08905.1.
CCDSiCCDS4362.1. [O75330-1]
CCDS4363.1. [O75330-2]
CCDS47334.1. [O75330-3]
CCDS47335.1. [O75330-4]
PIRiJC5016.
RefSeqiNP_001136028.1. NM_001142556.1. [O75330-3]
NP_001136029.1. NM_001142557.1. [O75330-4]
NP_036616.2. NM_012484.2. [O75330-1]
NP_036617.2. NM_012485.2. [O75330-2]
UniGeneiHs.740467.

3D structure databases

ProteinModelPortaliO75330.
SMRiO75330. Positions 645-678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109404. 25 interactions.
DIPiDIP-56496N.
IntActiO75330. 15 interactions.
MINTiMINT-4989385.
STRINGi9606.ENSP00000377492.

Chemistry

DrugBankiDB08818. Hyaluronan.

PTM databases

PhosphoSiteiO75330.

Polymorphism and mutation databases

BioMutaiHMMR.

2D gel databases

REPRODUCTION-2DPAGEO75330.

Proteomic databases

MaxQBiO75330.
PaxDbiO75330.
PRIDEiO75330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353866; ENSP00000185942; ENSG00000072571. [O75330-2]
ENST00000358715; ENSP00000351554; ENSG00000072571. [O75330-1]
ENST00000393915; ENSP00000377492; ENSG00000072571. [O75330-3]
ENST00000432118; ENSP00000402673; ENSG00000072571. [O75330-4]
GeneIDi3161.
KEGGihsa:3161.
UCSCiuc003lzf.3. human. [O75330-1]
uc003lzg.3. human. [O75330-2]
uc003lzh.3. human. [O75330-3]
uc011dem.2. human. [O75330-4]

Organism-specific databases

CTDi3161.
GeneCardsiGC05P162887.
H-InvDBHIX0032412.
HGNCiHGNC:5012. HMMR.
HPAiCAB002433.
HPA040025.
HPA043926.
MIMi600936. gene.
neXtProtiNX_O75330.
PharmGKBiPA29340.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG146600.
GeneTreeiENSGT00390000007135.
HOVERGENiHBG044411.
InParanoidiO75330.
KOiK06267.
OMAiNFALKTP.
PhylomeDBiO75330.
TreeFamiTF333963.

Enzyme and pathway databases

ReactomeiREACT_120996. Hyaluronan uptake and degradation.

Miscellaneous databases

GeneWikiiHyaluronan-mediated_motility_receptor.
GenomeRNAii3161.
NextBioi12532.
PROiO75330.
SOURCEiSearch...

Gene expression databases

BgeeiO75330.
CleanExiHS_HMMR.
ExpressionAtlasiO75330. baseline and differential.
GenevisibleiO75330. HS.

Family and domain databases

InterProiIPR026203. IHABP.
[Graphical view]
PANTHERiPTHR18956. PTHR18956. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The characterization of a human RHAMM cDNA: conservation of the hyaluronan-binding domains."
    Wang C., Entwistle J., Hou G., Li Q., Turley E.A.
    Gene 174:299-306(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Mammary gland.
  2. "The human hyaluronan receptor RHAMM is expressed as an intracellular protein in breast cancer cells."
    Assmann V., Marshall J.F., Fieber C., Hofmann M., Hart I.R.
    J. Cell Sci. 111:1685-1694(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), CHARACTERIZATION.
    Tissue: Mammary carcinoma.
  3. "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.
    , 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 2 AND 4), VARIANTS ALA-368 AND VAL-484.
    Tissue: Thymus.
  4. "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.
    , 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].
  5. 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] (ISOFORM 3), VARIANTS CYS-92; ALA-368 AND VAL-484.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHMMR_HUMAN
AccessioniPrimary (citable) accession number: O75330
Secondary accession number(s): A8K3G2
, B4E114, D3DQK9, D3DQL0, E9PCS0, Q32N02, Q92767
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 17, 2007
Last modified: June 24, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.